|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
18-255 |
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: 498.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGM 97
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQI 255
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
18-230 |
5.28e-151 |
|
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: 419.24 E-value: 5.28e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGM 97
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
12-257 |
1.97e-121 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 346.40 E-value: 1.97e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 12 SATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT--------- 82
Cdd:COG4598 3 DTAPPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 83 --NDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQR 160
Cdd:COG4598 83 vpADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 161 VAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFF 240
Cdd:COG4598 163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
|
250
....*....|....*..
gi 502303547 241 DNPQHERTKLFLSQILH 257
Cdd:COG4598 243 GNPKSERLRQFLSSSLK 259
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
18-255 |
7.88e-117 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 333.98 E-value: 7.88e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGM 97
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:PRK09493 82 VFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQI 255
Cdd:PRK09493 162 EPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFLQHV 239
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
17-256 |
1.86e-96 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 282.79 E-value: 1.86e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVV-----DGTELTNDLKK-IDE 90
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditiDTARSLSQQKGlIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 91 VRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMN 170
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 171 PKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKL 250
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242
|
....*.
gi 502303547 251 FLSQIL 256
Cdd:PRK11264 243 FLEKFL 248
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
18-256 |
9.94e-94 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 275.94 E-value: 9.94e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-----------DLK 86
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 87 KIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARS 166
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 167 LCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQH 245
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|.
gi 502303547 246 ERTKLFLSQIL 256
Cdd:TIGR03005 241 ERTREFLSKVI 251
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
17-253 |
1.90e-92 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 272.27 E-value: 1.90e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTE--LTNDL--KKIDEVR 92
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQfdFSQKPseKAIRLLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSpAEFFDNPQHERTKLFL 252
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYL 240
|
.
gi 502303547 253 S 253
Cdd:COG4161 241 S 241
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
17-253 |
5.08e-91 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 268.81 E-value: 5.08e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTEL----TNDLKKIDEVR 92
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfskTPSDKAIRELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSpAEFFDNPQHERTKLFL 252
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYL 240
|
.
gi 502303547 253 S 253
Cdd:PRK11124 241 S 241
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
18-257 |
1.15e-90 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 271.18 E-value: 1.15e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY----GDFHVLRDINLKVMRGErIV-IAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTnDLKKID--E 90
Cdd:COG1135 2 IELENLSKTFptkgGPVTALDDVSLTIEKGE-IFgIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLT-ALSERElrA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 91 VRREVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMN 170
Cdd:COG1135 80 ARRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 171 PKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTK 249
Cdd:COG1135 159 PKVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTR 238
|
....*...
gi 502303547 250 LFLSQILH 257
Cdd:COG1135 239 RFLPTVLN 246
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
17-253 |
8.68e-85 |
|
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: 252.99 E-value: 8.68e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEE-----HQKGKIVVDGTELTNDLKKIDEV 91
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMNDlvpgvRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 92 RREVGMVFQHFNLFPhLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQ----ANKYPGQLSGGQQQRVAIARSL 167
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEvkdrLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 168 CMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHER 247
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELKKK-YTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*.
gi 502303547 248 TKLFLS 253
Cdd:TIGR00972 239 TEDYIS 244
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
15-233 |
1.25e-83 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 249.19 E-value: 1.25e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNKWYGD----FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKID 89
Cdd:COG1136 2 SPLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 90 EVRRE-VGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLC 168
Cdd:COG1136 82 RLRRRhIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 169 MNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQvANRVIFMDQGQIVEQ 233
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
14-256 |
1.75e-83 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 250.27 E-value: 1.75e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 14 TEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT----------- 82
Cdd:PRK10619 2 SENKLNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 83 NDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQAN-KYPGQLSGGQQQRV 161
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 162 AIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
|
250
....*....|....*
gi 502303547 242 NPQHERTKLFLSQIL 256
Cdd:PRK10619 242 NPQSPRLQQFLKGSL 256
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
13-252 |
1.06e-82 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 247.59 E-value: 1.06e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 13 ATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEV 91
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 92 RREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPqHERTKL 250
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQ 239
|
..
gi 502303547 251 FL 252
Cdd:COG1127 240 FL 241
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
18-244 |
4.13e-82 |
|
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: 245.57 E-value: 4.13e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGD----FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTnDLKKID--EV 91
Cdd:cd03258 2 IELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLT-LLSGKElrKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 92 RREVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-255 |
1.78e-80 |
|
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: 250.59 E-value: 1.78e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 2 AEAPAKKLTVSATEVAVEIVNMNKWY-----GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVV 76
Cdd:COG1123 245 AARGRAAPAAAAAEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILF 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 77 DGTELTN-DLKKIDEVRREVGMVFQH-FN-LFPHLTILEncTLA-PIWVRK-MPKKQAEEVAMHFLKRVKIPEQ-ANKYP 150
Cdd:COG1123 325 DGKDLTKlSRRSLRELRRRVQMVFQDpYSsLNPRMTVGD--IIAePLRLHGlLSRAERRERVAELLERVGLPPDlADRYP 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 151 GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQ 229
Cdd:COG1123 403 HELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250 260
....*....|....*....|....*.
gi 502303547 230 IVEQNSPAEFFDNPQHERTKLFLSQI 255
Cdd:COG1123 483 IVEDGPTEEVFANPQHPYTRALLAAV 508
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
18-230 |
1.59e-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: 238.54 E-value: 1.59e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGD----FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVR 92
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 RE-VGMVFQHFNLFPHLTILENCTLAPIwVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQvANRVIFMDQGQI 230
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
17-239 |
4.41e-79 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 238.42 E-value: 4.41e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWY-GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT-NDLKKIDEVRRE 94
Cdd:COG3638 2 MLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 VGMVFQHFNLFPHLTILEN--------CTLAPIWVRKMPKKQAEEvAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARS 166
Cdd:COG3638 82 IGMIFQQFNLVPRLSVLTNvlagrlgrTSTWRSLLGLFPPEDRER-ALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 167 LCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEF 239
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
18-257 |
9.34e-79 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 240.86 E-value: 9.34e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY----GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVR 92
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLF 251
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
....*.
gi 502303547 252 LSQILH 257
Cdd:PRK11153 241 IQSTLH 246
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
14-244 |
2.14e-76 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 235.38 E-value: 2.14e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 14 TEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlkkideV-- 91
Cdd:COG3842 2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTG-------Lpp 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 92 -RREVGMVFQHFNLFPHLTILENctLA-PIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCM 169
Cdd:COG3842 75 eKRNVGMVFQDYALFPHLTVAEN--VAfGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 170 NPKIMLFDEPTSALDP----EMIKEVLDTmvgLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:COG3842 153 EPRVLLLDEPLSALDAklreEMREELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPA 228
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
18-229 |
2.84e-76 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 229.00 E-value: 2.84e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGM 97
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLApiwvrkmpkkqaeevamhflkrvkipeqankypgqLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQ 229
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
28-244 |
3.94e-76 |
|
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: 230.30 E-value: 3.94e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQhfN---- 103
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK--KNLRELRRKVGLVFQ--Npddq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 104 LFpHLTILENCTLAPIwVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:COG1122 88 LF-APTVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 184 DPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:COG1122 166 DPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
19-239 |
2.27e-75 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 228.99 E-value: 2.27e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGD-FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTND-LKKIDEVRREVG 96
Cdd:cd03256 2 EVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkGKALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHLTILENCTLA-----PIW--VRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCM 169
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGrlgrrSTWrsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 170 NPKIMLFDEPTSALDPEMIKEVLDTMVGLA-EEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEF 239
Cdd:cd03256 162 QPKLILADEPVASLDPASSRQVMDLLKRINrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
18-232 |
2.88e-75 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 227.79 E-value: 2.88e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlkkIDEVRREVGM 97
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG----VPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENctLA-PIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:cd03259 77 VFQDYALFPHLTVAEN--IAfGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 177 DEPTSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:cd03259 155 DEPLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQ 211
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
18-244 |
1.10e-73 |
|
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: 224.30 E-value: 1.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTnDLKKID--EVRREV 95
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIS-GLSEAElyRLRRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLTILENCTLapiWVR---KMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVAF---PLRehtRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFF--DNPQ 244
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPL 231
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
12-232 |
3.76e-73 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 223.81 E-value: 3.76e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 12 SATEVAVEIVNMNKWY----GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlKK 87
Cdd:COG1116 2 SAAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-------KP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 88 IDEVRREVGMVFQHFNLFPHLTILENCTLAPIwVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSL 167
Cdd:COG1116 75 VTGPGPDRGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 168 CMNPKIMLFDEPTSALDP----EMIKEVLDTmvgLAEEGMTMLCVTHEMGFARQVANRVIFMDQ--GQIVE 232
Cdd:COG1116 154 ANDPEVLLMDEPFGALDAltreRLQDELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
18-244 |
5.47e-73 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 226.57 E-value: 5.47e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKkideVR-REVG 96
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLP----PReRRVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHLTILEN--CTLApiwVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:COG1118 79 FVFQHYALFPHMTVAENiaFGLR---VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 175 LFDEPTSALD----PEMIKEVLDTmvgLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:COG1118 156 LLDEPFGALDakvrKELRRWLRRL---HDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPA 226
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
10-253 |
5.53e-73 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 223.38 E-value: 5.53e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 10 TVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ-----KGKIVVDGTELTNd 84
Cdd:COG1117 4 PASTLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDLIpgarvEGEILLDGEDIYD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 85 lKKID--EVRREVGMVFQHFNLFPHlTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQA----NKYPGQLSGGQQ 158
Cdd:COG1117 83 -PDVDvvELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALWDEVkdrlKKSALGLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 159 QRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG1117 161 QRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQ 239
|
250
....*....|....*
gi 502303547 239 FFDNPQHERTKLFLS 253
Cdd:COG1117 240 IFTNPKDKRTEDYIT 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
18-239 |
2.77e-72 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 220.71 E-value: 2.77e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKkidEVRREVGM 97
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA---EVRRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEF 239
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
18-234 |
9.08e-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: 219.30 E-value: 9.08e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY----GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRR 93
Cdd:cd03257 2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 94 -EVGMVFQH----FNlfPHLTILEncTLA-PIWVRKMPKKQAEEVAMHFLKRVKIP---EQANKYPGQLSGGQQQRVAIA 164
Cdd:cd03257 82 kEIQMVFQDpmssLN--PRMTIGE--QIAePLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 165 RSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQN 234
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
18-239 |
1.01e-71 |
|
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: 218.97 E-value: 1.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQK-----GKIVVDGTELTNDLKKIDEVR 92
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPgapdeGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQHFNLFPhLTILENCTLAPiWVRKM-PKKQAEEVAMHFLKRVKIPEQANK--YPGQLSGGQQQRVAIARSLCM 169
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGIkLKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 170 NPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEF 239
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
17-252 |
1.69e-71 |
|
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: 219.29 E-value: 1.69e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYG----DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKidEVR 92
Cdd:COG1124 1 MLEVRNLSVSYGqggrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK--AFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQH----FNlfPHLTILEncTLA-PIWVRKMPKKQAEEVAMhfLKRVKIPEQ-ANKYPGQLSGGQQQRVAIARS 166
Cdd:COG1124 79 RRVQMVFQDpyasLH--PRHTVDR--ILAePLRIHGLPDREERIAEL--LEQVGLPPSfLDRYPHQLSGGQRQRVAIARA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 167 LCMNPKIMLFDEPTSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQH 245
Cdd:COG1124 153 LILEPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKH 232
|
....*..
gi 502303547 246 ERTKLFL 252
Cdd:COG1124 233 PYTRELL 239
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
18-241 |
6.70e-71 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 217.55 E-value: 6.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYG-DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRREV 95
Cdd:TIGR02315 2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLTILENCTLA--------PIWVRKMPKKQAEEvAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSL 167
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGrlgykptwRSLLGRFSEEDKER-ALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 168 CMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD 235
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
33-246 |
1.41e-69 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 215.20 E-value: 1.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRRE-VGMVFQHFNLFPHLTI 110
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRKkISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKE 190
Cdd:cd03294 120 LENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 191 VLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHE 246
Cdd:cd03294 199 MQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPAND 255
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
17-245 |
7.89e-68 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 213.40 E-value: 7.89e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlkkIDEVRREVG 96
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTD----LPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHLTILENctLA-PIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:COG3839 79 MVFQSYALYPHMTVYEN--IAfPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 176 FDEPTSALDP----EM---IKEVldtmvgLAEEGMTMLCVTHEmgfarQV-----ANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:COG3839 157 LDEPLSNLDAklrvEMraeIKRL------HRRLGTTTIYVTHD-----QVeamtlADRIAVMNDGRIQQVGTPEELYDRP 225
|
..
gi 502303547 244 QH 245
Cdd:COG3839 226 AN 227
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
18-233 |
1.16e-67 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 208.48 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGD----FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlKKIDEVRR 93
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-------EPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 94 EVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 174 MLFDEPTSALDpEMIKEVL-DTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQ--GQIVEQ 233
Cdd:cd03293 153 LLLDEPFSALD-ALTREQLqEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
18-232 |
3.77e-66 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 204.90 E-value: 3.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY-GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtNDLK--KIDEVRRE 94
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDL-SRLKrrEIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 VGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
18-254 |
3.77e-66 |
|
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: 205.61 E-value: 3.77e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFH-VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKIDEV--RRE 94
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGE----DIREQDPVelRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 VGMVFQHFNLFPHLTILENCTLAPIwVRKMPKKQAEEVAMHFLKRVKIPEQ--ANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:cd03295 77 IGYVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLF 251
Cdd:cd03295 156 LLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEF 235
|
...
gi 502303547 252 LSQ 254
Cdd:cd03295 236 VGA 238
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
18-253 |
2.07e-65 |
|
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: 206.06 E-value: 2.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY----GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ---KGKIVVDGTELTN-DLKKID 89
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKlSEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 90 EVR-REVGMVFQH----FNlfPHLTILEncTLA-PIWV-RKMPKKQAEEVAMHFLKRVKIP---EQANKYPGQLSGGQQQ 159
Cdd:COG0444 82 KIRgREIQMIFQDpmtsLN--PVMTVGD--QIAePLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 160 RVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG0444 158 RVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEE 237
|
250
....*....|....*
gi 502303547 239 FFDNPQHERTKLFLS 253
Cdd:COG0444 238 LFENPRHPYTRALLS 252
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
33-243 |
3.08e-65 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 207.65 E-value: 3.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRRE-VGMVFQHFNLFPHLTI 110
Cdd:COG4175 43 VNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKlSKKELRELRRKkMSMVFQHFALLPHRTV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP----E 186
Cdd:COG4175 123 LENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrE 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 187 MIKEVLDtmvgL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:COG4175 202 MQDELLE----LqAKLKKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNP 255
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
28-244 |
1.23e-64 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 209.76 E-value: 1.23e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ---KGKIVVDGTELTNdlKKIDEVRREVGMVFQHF-- 102
Cdd:COG1123 17 GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLE--LSEALRGRRIGMVFQDPmt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 103 NLFPhLTILENCTLAPIwVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:COG1123 95 QLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTA 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 183 LDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:COG1123 173 LDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
19-229 |
2.14e-64 |
|
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: 200.00 E-value: 2.14e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFH--VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVG 96
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK--LSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNL-FPHLTILENCTLAPIwVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:cd03225 79 LVFQNPDDqFFGPTVEEEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502303547 176 FDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQ 229
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
18-244 |
1.52e-63 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 198.61 E-value: 1.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlkkIDEVRREVGM 97
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
19-246 |
1.09e-62 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 198.78 E-value: 1.09e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGD-FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGM 97
Cdd:COG1125 3 EFENVTKRYPDgTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRD--LDPVELRRRIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAPIwVRKMPKKQAEEVAMHFLKRVKI-PEQ-ANKYPGQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:COG1125 81 VIQQIGLFPHMTVAENIATVPR-LLGWDKERIRARVDELLELVGLdPEEyRDRYPHELSGGQQQRVGVARALAADPPILL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 176 FDEPTSALDPeMIKEVL-DTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHE 246
Cdd:COG1125 160 MDEPFGALDP-ITREQLqDELLRLQRElGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPAND 231
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
19-243 |
7.23e-61 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 195.64 E-value: 7.23e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlkkIDEVRREVGMV 98
Cdd:TIGR03265 6 SIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITR----LPPQKRDYGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 99 FQHFNLFPHLTILENCT--LAPiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:TIGR03265 82 FQSYALFPNLTVADNIAygLKN---RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 177 DEPTSALDPEmIKEVLDT-MVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:TIGR03265 159 DEPLSALDAR-VREHLRTeIRQLQRRlGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHP 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
19-244 |
1.52e-60 |
|
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: 190.73 E-value: 1.52e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDE-VRREVGM 97
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG--LPPHEiARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAP---------IWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLC 168
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAqartgsgllLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 169 MNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
33-252 |
2.09e-60 |
|
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: 194.69 E-value: 2.09e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRR-EVGMVFQHFNLFPHLTI 110
Cdd:TIGR01186 9 VNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKqSPVELREVRRkKIGMVFQQFALFPHMTI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLAPiWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKE 190
Cdd:TIGR01186 89 LQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRDS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 191 VLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFL 252
Cdd:TIGR01186 168 MQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFI 230
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
17-244 |
2.35e-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: 190.63 E-value: 2.35e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkKIDEVRREVG 96
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT----DVPVQERNVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHLTILENCTLA----PIWVRKmPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:cd03296 78 FVFQHYALFRHMTVFDNVAFGlrvkPRSERP-PEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPA 229
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
18-253 |
3.08e-59 |
|
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: 187.54 E-value: 3.08e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHvLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdLKKIdevRREVGM 97
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-LPPE---KRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 178 EPTSALDPEmIKEVLDTMVGLA--EEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLS 253
Cdd:cd03299 155 EPFSALDVR-TKEKLREELKKIrkEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
19-242 |
5.26e-58 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 183.79 E-value: 5.26e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdLKKIDEVRREVGMV 98
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-LPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 99 FQHFNLFPHLTILENCTLApIWVRKMPKKQAEevamhfLKRV-----KIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:cd03224 81 PEGRRIFPELTVEENLLLG-AYARRRAKRKAR------LERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:cd03224 154 LLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
18-240 |
3.22e-57 |
|
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: 183.40 E-value: 3.22e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY--GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlKKIDEVRREV 95
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDE-ENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQH-FNLFPHLTI-------LENctlapiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSL 167
Cdd:TIGR04520 80 GMVFQNpDNQFVGATVeddvafgLEN--------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 168 CMNPKIMLFDEPTSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFF 240
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
27-252 |
6.74e-57 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 181.49 E-value: 6.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVlrDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkKIDEVRREVGMVFQHFNLFP 106
Cdd:COG3840 11 YGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLT----ALPPAERPVSMLFQENNLFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLApiwVR---KMPKKQAEEVAmHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:COG3840 85 HLTVAQNIGLG---LRpglKLTAEQRAQVE-QALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 184 DPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFL 252
Cdd:COG3840 161 DPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYL 230
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
17-257 |
1.31e-56 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 184.52 E-value: 1.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKIDEVRREVG 96
Cdd:PRK10851 2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGT----DVSRLHARDRKVG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHLTILENC----TLAPiwVRKMPKKQA-EEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:PRK10851 78 FVFQHYALFRHMTVFDNIafglTVLP--RRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKL 250
Cdd:PRK10851 156 QILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLE 235
|
....*..
gi 502303547 251 FLSQILH 257
Cdd:PRK10851 236 FMGEVNR 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
18-232 |
1.41e-56 |
|
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: 180.14 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGtELTNDLKKIDevrREVGM 97
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGG-RDVTDLPPKD---RDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLaPIWVRKMPK----KQAEEVAmhflKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKdeidERVREVA----ELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:cd03301 152 FLMDEPLSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQ 211
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
13-248 |
1.68e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 180.67 E-value: 1.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 13 ATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlKKIDEVR 92
Cdd:COG1121 2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-------KPPRRAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQHFNL---FPhLTILE---NCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARS 166
Cdd:COG1121 75 RRIGYVPQRAEVdwdFP-ITVRDvvlMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 167 LCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEqNSPAEFFDNPQHE 246
Cdd:COG1121 154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPENLS 232
|
..
gi 502303547 247 RT 248
Cdd:COG1121 233 RA 234
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
12-232 |
2.44e-56 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 179.94 E-value: 2.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 12 SATEVAVEIVNMNKWYGD----FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkK 87
Cdd:COG4181 3 SSSAPIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLF----A 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 88 IDE-----VRRE-VGMVFQHFNLFPHLTILENCTLaPIWVRKMPkkQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRV 161
Cdd:COG4181 79 LDEdararLRARhVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 162 AIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQvANRVIFMDQGQIVE 232
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-256 |
2.51e-56 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 180.81 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL-----EEHQKGKIVVDGTELTNDLKKID 89
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 90 EVRREVGMVFQHFNLFPHLTILENCTLApIWVRKM--PKKQAEEVAMHFLKRV----KIPEQANKYPGQLSGGQQQRVAI 163
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLvkSKKELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 164 ARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PRK14267 161 ARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENP 239
|
250
....*....|...
gi 502303547 244 QHERTKLFLSQIL 256
Cdd:PRK14267 240 EHELTEKYVTGAL 252
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
18-230 |
5.84e-56 |
|
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: 176.82 E-value: 5.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIdevRREVGM 97
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV---KRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENctlapiwvrkmpkkqaeevamhfLKrvkipeqankypgqLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03230 78 LPEEPSLYENLTVREN-----------------------LK--------------LSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
27-230 |
6.75e-56 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 178.09 E-value: 6.75e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQHFNLFP 106
Cdd:COG4619 10 VGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAYVPQEPALWG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HlTILENctLAPIWVRKmPKKQAEEVAMHFLKRVKIPEQANKYP-GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:COG4619 88 G-TVRDN--LPFPFQLR-ERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502303547 186 EMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:COG4619 164 ENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
27-238 |
1.36e-55 |
|
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: 178.70 E-value: 1.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNL 104
Cdd:COG1120 11 YGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGR----DLASLSrrELARRIAYVPQEPPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 FPHLTILEncTLA-------PIWVRkmPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:COG1120 87 PFGLTVRE--LVAlgryphlGLFGR--PSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLLLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLA-EEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG1120 163 EPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
19-244 |
4.33e-55 |
|
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: 177.10 E-value: 4.33e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDE-VRREVGM 97
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG--LPPHRiARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAPiWVRKMPKKQAEEVAMHF-----LKrvkipEQANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGA-YARRDRAEVRADLERVYelfprLK-----ERRRQRAGTLSGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
14-244 |
4.59e-55 |
|
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: 177.54 E-value: 4.59e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 14 TEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRR 93
Cdd:COG0411 1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRIAR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 94 eVGMV--FQHFNLFPHLTILENCTLA--------------PIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQ 157
Cdd:COG0411 79 -LGIArtFQNPRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 158 QQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSP 236
Cdd:COG0411 158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237
|
....*...
gi 502303547 237 AEFFDNPQ 244
Cdd:COG0411 238 AEVRADPR 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
19-239 |
1.49e-54 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 175.82 E-value: 1.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlKKIDEVRREVGMV 98
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR---KEPREARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 99 FQHFNLFPHLTILENCTLApIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:COG4555 80 PDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 179 PTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEF 239
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
30-244 |
1.88e-54 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 176.49 E-value: 1.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 30 FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKK-IDEVRREVGMVFQhfnlFPH- 107
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKkLKDLRKKVGLVFQ----FPEh 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 108 ----LTILENCTLAPIWVrKMPKKQAEEVAMHFLKRVKIPEQ-ANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:TIGR04521 94 qlfeETVYKDIAFGPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 183 LDPEMIKEVLDTMVGLA-EEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:TIGR04521 173 LDPKGRKEILDLFKRLHkEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
20-225 |
5.43e-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: 173.19 E-value: 5.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 20 IVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRRE-VGM 97
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPlNSKKASKFRREkLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAPIWVRKmPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFM 225
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
19-229 |
1.08e-53 |
|
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: 170.89 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMV 98
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--LPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 99 FQhfnlfphltilenctlapiwvrkmpkkqaeevamhflkrvkipeqankypgqLSGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502303547 179 PTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQ 229
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-252 |
1.17e-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: 1.17e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL----EEHQKGKIVVDGTELTN-DLKKIDEVR-REVGMVFQH 101
Cdd:COG4172 21 GTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGlSERELRRIRgNRIAMIFQE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 102 ----FNlfPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANK---YPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:COG4172 101 pmtsLN--PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFL 252
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLL 257
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
32-238 |
8.04e-52 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 179.26 E-value: 8.04e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNLFpHLT 109
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGI----DLRQIDpaSLRRQIGVVLQDVFLF-SGT 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLapiWVRKMPKKQAEEVAmhflKRVKIPEQANKYP-----------GQLSGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:COG2274 565 IRENITL---GDPDATDEEIIEAA----RLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDE 637
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 179 PTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAE 238
Cdd:COG2274 638 ATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE 695
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
18-229 |
1.06e-51 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 167.43 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY-GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtNDL--KKIDEVRRE 94
Cdd:TIGR02673 2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDV-NRLrgRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 VGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQ 229
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDGR 214
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-255 |
2.14e-51 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 170.30 E-value: 2.14e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 11 VSATEVAVEIVNMNKWY-----------GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGT 79
Cdd:COG4608 1 AAMAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 80 ELTN-DLKKIDEVRREVGMVFQ--HFNLFPHLTILEncTLA-PIWVRKM-PKKQAEEVAMHFLKRVKI-PEQANKYPGQL 153
Cdd:COG4608 81 DITGlSGRELRPLRRRMQMVFQdpYASLNPRMTVGD--IIAePLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 154 SGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVE 238
|
250 260
....*....|....*....|...
gi 502303547 233 QNSPAEFFDNPQHERTKLFLSQI 255
Cdd:COG4608 239 IAPRDELYARPLHPYTQALLSAV 261
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-243 |
2.84e-51 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 171.28 E-value: 2.84e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 7 KKLTVSATEVA--VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNd 84
Cdd:PRK09452 2 KKLNKQPSSLSplVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 85 lkkIDEVRREVGMVFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIA 164
Cdd:PRK09452 81 ---VPAENRHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 165 RSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PRK09452 157 RAVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEP 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
32-229 |
1.51e-50 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 162.94 E-value: 1.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNLFpHLT 109
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGV----DLRDLDleSLRKNIAYVPQDPFLF-SGT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENctlapiwvrkmpkkqaeevamhflkrvkIpeqankypgqLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIK 189
Cdd:cd03228 92 IREN----------------------------I----------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEA 133
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502303547 190 EVLDTMVGLAeEGMTMLCVTHEMGFARQvANRVIFMDQGQ 229
Cdd:cd03228 134 LILEALRALA-KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
33-181 |
7.51e-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: 160.51 E-value: 7.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIdeVRREVGMVFQHFNLFPHLTILE 112
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS--LRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 113 NCTLAPIwVRKMPKKQAEEVAMHFLKRVKIPEQAN----KYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTS 181
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
18-230 |
1.57e-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: 162.19 E-value: 1.57e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY-GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtNDLKK--IDEVRRE 94
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDV-SDLRGraIPYLRRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 VGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMhFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:cd03292 80 IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPA-ALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:cd03292 159 IADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
28-249 |
2.32e-49 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 169.87 E-value: 2.32e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQkGKIVVDGTELTN-DLKKIDEVRREVGMVFQ----HF 102
Cdd:COG4172 297 GHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGlSRRALRPLRRRMQVVFQdpfgSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 103 NlfPHLTILEncTLA-PIWV--RKMPKKQAEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:COG4172 376 S--PRMTVGQ--IIAeGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDE 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 179 PTSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTK 249
Cdd:COG4172 452 PTSALDVSVQAQILDLLRDLqREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTR 523
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-243 |
3.09e-49 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 165.66 E-value: 3.09e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 21 VNMNKWYGDFHVlrDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKID---EvRREVGM 97
Cdd:COG4148 5 VDFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFlppH-RRRIGY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCT--LAPIWVRKMPKKQAEEVAM----HFLKRvkipeqankYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:COG4148 82 VFQEARLFPHLSVRGNLLygRKRAPRAERRISFDEVVELlgigHLLDR---------RPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP 225
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
35-233 |
3.44e-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: 161.12 E-value: 3.44e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 35 DINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlkkIDEVRREVGMVFQHFNLFPHLTILENC 114
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA----APPADRPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 115 TLAPIWVRKMPKKQAEEVAMhFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDT 194
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEV-ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 502303547 195 MVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQ 233
Cdd:cd03298 171 VLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
25-238 |
4.43e-49 |
|
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: 163.71 E-value: 4.43e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 25 KWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlKKIDEVRREVGMVFQHFNL 104
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVV---REPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 FPHLTILENCTL-APIWvrKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:TIGR01188 78 DEDLTGRENLEMmGRLY--GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 184 DPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
32-230 |
8.83e-49 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 160.27 E-value: 8.83e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN--DLKKIDEVRREVGMVFQHFNLFPHLT 109
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNlsYSQKIILRRELIGYIFQSFNLIPHLS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIK 189
Cdd:NF038007 100 IFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNAR 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502303547 190 EVLDTMVGLAEEGMTMLCVTHEMGfARQVANRVIFMDQGQI 230
Cdd:NF038007 179 AVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-257 |
8.91e-49 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 161.23 E-value: 8.91e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL-----EEHQKGKIVVDGteltNDLKKID--E 90
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDG----QDIFKMDviE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 91 VRREVGMVFQHFNLFPHLTILENCTLAPIWVRKM-PKKQAEEVAMHFLKRVKIPEQA----NKYPGQLSGGQQQRVAIAR 165
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQLWDEVkdrlDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 166 SLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQH 245
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
250
....*....|..
gi 502303547 246 ERTKLFLSQILH 257
Cdd:PRK14247 239 ELTEKYVTGRLY 250
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
27-228 |
2.53e-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: 158.85 E-value: 2.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlKKIDEVRREVGMVFQHFNL-- 104
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-------KPLEKERKRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 -FPhLTILE----NCTLAPIWVRKMPKKQAEEVaMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEP 179
Cdd:cd03235 82 dFP-ISVRDvvlmGLYGHKGLFRRLSKADKAKV-DEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502303547 180 TSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQG 228
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
14-253 |
5.05e-48 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 159.56 E-value: 5.05e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 14 TEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL-----EEHQKGKIVVDGTELTNDLKKI 88
Cdd:PRK14239 2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 89 DEVRREVGMVFQHFNLFPhLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQ----LSGGQQQRVAIA 164
Cdd:PRK14239 82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRLHDsalgLSGGQQQRVCIA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 165 RSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPK 239
|
....*....
gi 502303547 245 HERTKLFLS 253
Cdd:PRK14239 240 HKETEDYIS 248
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
28-238 |
1.32e-47 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 166.11 E-value: 1.32e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNLF 105
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV----DIRDLTleSLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 pHLTILENCTLApiwvrkmpKKQA--EEV--------AMHFLKRvkIPEQANKYPGQ----LSGGQQQRVAIARSLCMNP 171
Cdd:COG1132 427 -SGTIRENIRYG--------RPDAtdEEVeeaakaaqAHEFIEA--LPDGYDTVVGErgvnLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAE 238
Cdd:COG1132 496 PILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
18-243 |
1.55e-47 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 161.04 E-value: 1.55e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEvrREVGM 97
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQ--RDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLApiwvRKMPKKQAEEVAMHF---LKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:PRK11432 83 VFQSYALFPHMSLGENVGYG----LKMLGVPKEERKQRVkeaLELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQP 228
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
48-255 |
2.46e-47 |
|
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: 159.97 E-value: 2.46e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 48 IAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlkkIDEVRREVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKK 127
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 128 QAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTML 206
Cdd:TIGR01187 76 EIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITFV 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502303547 207 CVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQI 255
Cdd:TIGR01187 156 FVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
5-243 |
1.03e-46 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 159.62 E-value: 1.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 5 PAKKLTVSATEVaVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnD 84
Cdd:PRK11607 8 PQAKTRKALTPL-LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV----D 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 85 LKKIDEVRREVGMVFQHFNLFPHLTILENCTLApIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIA 164
Cdd:PRK11607 83 LSHVPPYQRPINMMFQSYALFPHMTVEQNIAFG-LKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 165 RSLCMNPKIMLFDEPTSALDPE----MIKEVLDTmvgLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK11607 162 RSLAKRPKLLLLDEPMGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY 238
|
...
gi 502303547 241 DNP 243
Cdd:PRK11607 239 EHP 241
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-233 |
1.70e-46 |
|
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: 152.97 E-value: 1.70e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtNDLKKIdEVRREVGMV 98
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-ASLSPK-ELARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 99 FQhfnlfphltilenctlapiwvrkmpkkqaeevamhFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:cd03214 79 PQ-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 179 PTSALDPEMIKEVLDTMVGLA-EEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQ 233
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLArERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
32-238 |
2.13e-46 |
|
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: 162.63 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTnDLKKiDEVRREVGMVFQHfnlfPHL--- 108
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLR-DLDE-DDLRRRIAVVPQR----PHLfdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILENCTLApiwvrkmpKKQA-EEVAMHFLKRVKIPEQANKYPG-----------QLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:COG4987 424 TLRENLRLA--------RPDAtDEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLL 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 177 DEPTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHEM-GFARqvANRVIFMDQGQIVEQNSPAE 238
Cdd:COG4987 496 DEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLaGLER--MDRILVLEDGRIVEQGTHEE 555
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-231 |
2.39e-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: 153.99 E-value: 2.39e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 20 IVNMNKWYGDFHVLRDINLKvmrGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKID--EVRREVGM 97
Cdd:cd03297 3 CVDIEKRLPDFTLKIDFDLN---EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINlpPQQRKIGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEvamHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03297 80 VFQQYALFPHLNVRENLAFGLKRKRNREDRISVD---ELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:cd03297 157 EPFSALDRALRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
33-252 |
6.03e-46 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 158.27 E-value: 6.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRRE-VGMVFQHFNLFPHLTI 110
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKiSDAELREVRRKkIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLApIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKE 190
Cdd:PRK10070 124 LDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 191 VLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFL 252
Cdd:PRK10070 203 MQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-257 |
6.08e-46 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 154.85 E-value: 6.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGD-FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVG 96
Cdd:PRK13639 2 LETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFN--LFPHlTILENCTLAPIWVrKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:PRK13639 82 IVFQNPDdqLFAP-TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQH-ERTKLFLS 253
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETiRKANLRLP 239
|
....
gi 502303547 254 QILH 257
Cdd:PRK13639 240 RVAH 243
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
9-238 |
2.62e-45 |
|
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: 159.54 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 9 LTVSATEVAVeivnmnKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlkKI 88
Cdd:COG4988 335 PSIELEDVSF------SYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL--DP 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 89 DEVRREVGMVFQHFNLFpHLTILENCTLApiwvrkmpKKQAEEVAMH-FLKRVKIPEQANKYPG-----------QLSGG 156
Cdd:COG4988 407 ASWRRQIAWVPQNPYLF-AGTIRENLRLG--------RPDASDEELEaALEAAGLDEFVAALPDgldtplgeggrGLSGG 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 157 QQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSP 236
Cdd:COG4988 478 QAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTH 555
|
..
gi 502303547 237 AE 238
Cdd:COG4988 556 EE 557
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
33-240 |
9.87e-45 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 151.71 E-value: 9.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQH-FNLFPHLTI- 110
Cdd:PRK13635 23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVWDVRRQVGMVFQNpDNQFVGATVq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 ------LENctlapiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:PRK13635 101 ddvafgLEN--------IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLD 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 185 PEMIKEVLDTMVGLAEEGM-TMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK13635 173 PRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
15-244 |
1.64e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 150.91 E-value: 1.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNKWYGDFH--VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlkKIDEVR 92
Cdd:PRK13632 5 SVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE--NLKEIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQH-FNLFPHLTI-------LENctlapiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIA 164
Cdd:PRK13632 83 KKIGIIFQNpDNQFIGATVeddiafgLEN--------KKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 165 RSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGM-TMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
|
.
gi 502303547 244 Q 244
Cdd:PRK13632 234 E 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
20-238 |
9.83e-44 |
|
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: 151.03 E-value: 9.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 20 IVNMNKWYGDFHVlrDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKID--EVRREVGM 97
Cdd:TIGR02142 2 SARFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFlpPEKRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENctLAPIWVRKMPKKQ----AEEVAM----HFLKRvkipeqankYPGQLSGGQQQRVAIARSLCM 169
Cdd:TIGR02142 80 VFQEARLFPHLSVRGN--LRYGMKRARPSERrisfERVIELlgigHLLGR---------LPGRLSGGEKQRVAIGRALLS 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 170 NPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:TIGR02142 149 SPRLLLMDEPLAALDDPRKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAE 218
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
10-253 |
2.50e-43 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 147.62 E-value: 2.50e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 10 TVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEE-----HQKGKIVVDGTELTNd 84
Cdd:PRK14243 3 TLNGTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfRVEGKVTFHGKNLYA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 85 lKKID--EVRREVGMVFQHFNLFPHlTILENCTLAPiWVRKMpKKQAEEVAMHFLKRVKIPEQAN---KYPGQ-LSGGQQ 158
Cdd:PRK14243 82 -PDVDpvEVRRRIGMVFQKPNPFPK-SIYDNIAYGA-RINGY-KGDMDELVERSLRQAALWDEVKdklKQSGLsLSGGQQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 159 QRVAIARSLCMNPKIMLFDEPTSALDP-------EMIKEVldtmvglaEEGMTMLCVTHEMGFARQVANRVIFMD----- 226
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPistlrieELMHEL--------KEQYTIIIVTHNMQQAARVSDMTAFFNvelte 229
|
250 260 270
....*....|....*....|....*....|.
gi 502303547 227 ----QGQIVEQNSPAEFFDNPQHERTKLFLS 253
Cdd:PRK14243 230 gggrYGYLVEFDRTEKIFNSPQQQATRDYVS 260
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-253 |
2.87e-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: 146.52 E-value: 2.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTnDLKKIDEVRREVGMV 98
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDIT-KLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 99 FQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHF--LKRVKipeqaNKYPGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYELFpvLKEML-----GRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 177 DEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFfdnpQHERTKLFLS 253
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL----DEDKVRRYLA 229
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-252 |
8.28e-43 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 146.35 E-value: 8.28e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 11 VSATEVAVEIVNMNKWY---GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTEL--TNDL 85
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfGKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 86 KKIDEV--RREVGMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRV----KIPEQANKYPGQLSGGQQQ 159
Cdd:PRK14246 81 FQIDAIklRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 160 RVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEF 239
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
250
....*....|...
gi 502303547 240 FDNPQHERTKLFL 252
Cdd:PRK14246 240 FTSPKNELTEKYV 252
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
32-249 |
1.51e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 146.00 E-value: 1.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTElTNDLKKIDEVRREVGMVFQHFNLFPHLTIL 111
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWDIRNKAGMVFQNPDNQIVATIV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 E--------NCTLAPIWVRKmpkkQAEEVamhfLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:PRK13633 104 EedvafgpeNLGIPPEEIRE----RVDES----LKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 184 DPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFdnPQHERTK 249
Cdd:PRK13633 176 DPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIF--KEVEMMK 239
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
18-244 |
2.01e-42 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 148.25 E-value: 2.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGtELTNDLKKIDevrREVGM 97
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE-KRMNDVPPAE---RGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCT----LAPIWVRKMPKK--QAEEVAM--HFLKRvkipeqankYPGQLSGGQQQRVAIARSLCM 169
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSfglkLAGAKKEEINQRvnQVAEVLQlaHLLDR---------KPKALSGGQRQRVAIGRTLVA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 170 NPKIMLFDEPTSALDP----EMIKEVLDTMVGLaeeGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
18-238 |
2.09e-42 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 143.80 E-value: 2.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGD--FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIdevRREV 95
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAA---RQSL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLTILENCTL-APIwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:cd03263 78 GYCPQFDALFDELTVREHLRFyARL--KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
37-238 |
2.82e-42 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 143.95 E-value: 2.82e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 37 NLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTL 116
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG----QDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 117 APIWVRKMPKKQAEEVAmHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEvldtMV 196
Cdd:PRK10771 95 GLNPGLKLNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE----ML 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502303547 197 GL-----AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:PRK10771 170 TLvsqvcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
18-238 |
3.17e-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: 3.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtndLKKIDEVRREVGM 97
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV---VREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTL-APIWvrKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIhARLY--GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 177 DEPTSALDP---EMIKEVLDTMVglAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:cd03265 156 DEPTIGLDPqtrAHVWEYIEKLK--EEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
30-231 |
4.20e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 145.61 E-value: 4.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 30 FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL-------------EEHQKGKIVVDGTELTND---------LKK 87
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALllpdtgtiewifkDEKNKKKTKEKEKVLEKLviqktrfkkIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 88 IDEVRREVGMVFQ--HFNLFPHlTILENCTLAPIWVrKMPKKQAEEVAMHFLKRVKIPEQ-ANKYPGQLSGGQQQRVAIA 164
Cdd:PRK13651 100 IKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDESyLQRSPFELSGGQKRRVALA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 165 RSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:PRK13651 178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKII 244
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
28-215 |
6.74e-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: 141.79 E-value: 6.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGMVFQHFN--LF 105
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 pHLTILENCTLAPIWVrKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:TIGR01166 83 -AADVDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDP 160
|
170 180 190
....*....|....*....|....*....|
gi 502303547 186 EMIKEVLDTMVGLAEEGMTMLCVTHEMGFA 215
Cdd:TIGR01166 161 AGREQMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
32-231 |
1.08e-41 |
|
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: 141.63 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtndlkKIDEVRREVGMVFQH--FNLFPHlT 109
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERRKSIGYVMQDvdYQLFTD-S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLapiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIK 189
Cdd:cd03226 89 VREELLL-----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNME 163
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502303547 190 EVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:cd03226 164 RVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
27-233 |
1.34e-41 |
|
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: 141.54 E-value: 1.34e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkKIDEVRREVGMVFQHFNLFP 106
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHT----GLAPYQRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLA---PIWVRKMPKKQAEEVAmhflKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:TIGR01277 84 HLTVRQNIGLGlhpGLKLNAEQQEKVVDAA----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502303547 184 DPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQ 233
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKIKVV 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
14-239 |
1.51e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 148.24 E-value: 1.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 14 TEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndLKKIDEVRR 93
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR--FRSPRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 94 E-VGMVFQHFNLFPHLTILENctlapIWVRKMPKK-----------QAEEVamhfLKRVKIPEQANKYPGQLSGGQQQRV 161
Cdd:COG1129 79 AgIAIIHQELNLVPNLSVAEN-----IFLGREPRRgglidwramrrRAREL----LARLGLDIDPDTPVGDLSVAQQQLV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 162 AIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEF 239
Cdd:COG1129 150 EIARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
31-233 |
2.47e-41 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 142.31 E-value: 2.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlkkidEVRRevGMVFQHFNLFPHLTI 110
Cdd:COG4525 21 PALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-----GADR--GVVFQKDALLPWLNV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP---EM 187
Cdd:COG4525 94 LDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDAltrEQ 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502303547 188 IKEVLDTMvgLAEEGMTMLCVTHEMGFARQVANRVIFMD--QGQIVEQ 233
Cdd:COG4525 173 MQELLLDV--WQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIVER 218
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
13-238 |
2.58e-41 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 147.87 E-value: 2.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 13 ATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkkI---- 88
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVR-----Irspr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 89 DEVRREVGMVFQHFNLFPHLTILENCTLA--PIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARS 166
Cdd:COG3845 76 DAIALGIGMVHQHFMLVPNLTVAENIVLGlePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 167 LCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG3845 156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
33-244 |
3.61e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 142.66 E-value: 3.61e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDL--KKIDEVRREVGMVFQhfnlFPHLTI 110
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLAPiwVRKMPK------KQAEEVAMHFLKRVKIPEQ-ANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:PRK13641 99 FENTVLKD--VEFGPKnfgfseDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 184 DPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
18-231 |
3.65e-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: 138.72 E-value: 3.65e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdLKKIDEVRREVGM 97
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSF-ASPRDARRAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQhfnlfphltilenctlapiwvrkmpkkqaeevamhflkrvkipeqankypgqLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
33-242 |
3.68e-41 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 142.88 E-value: 3.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGMVFQH--FNLFPHlTI 110
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQYpeYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLAPIwVRKMPKKQAEEVAMHFLKRVKIP--EQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMI 188
Cdd:PRK13637 102 EKDIAFGPI-NLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 189 KEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
33-244 |
1.81e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 140.93 E-value: 1.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN--DLKKIDEVRREVGMVFQhfnlFPHLTI 110
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkKNKKLKPLRKKVGIVFQ----FPEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLAPIWVRKM----PKKQAEEVAMHFLKRVKIPEQA-NKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:PRK13634 99 FEETVEKDICFGPMnfgvSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 186 EMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:PRK13634 179 KGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
32-238 |
2.50e-40 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 138.90 E-value: 2.50e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltNDLKKI--DEVRREVGMVFQHFNLFpHLT 109
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG----QDIREVtlDSLRRAIGVVPQDTVLF-NDT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQ----LSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:cd03253 91 IGYNIRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 186 EMIKEVLDTMVGLAeEGMTMLCVTHEMgfaRQVAN--RVIFMDQGQIVEQNSPAE 238
Cdd:cd03253 171 HTEREIQAALRDVS-KGRTTIVIAHRL---STIVNadKIIVLKDGRIVERGTHEE 221
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
32-241 |
3.38e-40 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 138.77 E-value: 3.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltNDLKKIDE--VRREVGMVFQHFNLFpHLT 109
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG----HDLALADPawLRRQVGVVLQENVLF-NRS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLAPiwvRKMPKKQAEEVA----MHFLKRvKIPEQANKYPGQ----LSGGQQQRVAIARSLCMNPKIMLFDEPTS 181
Cdd:cd03252 92 IRDNIALAD---PGMSMERVIEAAklagAHDFIS-ELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 182 ALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:cd03252 168 ALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
18-233 |
4.75e-40 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 137.71 E-value: 4.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGeRIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTEltnDLKKIDEVRREVGM 97
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQD---VLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILEncTLAPI-WVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:cd03264 77 LPQEFGVYPNFTVRE--FLDYIaWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 177 DEPTSALDPEMIKEVLDTMVGLAEEGMTMLCvTHEMGFARQVANRVIFMDQGQIVEQ 233
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDRIVILS-THIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
29-240 |
8.84e-40 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 138.71 E-value: 8.84e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlkKIDEVRREVGMVFQH-FNLFPH 107
Cdd:PRK13650 19 EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE--NVWDIRHKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 108 LTI-------LENctlapiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPT 180
Cdd:PRK13650 97 ATVeddvafgLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 181 SALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGfarQVA--NRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK13650 169 SMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELF 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
33-240 |
1.16e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 138.72 E-value: 1.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDL--KKIDEVRREVGMVFQhfnlFPHLTI 110
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknKDIKQIRKKVGLVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLAPIWVRK----MPKKQAEEVAMHFLKRVKIPEQA-NKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:PRK13649 99 FEETVLKDVAFGPqnfgVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 186 EMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK13649 179 KGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIF 233
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
31-231 |
1.73e-39 |
|
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: 136.18 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNLFpHL 108
Cdd:cd03245 18 PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGT----DIRQLDpaDLRRNIGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILENCTLApiwvrkMPKKQAEEVaMHFLKRVKIPEQANKYP----------GQ-LSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03245 93 TLRDNITLG------APLADDERI-LRAAELAGVTDFVNKHPngldlqigerGRgLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 178 EPTSALD---PEMIKEVLDTMVGlaeeGMTMLCVTHEMGFArQVANRVIFMDQGQIV 231
Cdd:cd03245 166 EPTSAMDmnsEERLKERLRQLLG----DKTLIIITHRPSLL-DLVDRIIVMDSGRIV 217
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
32-241 |
1.84e-39 |
|
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: 136.59 E-value: 1.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLK--KIDEVRREVGMVFQHFNLFpHLT 109
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH----DVRdyTLASLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLApiwVRKMPKKQAEEVA-----MHFLKRvkIPEQANKYPG----QLSGGQQQRVAIARSLCMNPKIMLFDEPT 180
Cdd:cd03251 92 VAENIAYG---RPGATREEVEEAAraanaHEFIME--LPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPILILDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 181 SALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:cd03251 167 SALDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLA 225
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
33-228 |
2.11e-39 |
|
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: 136.44 E-value: 2.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlKKIDEVRREVGMVFQHFNLFPHLTILE 112
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-------KQITEPGPDRMVVFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 113 NCTLAPIWV-RKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEV 191
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 502303547 192 LDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQG 228
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
33-243 |
2.48e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 137.81 E-value: 2.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTElTNDLKKIDEVRREVGMVFQHfnlfPHLTIL- 111
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIRKLVGIVFQN----PETQFVg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 -----------ENCTLAPIWVRKMPKKQaeevamhfLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPT 180
Cdd:PRK13644 93 rtveedlafgpENLCLPPIEIRKRVDRA--------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 181 SALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGfARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PRK13644 165 SMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEPENVLSDV 226
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
32-238 |
2.76e-39 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 144.10 E-value: 2.76e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGT---ELTNDlkKIDEVRRE-VGMVFQHFNLFPH 107
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQdvaTLDAD--ALAQLRREhFGFIFQRYHLLSH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 108 LTILENCTLAPIWVrKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEM 187
Cdd:PRK10535 101 LTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502303547 188 IKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVeQNSPAE 238
Cdd:PRK10535 180 GEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV-RNPPAQ 228
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
32-244 |
3.44e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 137.62 E-value: 3.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL---EEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQH-FNLFPH 107
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA--KTVWDIREKVGIVFQNpDNQFVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 108 LTI-------LENctlapiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPT 180
Cdd:PRK13640 100 ATVgddvafgLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDEST 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 181 SALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:PRK13640 172 SMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIFSKVE 235
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
18-241 |
5.84e-39 |
|
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: 135.43 E-value: 5.84e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWY-GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtNDLKKIdEVRREVG 96
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRK-SLRSMIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHlTILENCTLA-PIWVRKMPKKQAEEVAMH-FLKrvKIPEQANKYPGQ----LSGGQQQRVAIARSLCMN 170
Cdd:cd03254 81 VVLQDTFLFSG-TIMENIRLGrPNATDEEVIEAAKEAGAHdFIM--KLPNGYDTVLGEnggnLSQGERQLLAIARAMLRD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 171 PKIMLFDEPTSALDPEMIKEVLDTMVGLaEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:cd03254 158 PKILILDEATSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
33-253 |
1.18e-38 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 137.02 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT-NDLKKIDEVRREVGMVFQhfNLFPHL--- 108
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkADPEAQKLLRQKIQIVFQ--NPYGSLnpr 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 ----TILEnctlAPIWVR-KMPKKQAEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:PRK11308 109 kkvgQILE----EPLLINtSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSA 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 183 LDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLS 253
Cdd:PRK11308 185 LDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
8-231 |
1.94e-38 |
|
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: 132.67 E-value: 1.94e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 8 KLTVSATEVAVEIVNmNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCIN--RLEEHQKGKIVVDGTELtndl 85
Cdd:cd03213 1 GVTLSFRNLTVTVKS-SPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 86 kKIDEVRREVGMVFQHFNLFPHLTILEnctlapiwvrkmpkkqaeevAMHFLKRVKipeqankypgQLSGGQQQRVAIAR 165
Cdd:cd03213 76 -DKRSFRKIIGYVPQDDILHPTLTVRE--------------------TLMFAAKLR----------GLSGGERKRVSIAL 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 166 SLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTH----EMgFarQVANRVIFMDQGQIV 231
Cdd:cd03213 125 ELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVI 191
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
18-233 |
2.33e-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: 133.11 E-value: 2.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltNDLKKIDEVRREVGM 97
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDG----KSYQKNIEALRRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILEN----CTLAPIwvrkmPKKQAEEVamhfLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:cd03268 77 LIEAPGFYPNLTARENlrllARLLGI-----RKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQ 233
Cdd:cd03268 148 LILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
32-238 |
4.45e-38 |
|
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: 141.03 E-value: 4.45e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKIDEV--RREVGMVFQHFNLFPHlT 109
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGV----DLAIADPAwlRRQMGVVLQENVLFSR-S 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLAPiwvrkmPKKQAEEV--------AMHFLKRVK--IPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEP 179
Cdd:TIGR01846 547 IRDNIALCN------PGAPFEHVihaaklagAHDFISELPqgYNTEVGEKGANLSGGQRQRIAIARALVGNPRILIFDEA 620
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 180 TSALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAE 238
Cdd:TIGR01846 621 TSALDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEE 677
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
15-242 |
4.63e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 133.98 E-value: 4.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL-------EEHQK--GKIVVDGTELTNDL 85
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksaGSHIEllGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 86 KKideVRREVGMVFQHFNLFPHLTILENCTLA-----PIW---VRKMPKKQAEEvAMHFLKRVKIPEQANKYPGQLSGGQ 157
Cdd:PRK09984 82 RK---SRANTGYIFQQFNLVNRLSVLENVLIGalgstPFWrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 158 QQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAE-EGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSp 236
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS- 236
|
....*.
gi 502303547 237 AEFFDN 242
Cdd:PRK09984 237 SQQFDN 242
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
32-256 |
5.07e-38 |
|
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: 133.78 E-value: 5.07e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRREVGMVFQH----FNlfP 106
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQRRAFRRDVQLVFQDspsaVN--P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTI-------LENCTlapiwvrKMPKKQAEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:TIGR02769 104 RMTVrqiigepLRHLT-------SLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDE 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 179 PTSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNpQHERTKLFLSQIL 256
Cdd:TIGR02769 177 AVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSAVL 254
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
17-243 |
5.18e-38 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 136.13 E-value: 5.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWY-GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGtELTNDLKKIDevrREV 95
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG-RVVNELEPAD---RDI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLTILENctLApiW---VRKMPK----KQAEEVA-----MHFLKRvkipeqankYPGQLSGGQQQRVAI 163
Cdd:PRK11650 79 AMVFQNYALYPHMSVREN--MA--YglkIRGMPKaeieERVAEAArilelEPLLDR---------KPRELSGGQRQRVAM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 164 ARSLCMNPKIMLFDEPTSALDP----EM---IKEV---LDTmvglaeegmTMLCVTHEMGFARQVANRVIFMDQGQIvEQ 233
Cdd:PRK11650 146 GRAIVREPAVFLFDEPLSNLDAklrvQMrleIQRLhrrLKT---------TSLYVTHDQVEAMTLADRVVVMNGGVA-EQ 215
|
250
....*....|.
gi 502303547 234 -NSPAEFFDNP 243
Cdd:PRK11650 216 iGTPVEVYEKP 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
18-233 |
6.40e-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: 132.02 E-value: 6.40e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkkiDEVRREVGM 97
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD------IAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCT-LAPIwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLAQL--KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 177 DEPTSALDP---EMIKEVLDTmvgLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQ 233
Cdd:cd03269 153 DEPFSGLDPvnvELLKDVIRE---LARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-253 |
1.08e-37 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 133.30 E-value: 1.08e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 11 VSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEE-----HQKGKIVVDGTELTNdL 85
Cdd:PRK14271 15 VDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDkvsgyRYSGDVLLGGRSIFN-Y 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 86 KKIDEVRREVGMVFQHFNLFPhLTILENcTLAPIWVRKM-PKKQAEEVAMHFLKRV----KIPEQANKYPGQLSGGQQQR 160
Cdd:PRK14271 94 RDVLEFRRRVGMLFQRPNPFP-MSIMDN-VLAGVRAHKLvPRKEFRGVAQARLTEVglwdAVKDRLSDSPFRLSGGQQQL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 161 VAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK14271 172 LCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
250
....*....|...
gi 502303547 241 DNPQHERTKLFLS 253
Cdd:PRK14271 251 SSPKHAETARYVA 263
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
32-229 |
1.34e-37 |
|
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: 131.79 E-value: 1.34e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEV------RREVGMVFQHFNLF 105
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVDLAQASPReilalrRRTIGYVSQFLRVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 PHLTILEnCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQ-ANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:COG4778 106 PRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502303547 185 PEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQ 229
Cdd:COG4778 185 AANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
29-242 |
3.09e-37 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 132.44 E-value: 3.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEV---RREVGMVFQ--HFN 103
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKIKEVkrlRKEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 104 LFPHlTILENCTLAPIWVRKmPKKQAEEVAMHFLKRVKIPEQ-ANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:PRK13645 103 LFQE-TIEKDIAFGPVNLGE-NKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 183 LDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
25-211 |
3.40e-37 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 129.91 E-value: 3.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 25 KWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLkkiDEVRREVGMVFQHFNL 104
Cdd:COG4133 10 CRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRLAYLGHADGL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 FPHLTILENCTLapiWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:COG4133 87 KPELTVRENLRF---WAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALD 163
|
170 180
....*....|....*....|....*..
gi 502303547 185 PEMIKEVLDTMVGLAEEGMTMLCVTHE 211
Cdd:COG4133 164 AAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
17-236 |
9.27e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 131.01 E-value: 9.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGD-FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREV 95
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNA--ENEKWVRSKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFN--LFPhLTILENCTLAPIWVRkMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:PRK13647 82 GLVFQDPDdqVFS-STVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 174 MLFDEPTSALDP---EMIKEVLDtmvGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSP 236
Cdd:PRK13647 160 IVLDEPMAYLDPrgqETLMEILD---RLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
32-238 |
1.03e-36 |
|
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: 129.58 E-value: 1.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtNDLKkIDEVRREVGMVFQHFNLFPhLTIL 111
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI-RDLN-LRWLRSQIGLVSQEPVLFD-GTIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENCTL-APIWVRKMPKKQAEEVAMH-FLkrVKIPEQANKYPG----QLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:cd03249 95 ENIRYgKPDATDEEVEEAAKKANIHdFI--MSLPDGYDTLVGergsQLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502303547 186 EMIKEVLDTMVGLAeEGMTMLCVTHEMGfARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:cd03249 173 ESEKLVQEALDRAM-KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-257 |
2.09e-36 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 130.35 E-value: 2.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGD-FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVG 96
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLRESVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQH--FNLFPhLTILENCTLAPIWVrKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:PRK13636 86 MVFQDpdNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERT-KLFL 252
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKvNLRL 243
|
....*
gi 502303547 253 SQILH 257
Cdd:PRK13636 244 PRIGH 248
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
35-255 |
2.78e-36 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 130.98 E-value: 2.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 35 DINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRREVGMVFQH--FNLFPHLTIL 111
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQDplASLNPRMTIG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENC-----TLAPiwvrKMPKKQAEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:PRK15079 119 EIIaeplrTYHP----KLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDV 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 186 EMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQI 255
Cdd:PRK15079 195 SIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
32-233 |
3.87e-36 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.01 E-value: 3.87e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT--NDLKKIDEVRREVGMVFQHFNLFPHLT 109
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklSSAAKAELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIK 189
Cdd:PRK11629 104 ALENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502303547 190 EVLDTMVGL-AEEGMTMLCVTHEMGFARQVaNRVIFMDQGQIVEQ 233
Cdd:PRK11629 183 SIFQLLGELnRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAE 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
29-240 |
4.00e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 129.51 E-value: 4.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKK--IDEVRREVGMVFQhfnlFP 106
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDkyIRPVRKRIGMVFQ----FP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLAPIWVR----KMPKKQAEEVAMHFLKRVKIPEQA-NKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTS 181
Cdd:PRK13646 95 ESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDVmSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 182 ALDPEMIKEVLDTMVGLA-EEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-256 |
4.40e-36 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 128.51 E-value: 4.40e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 22 NMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTE-LTNDLKKIDEVRR------E 94
Cdd:PRK11701 11 GLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgQLRDLYALSEAERrrllrtE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 VGMVFQHF--NLFPHLTILENctlapIWVRKMPKKQ-----AEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVAIARS 166
Cdd:PRK11701 91 WGFVHQHPrdGLRMQVSAGGN-----IGERLMAVGArhygdIRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 167 LCMNPKIMLFDEPTSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQH 245
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQH 245
|
250
....*....|.
gi 502303547 246 ERTKLFLSQIL 256
Cdd:PRK11701 246 PYTQLLVSSVL 256
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
18-256 |
5.36e-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: 5.36e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCI-NRLEEHQKGKIVVDGTELTNDLKKIDEVRR--- 93
Cdd:TIGR02323 4 LQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLaGRLAPDHGTATYIMRSGAELELYQLSEAERrrl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 94 ---EVGMVFQH------FNLFPHLTILENctLAPIWVRKMPKKQAEevAMHFLKRVKIPE-QANKYPGQLSGGQQQRVAI 163
Cdd:TIGR02323 84 mrtEWGFVHQNprdglrMRVSAGANIGER--LMAIGARHYGNIRAT--AQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 164 ARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:TIGR02323 160 ARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDD 239
|
250
....*....|....
gi 502303547 243 PQHERTKLFLSQIL 256
Cdd:TIGR02323 240 PQHPYTQLLVSSIL 253
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
17-238 |
5.71e-36 |
|
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]
Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 135.08 E-value: 5.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGD--FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltNDLKKID--EVR 92
Cdd:TIGR03797 451 AIEVDRVTFRYRPdgPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDG----QDLAGLDvqAVR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQHFNLFPHlTILEN-CTLAPI-----W-----------VRKMPkkqaeeVAMHFLkrvkIPEQAnkypGQLSG 155
Cdd:TIGR03797 527 RQLGVVLQNGRLMSG-SIFENiAGGAPLtldeaWeaarmaglaedIRAMP------MGMHTV----ISEGG----GTLSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 156 GQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAeegMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNS 235
Cdd:TIGR03797 592 GQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLK---VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGT 667
|
...
gi 502303547 236 PAE 238
Cdd:TIGR03797 668 YDE 670
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
27-232 |
6.03e-36 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 128.28 E-value: 6.03e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlKKIDEVRREVGMVFQHFNLFP 106
Cdd:PRK11248 11 YGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-------KPVEGPGAERGVVFQNEGLLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLApIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP- 185
Cdd:PRK11248 84 WRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAf 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502303547 186 --EMIKEVLDTMvgLAEEGMTMLCVTHEMGFARQVANRVIFM--DQGQIVE 232
Cdd:PRK11248 163 trEQMQTLLLKL--WQETGKQVLLITHDIEEAVFMATELVLLspGPGRVVE 211
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
20-230 |
6.57e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 128.26 E-value: 6.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 20 IVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkkidEVRREVGMVF 99
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLA-------EAREDTRLMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 100 QHFNLFPHLTILENCTLApiwVRKMPKKQAEEVamhfLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEP 179
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLG---LKGQWRDAALQA----LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502303547 180 TSALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
32-241 |
1.94e-35 |
|
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: 132.53 E-value: 1.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTnDLKkIDEVRREVGMVFQHFNLFPHlTIL 111
Cdd:TIGR02203 347 ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA-DYT-LASLRRQVALVSQDVVLFND-TIA 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENCTLAPIwvRKMPKKQAEE-VAMHFLKRV--KIPEQANKYPGQ----LSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:TIGR02203 424 NNIAYGRT--EQADRAEIERaLAAAYAQDFvdKLPLGLDTPIGEngvlLSGGQRQRLAIARALLKDAPILILDEATSALD 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 185 PEMIKEVLDTMVGLaEEGMTMLCVTHEMGfARQVANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:TIGR02203 502 NESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
28-243 |
2.13e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 127.61 E-value: 2.13e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQHFN--LF 105
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK--ENIREVRKFVGLVFQNPDdqIF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 PHlTILENCTLAPIWVRKMPKKQAEEVAmHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:PRK13652 93 SP-TVEQDIAFGPINLGLDEETVAHRVS-SALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 186 EMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PRK13652 171 QGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
29-243 |
2.14e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 128.43 E-value: 2.14e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVV--------------DGTELTNDLKKIDEVRRE 94
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknnhelITNPYSKKIKNFKELRRR 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 VGMVFQ--HFNLFPHlTILENCTLAPIWVrKMPKKQAEEVAMHFLKRVKIPEQ-ANKYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:PRK13631 118 VSMVFQfpEYQLFKD-TIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-252 |
2.50e-35 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 126.69 E-value: 2.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ-----KGKIVVDGTELTNDLKKIDEV 91
Cdd:PRK14258 7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 92 RREVGMVFQHFNLFPhLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRV----KIPEQANKYPGQLSGGQQQRVAIARSL 167
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDAdlwdEIKHKIHKSALDLSGGQQQRLCIARAL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 168 CMNPKIMLFDEPTSALDP--EMIKEVLDTMVGLAEEgMTMLCVTHEMGFARQVANRVIFMDQ-----GQIVEQNSPAEFF 240
Cdd:PRK14258 166 AVKPKVLLMDEPCFGLDPiaSMKVESLIQSLRLRSE-LTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIF 244
|
250
....*....|..
gi 502303547 241 DNPQHERTKLFL 252
Cdd:PRK14258 245 NSPHDSRTREYV 256
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-255 |
2.80e-35 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 132.67 E-value: 2.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 1 MAEAPAKKLTVSATEVAVEIVNM-----------NKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEH 69
Cdd:PRK10261 297 KQEPPIEQDTVVDGEPILQVRNLvtrfplrsgllNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVES 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 70 QKGKIVVDGTEL-TNDLKKIDEVRREVGMVFQ--HFNLFPHLTILENcTLAPIWVRKM-PKKQAEEVAMHFLKRVKI-PE 144
Cdd:PRK10261 377 QGGEIIFNGQRIdTLSPGKLQALRRDIQFIFQdpYASLDPRQTVGDS-IMEPLRVHGLlPGKAAAARVAWLLERVGLlPE 455
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 145 QANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVI 223
Cdd:PRK10261 456 HAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVA 535
|
250 260 270
....*....|....*....|....*....|..
gi 502303547 224 FMDQGQIVEQNSPAEFFDNPQHERTKLFLSQI 255
Cdd:PRK10261 536 VMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
24-231 |
3.19e-35 |
|
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: 125.46 E-value: 3.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 24 NKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCI-NRLEEHQ--KGKIVVDGTELtndlkKIDEVRREVGMVFQ 100
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGttSGQILFNGQPR-----KPDQFQKCVAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 101 HFNLFPHLTILENCTLAPIWV--RKMPKKQ-AEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03234 89 DDILLPGLTVRETLTYTAILRlpRKSSDAIrKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMG---FarQVANRVIFMDQGQIV 231
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIV 223
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-253 |
3.27e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 127.53 E-value: 3.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkkiDEVRR--- 93
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD------PEDRRrig 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 94 ----EVGmvfqhfnLFPHLTILENCT-LAPIwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLC 168
Cdd:COG4152 75 ylpeERG-------LYPKMKVGEQLVyLARL--KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 169 MNPKIMLFDEPTSALDP---EMIKEVLdtmVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDnpQH 245
Cdd:COG4152 146 HDPELLILDEPFSGLDPvnvELLKDVI---RELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR--QF 220
|
....*...
gi 502303547 246 ERTKLFLS 253
Cdd:COG4152 221 GRNTLRLE 228
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
31-231 |
6.97e-35 |
|
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: 131.91 E-value: 6.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNLFpHL 108
Cdd:TIGR03375 479 PALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGV----DIRQIDpaDLRRNIGYVPQDPRLF-YG 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILENCTLApiwvrkMPkkQAEEVAM-HFLKRVKIPEQANKYP----------GQ-LSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:TIGR03375 554 TLRDNIALG------AP--YADDEEIlRAAELAGVTEFVRRHPdgldmqigerGRsLSGGQRQAVALARALLRDPPILLL 625
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 177 DEPTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARQVaNRVIFMDQGQIV 231
Cdd:TIGR03375 626 DEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIV 678
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
32-232 |
1.77e-34 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 124.80 E-value: 1.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDEVRREVGMVFQH----FNlfP 106
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlNRAQRKAFRRDIQMVFQDsisaVN--P 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 -------------HLTILEnctlapiwvrkmpKKQAEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:PRK10419 105 rktvreiireplrHLLSLD-------------KAERLARASEMLRAVDLdDSVLDKRPPQLSGGQLQRVCLARALAVEPK 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:PRK10419 172 LLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
15-238 |
1.97e-34 |
|
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: 124.04 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRlEEHQ--KGKIVVDGTEL--TNdlkkIDE 90
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPtyGNDVRLFGERRggED----VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 91 VRREVGMV--FQHFNLFPHLTILEncTLAP-------IWVRkmPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRV 161
Cdd:COG1119 76 LRKRIGLVspALQLRFPRDETVLD--VVLSgffdsigLYRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 162 AIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEG-MTMLCVTH---EM--GFarqvaNRVIFMDQGQIVEQNS 235
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGI-----THVLLLKDGRVVAAGP 226
|
...
gi 502303547 236 PAE 238
Cdd:COG1119 227 KEE 229
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
13-233 |
2.86e-34 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 122.97 E-value: 2.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 13 ATEVAVEIVNMNKWYGD----FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkKI 88
Cdd:PRK10584 2 PAENIVEVHHLKKSVGQgeheLSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLH----QM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 89 DEVRR------EVGMVFQHFNLFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVA 162
Cdd:PRK10584 78 DEEARaklrakHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 163 IARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDqGQIVEQ 233
Cdd:PRK10584 157 LARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVN-GQLQEE 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
32-230 |
2.40e-33 |
|
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: 118.86 E-value: 2.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNLFPHlT 109
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGA----DISQWDpnELGDHVGYLPQDDELFSG-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCtlapiwvrkmpkkqaeevamhflkrvkipeqankypgqLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIK 189
Cdd:cd03246 92 IAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502303547 190 EVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQI 230
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
33-223 |
3.79e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.51 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCIN-RLEEH--QKGKIVVDGTELTndlkKIDEVRREVGMVFQHFNLFPHLT 109
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLT----ALPAEQRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLA-PiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMI 188
Cdd:COG4136 93 VGENLAFAlP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 502303547 189 KEVLD---TMVglAEEGMTMLCVTHEMGfARQVANRVI 223
Cdd:COG4136 170 AQFREfvfEQI--RQRGIPALLVTHDEE-DAPAAGRVL 204
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-238 |
6.32e-33 |
|
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: 125.30 E-value: 6.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 2 AEAPAKKLTVSATEVAVEIVNMNKWY-----GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIV- 75
Cdd:TIGR03269 264 VSEVEKECEVEVGEPIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNv 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 76 ------VDGTELTNDLKkiDEVRREVGMVFQHFNLFPHLTILENCTLApIWVrKMPKKQAEEVAMHFLKRVKIPEQA--- 146
Cdd:TIGR03269 344 rvgdewVDMTKPGPDGR--GRAKRYIGILHQEYDLYPHRTVLDNLTEA-IGL-ELPDELARMKAVITLKMVGFDEEKaee 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 147 --NKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVI 223
Cdd:TIGR03269 420 ilDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAA 499
|
250
....*....|....*
gi 502303547 224 FMDQGQIVEQNSPAE 238
Cdd:TIGR03269 500 LMRDGKIVKIGDPEE 514
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
32-238 |
9.17e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 119.84 E-value: 9.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT----NDLKKidevRREVgmVFQHFNL-FP 106
Cdd:COG4559 16 LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAawspWELAR----RRAV--LPQHSSLaFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 hLTILEnctlapiwVRKM-------PKKQAEEVAMHFLKRVKIPEQANK-YPgQLSGGQQQRVAIARSLC-------MNP 171
Cdd:COG4559 90 -FTVEE--------VVALgraphgsSAAQDRQIVREALALVGLAHLAGRsYQ-TLSGGEQQRVQLARVLAqlwepvdGGP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG4559 160 RWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
16-238 |
1.00e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.88 E-value: 1.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 16 VAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCI-NRLEEHQkGKIVVDGTELTnDLKKIDEVRRe 94
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPDS-GEVRLNGRPLA-DWSPAELARR- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 VGMVFQHFNL-FPhLTILEnctlapiwVRKM-------PKKQAEEVAMHFLKRVKIPEQANK-YPgQLSGGQQQRVAIAR 165
Cdd:PRK13548 78 RAVLPQHSSLsFP-FTVEE--------VVAMgraphglSRAEDDALVAAALAQVDLAHLAGRdYP-QLSGGEQQRVQLAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 166 SLC------MNPKIMLFDEPTSALDPEMIKEVLDTMVGLA-EEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
18-232 |
2.00e-32 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 123.64 E-value: 2.00e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVdGTELtndlkkidevrrEVGM 97
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHF-NLFPHLTILEnctlapiWVRKMPKKQAEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:COG0488 383 FDQHQeELDPDKTVLD-------ELRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLL 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 176 FDEPTSALDPEMIkEVLDTmvGLAE-EGmTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:COG0488 456 LDEPTNHLDIETL-EALEE--ALDDfPG-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
18-243 |
2.71e-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: 118.03 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEvRREVGM 97
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK--LPMHK-RARLGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VF--QHFNLFPHLTILENcTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:cd03218 78 GYlpQEASIFRKLTVEEN-ILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 176 FDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:cd03218 157 LDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANE 224
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
36-243 |
4.27e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 118.17 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 36 INLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdLKKIDEVRREVGMVFQHFNLFPHLTILENCT 115
Cdd:PRK11300 24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG-LPGHQIARMGVVRTFQHVRLFREMTVIENLL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 116 LA----------------PIWVRKmpKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEP 179
Cdd:PRK11300 103 VAqhqqlktglfsgllktPAFRRA--ESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEP 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 180 TSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PRK11300 181 AAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-250 |
5.42e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 118.26 E-value: 5.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdLKkidEVRRE--VGMVFQHFNL--FP 106
Cdd:COG1101 20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK-LP---EYKRAkyIGRVFQDPMMgtAP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLA-------------PIWVRKMPKKQAEEVAMHFLKRVKIPEqankypGQLSGGQQQrvaiARSLCM---- 169
Cdd:COG1101 96 SMTIEENLALAyrrgkrrglrrglTKKRRELFRELLATLGLGLENRLDTKV------GLLSGGQRQ----ALSLLMatlt 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 170 NPKIMLFDEPTSALDPEMIKEVLD-TMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVeqnspaefFDNPQHERT 248
Cdd:COG1101 166 KPKLLLLDEHTAALDPKTAALVLElTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII--------LDVSGEEKK 237
|
..
gi 502303547 249 KL 250
Cdd:COG1101 238 KL 239
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
32-252 |
6.07e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.51 E-value: 6.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL-----EEHQKGKIVVDGTELTN-DLKKIDEVR-REVGMVFQH--F 102
Cdd:PRK15134 24 VVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHaSEQTLRGVRgNKIAMIFQEpmV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 103 NLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANK---YPGQLSGGQQQRVAIARSLCMNPKIMLFDEP 179
Cdd:PRK15134 104 SLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADEP 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 180 TSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFL 252
Cdd:PRK15134 184 TTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
33-240 |
7.45e-32 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 118.30 E-value: 7.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN--DLKKIDEVRREVGMVFQhfnlFPHLTI 110
Cdd:PRK13643 22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStsKQKEIKPVRKKVGVVFQ----FPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLAPIWVRK----MPKKQAEEVAMHFLKRVKIPEQA-NKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:PRK13643 98 FEETVLKDVAFGPqnfgIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 186 EMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
31-253 |
9.41e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.12 E-value: 9.41e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQkGKIVVDGTELTN-DLKKIDEVRREVGMVFQHFN--LFPH 107
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNlNRRQLLPVRHRIQVVFQDPNssLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 108 LTILEncTLAP---IWVRKMPKKQAEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:PRK15134 379 LNVLQ--IIEEglrVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 184 DPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLS 253
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
12-241 |
4.97e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 117.24 E-value: 4.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 12 SATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlKKIDEV 91
Cdd:PRK13536 36 SMSTVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP---ARARLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 92 RREVGMVFQHFNLFPHLTILENCTLAPIWVRkMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFG-MSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDP 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:PRK13536 192 QLLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-238 |
5.77e-31 |
|
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: 120.31 E-value: 5.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 2 AEAP-AKKLTVSATEVAVEIVnmnkwygDFH------VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKI 74
Cdd:COG5265 343 ADAPdAPPLVVGGGEVRFENV-------SFGydperpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRI 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 75 VVDGTeltnDLKKI--DEVRREVGMVFQHFNLFpHLTILEN-------CTLAPIW-----------VRKMPKKQAEEVAM 134
Cdd:COG5265 416 LIDGQ----DIRDVtqASLRAAIGIVPQDTVLF-NDTIAYNiaygrpdASEEEVEaaaraaqihdfIESLPDGYDTRVGE 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 135 HFLKrvkipeqankypgqLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHemgf 214
Cdd:COG5265 491 RGLK--------------LSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH---- 551
|
250 260
....*....|....*....|....*...
gi 502303547 215 aR----QVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG5265 552 -RlstiVDADEILVLEAGRIVERGTHAE 578
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
27-252 |
6.92e-31 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 116.76 E-value: 6.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGD----FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHqKGKIVVDGTELTN-DLKKIDEVRR------EV 95
Cdd:PRK11022 13 FGDesapFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGqDLQRISEKERrnlvgaEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQH--FNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANK---YPGQLSGGQQQRVAIARSLCMN 170
Cdd:PRK11022 92 AMIFQDpmTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACR 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 171 PKIMLFDEPTSALDPEMIKEVLDTMVGLAE-EGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTK 249
Cdd:PRK11022 172 PKLLIADEPTTALDVTIQAQIIELLLELQQkENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQ 251
|
...
gi 502303547 250 LFL 252
Cdd:PRK11022 252 ALL 254
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
32-236 |
9.68e-31 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 113.74 E-value: 9.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNLFPHlT 109
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGV----DISKIGlhDLRSRISIIPQDPVLFSG-T 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENctLAPIwvrkmpKKQAEEVAMHFLKRVKIPEQANKYPGQL-----------SGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:cd03244 94 IRSN--LDPF------GEYSDEELWQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 179 PTSALDPE---MIKEVLDTmvglAEEGMTMLCVTHE----MGFarqvaNRVIFMDQGQIVEQNSP 236
Cdd:cd03244 166 ATASVDPEtdaLIQKTIRE----AFKDCTVLTIAHRldtiIDS-----DRILVLDKGRVVEFDSP 221
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
18-231 |
2.34e-30 |
|
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: 112.46 E-value: 2.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGD----FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtndLKKIDEVRR 93
Cdd:cd03266 2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV---VKEPAEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 94 EVGMVFQHFNLFPHLTILENCT-------LApiwvRKMPKKQAEEVAmhflKRVKIPEQANKYPGQLSGGQQQRVAIARS 166
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEyfaglygLK----GDELTARLEELA----DRLGMEELLDRRVGGFSTGMRQKVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 167 LCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:cd03266 151 LVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
33-255 |
4.24e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 118.03 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRR------------EVGMVFQ 100
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELSEqsaaqmrhvrgaDMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 101 H--FNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQA---NKYPGQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 176 FDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLSQ 254
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLAA 271
|
.
gi 502303547 255 I 255
Cdd:PRK10261 272 V 272
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
10-231 |
4.51e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 117.04 E-value: 4.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 10 TVSATEVAVEIVNMNKWygdfHVLRDINLKVMRGErIV-IAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndLKKI 88
Cdd:COG1129 249 AAAPGEVVLEVEGLSVG----GVVRDVSFSVRAGE-ILgIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSP 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 89 DEVRREvGMVF-----QHFNLFPHLTILENCTLAPI----WVRKMPKKQAEEVAMHFLKRVKI----PEQAnkyPGQLSG 155
Cdd:COG1129 322 RDAIRA-GIAYvpedrKGEGLVLDLSIRENITLASLdrlsRGGLLDRRRERALAEEYIKRLRIktpsPEQP---VGNLSG 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 156 GQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:COG1129 398 GNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-225 |
6.17e-30 |
|
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: 117.00 E-value: 6.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 3 EAPAKKLTVSATEVAVEivnmnkwyGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT 82
Cdd:TIGR02857 316 AAPASSLEFSGVSVAYP--------GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 83 nDLKKiDEVRREVGMVFQHFNLFPHlTILENCTLA-PIWVRKMPKKQAEEVAMHFLKRVkIPEQANKYPGQ----LSGGQ 157
Cdd:TIGR02857 388 -DADA-DSWRDQIAWVPQHPFLFAG-TIAENIRLArPDASDAEIREALERAGLDEFVAA-LPQGLDTPIGEggagLSGGQ 463
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 158 QQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHEMGFARqVANRVIFM 225
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALA-QGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
26-210 |
7.41e-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: 116.69 E-value: 7.41e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 26 WYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQHFNLF 105
Cdd:TIGR02868 344 YPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVSVCAQDAHLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 pHLTILENCTLApiwvrkmpKKQA-EEVAMHFLKRVKIPEQANKYPG-----------QLSGGQQQRVAIARSLCMNPKI 173
Cdd:TIGR02868 422 -DTTVRENLRLA--------RPDAtDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGlAEEGMTMLCVTH 210
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
48-231 |
1.04e-29 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 114.20 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 48 IAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKID---EVRReVGMVFQHFNLFPHLTILENCTLApiwvrkM 124
Cdd:PRK11144 29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIClppEKRR-IGYVFQDARLFPHYKVRGNLRYG------M 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 125 PKKQAEE----VAM----HFLKRvkipeqankYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMV 196
Cdd:PRK11144 102 AKSMVAQfdkiVALlgiePLLDR---------YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLE 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 502303547 197 GLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:PRK11144 173 RLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
32-243 |
2.74e-29 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 115.97 E-value: 2.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKIDEV--RREVGMVFQHFNLFPHlT 109
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGV----PLVQYDHHylHRQVALVGQEPVLFSG-S 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLApiwVRKMPKKQAEEVAMHFLKRVKIPEQANKYP-------GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:TIGR00958 571 VRENIAYG---LTDTPDEEIMAAAKAANAHDFIMEFPNGYDtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 183 LDPEMIKEVLDTMvglAEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:TIGR00958 648 LDAECEQLLQESR---SRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
33-235 |
2.96e-29 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 115.44 E-value: 2.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKI--DEVRREVGMVFQHFNLFPHlTI 110
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGT----DIRTVtrASLRRNIAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENctlapIWVRKmPKKQAEEV--------AMHFLKRvkipeQANKYP-------GQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:PRK13657 426 EDN-----IRVGR-PDATDEEMraaaeraqAHDFIER-----KPDGYDtvvgergRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 176 FDEPTSALDPEM---IKEVLDTMVglaeEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNS 235
Cdd:PRK13657 495 LDEATSALDVETeakVKAALDELM----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
33-244 |
3.24e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 111.00 E-value: 3.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKidEVRREVGMVFQH-FNLFPHLTI- 110
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE--KLRKHIGIVFQNpDNQFVGSIVk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 ------LENctlapiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:PRK13648 103 ydvafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 185 PEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-231 |
3.60e-29 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 109.58 E-value: 3.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 26 WYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdLKK--IDEVRREVGMVFQHFN 103
Cdd:PRK10908 11 YLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITR-LKNreVPFLRRQIGMIFQDHH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 104 LFPHLTILENCTLaPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:PRK10908 90 LLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502303547 184 DPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:PRK10908 169 DDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
29-233 |
6.79e-29 |
|
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: 107.78 E-value: 6.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlkKIDEVRREVGMVFQHFNLFpHL 108
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD---LEKALSSLISVLNQRPYLF-DT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILENctlapiwvrkmpkkqaeevamhfLKRvkipeqankypgQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMI 188
Cdd:cd03247 90 TLRNN-----------------------LGR------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITE 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 502303547 189 KEVLDTMVGLAEEgMTMLCVTHEM-GFARqvANRVIFMDQGQIVEQ 233
Cdd:cd03247 135 RQLLSLIFEVLKD-KTLIWITHHLtGIEH--MDKILFLENGKIIMQ 177
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
32-230 |
9.67e-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: 107.13 E-value: 9.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndLKKIDEVRREvGMVF-----QHFNLFP 106
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVT--RRSPRDAIRA-GIAYvpedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLapiwvrkmpkkqaeevamhflkrvkipeqankyPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPE 186
Cdd:cd03215 92 DLSVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 502303547 187 MIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
19-256 |
1.05e-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: 108.64 E-value: 1.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT-NDLKKIdevrrevGM 97
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTrKDLHKI-------GS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILEN----CTLapiwvRKMPKKQAEEVamhfLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:TIGR03740 75 LIESPPLYENLTARENlkvhTTL-----LGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSpaeffDNPQHERTKLFLS 253
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK-----INKSENLEKLFVE 220
|
...
gi 502303547 254 QIL 256
Cdd:TIGR03740 221 VVK 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
18-255 |
1.99e-28 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 109.08 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTEL-TNDLKKIDEVRREVG 96
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpAMSRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 177 DEPTSALDPemikEVLDTMVGLAEE-----GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHeRTKLF 251
Cdd:PRK11831 168 DEPFVGQDP----ITMGVLVKLISElnsalGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDP-RVRQF 242
|
....
gi 502303547 252 LSQI 255
Cdd:PRK11831 243 LDGI 246
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-240 |
2.81e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 108.64 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlkKIDEVRREVGMVFQH-FNLFPH 107
Cdd:PRK13642 19 DVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAE--NVWNLRRKIGMVFQNpDNQFVG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 108 LTILENCTLApIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEM 187
Cdd:PRK13642 97 ATVEDDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502303547 188 IKEVLDTMVGLAEE-GMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK13642 176 RQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
22-250 |
3.05e-28 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 107.67 E-value: 3.05e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 22 NMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdLKKIDEVRREVGMVFQH 101
Cdd:PRK10895 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-LPLHARARRGIGYLPQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 102 FNLFPHLTILENcTLAPIWVRK-MPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPT 180
Cdd:PRK10895 87 ASIFRRLSVYDN-LMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 181 SALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKL 250
Cdd:PRK10895 166 AGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYL 235
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
10-235 |
3.57e-28 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 112.23 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 10 TVSATEVAVEIVNMNKWYGD--FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKK 87
Cdd:PRK11160 331 TAAADQVSLTLNNVSFTYPDqpQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQ----PIAD 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 88 IDE--VRREVGMVFQHFNLFPHlTILENCTLApiwvrkmpKKQA-EEVAMHFLKRVKIPEQANKYPG----------QLS 154
Cdd:PRK11160 407 YSEaaLRQAISVVSQRVHLFSA-TLRDNLLLA--------APNAsDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLS 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 155 GGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAeEGMTMLCVTHemgfaRQVA----NRVIFMDQGQI 230
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITH-----RLTGleqfDRICVMDNGQI 551
|
....*
gi 502303547 231 VEQNS 235
Cdd:PRK11160 552 IEQGT 556
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
27-238 |
1.03e-27 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 106.99 E-value: 1.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKidEVRREVGMVFQHFNLFP 106
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASK--EVARRIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLA-----PIWVRKmpKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTS 181
Cdd:PRK10253 95 DITVQELVARGryphqPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 182 ALDPEMIKEVLDTMVGL-AEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:PRK10253 173 WLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
27-238 |
1.63e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 106.25 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltNDLKKIDEvrREVGmvfQHFNLFP 106
Cdd:PRK11231 12 YGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGD----KPISMLSS--RQLA---RRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 -HLTILENCTLA-----------PIWVRKMPKKQAE-EVAMHflkRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:PRK11231 83 qHHLTPEGITVRelvaygrspwlSLWGRLSAEDNARvNQAME---QTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
16-242 |
2.57e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 105.35 E-value: 2.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 16 VAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTnDLKKIDEVRREV 95
Cdd:PRK11614 4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT-DWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKipEQANKYPGQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLH--ERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 176 FDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-241 |
4.47e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 106.04 E-value: 4.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 13 ATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlKKIDEVR 92
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP---SRARHAR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVGMVFQHFNLFPHLTILENCTlapIWVR--KMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMN 170
Cdd:PRK13537 80 QRVGVVPQFDNLDPDFTVRENLL---VFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 171 PKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
18-238 |
4.85e-27 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 104.78 E-value: 4.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGM 97
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVAT--TPSRELAKRLAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQ--HFNL------------FPH----LTilenctlapiwvrkmpkKQAEEV---AMHFLKrvkIPEQANKYPGQLSGG 156
Cdd:COG4604 80 LRQenHINSrltvrelvafgrFPYskgrLT-----------------AEDREIideAIAYLD---LEDLADRYLDELSGG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 157 QQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNS 235
Cdd:COG4604 140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGT 219
|
...
gi 502303547 236 PAE 238
Cdd:COG4604 220 PEE 222
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-249 |
6.86e-27 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 104.87 E-value: 6.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNK-------WYGDFHV--LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDL 85
Cdd:PRK15112 2 ETLLEVRNLSKtfryrtgWFRRQTVeaVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 86 KKIDEVRreVGMVFQ--HFNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKI-PEQANKYPGQLSGGQQQRVA 162
Cdd:PRK15112 82 YSYRSQR--IRMIFQdpSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 163 IARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
....*...
gi 502303547 242 NPQHERTK 249
Cdd:PRK15112 240 SPLHELTK 247
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
27-238 |
6.91e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.01 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlkkidevrR-----EVGMVFQh 101
Cdd:COG1134 36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG--------------RvsallELGAGFH- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 102 fnlfPHLTILENCTL-APIWvrKMPKKQAE----------EVAMHFLKRVKipeqankypgQLSGGQQQRVAIARSLCMN 170
Cdd:COG1134 101 ----PELTGRENIYLnGRLL--GLSRKEIDekfdeivefaELGDFIDQPVK----------TYSSGMRARLAFAVATAVD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 171 PKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG1134 165 PDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
19-244 |
7.84e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.96 E-value: 7.84e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGErIV-IAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDE-VRREVG 96
Cdd:COG1137 5 EAENLVKSYGKRTVVKDVSLEVNQGE-IVgLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITH--LPMHKrARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHLTILENcTLAPIWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:COG1137 82 YLPQEASIFRKLTVEDN-ILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 177 DEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEmgfAR---QVANRVIFMDQGQIVEQNSPAEFFDNPQ 244
Cdd:COG1137 161 DEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHN---VRetlGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-242 |
1.33e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.83 E-value: 1.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIrciNRLEEHQKGKIVVDGTELTNDlKKID--EVRREVGMVFQHFNLFPHL 108
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLLNG-MPIDakEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILENCTLA-----PiwvRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQ------LSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:TIGR00955 115 TVREHLMFQahlrmP---RRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTH-------EMgFarqvaNRVIFMDQGQIVEQNSP---AEFFDN 242
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPdqaVPFFSD 260
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-230 |
1.95e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 107.07 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 22 NMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDgteltNDLKkidevrreVGMVFQH 101
Cdd:COG0488 3 NLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-----KGLR--------IGYLPQE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 102 FNLFPHLTILENCT--LAPIWvRKMPKKQAEEVAMHF------------------------------LKRVKIP-EQANK 148
Cdd:COG0488 70 PPLDDDLTVLDTVLdgDAELR-ALEAELEELEAKLAEpdedlerlaelqeefealggweaearaeeiLSGLGFPeEDLDR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 149 YPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIkEVLDTMvgLAEEGMTMLCVTHEMGFARQVANRVIFMDQG 228
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESI-EWLEEF--LKNYPGTVLVVSHDRYFLDRVATRILELDRG 225
|
..
gi 502303547 229 QI 230
Cdd:COG0488 226 KL 227
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
27-216 |
2.98e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.16 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltndlkkidevrREVGMVFQHFNL-- 104
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG-------------ARVAYVPQRSEVpd 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 -FPhLTILENCTLApIWVRKMP----KKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEP 179
Cdd:NF040873 69 sLP-LTVRDLVAMG-RWARRGLwrrlTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 502303547 180 TSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFAR 216
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARGATVVVVTHDLELVR 183
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
34-253 |
4.29e-26 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 102.47 E-value: 4.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 34 RDINLKVMRGERIVIAGPSGSGKStmIRCINRLE------EHQKGKIVVDGTELT-NDLKKidevrREVGMVFQH----F 102
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagvRQTAGRVLLDGKPVApCALRG-----RKIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 103 NlfPHLTI----LENCtlapiwvRKMPKKQAEEVAMHFLKRVKIPEQA---NKYPGQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:PRK10418 93 N--PLHTMhthaRETC-------LALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 176 FDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKLFLS 253
Cdd:PRK10418 164 ADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVS 242
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
28-245 |
4.46e-26 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 104.04 E-value: 4.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRL---EEHQKGKIVVDGTELTN-DLKKIDEVRRE-VGMVFQH- 101
Cdd:PRK09473 27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLlaaNGRIGGSATFNGREILNlPEKELNKLRAEqISMIFQDp 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 102 -FNLFPHLTILENCTLAPIWVRKMPKKQAEEVAMHFLKRVKIPE---QANKYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQH 245
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSH 255
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-238 |
8.71e-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: 105.27 E-value: 8.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ--KGKIV-------------------- 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 76 ---VDGTELTN---DLKKIDE-----VRREVGMVFQH-FNLFPHLTILENcTLAPIWVRKMPKKQAEEVAMHFLKRVKIP 143
Cdd:TIGR03269 81 pcpVCGGTLEPeevDFWNLSDklrrrIRKRIAIMLQRtFALYGDDTVLDN-VLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 144 EQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMV-GLAEEGMTMLCVTHEMGFARQVANRV 222
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEeAVKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|....*.
gi 502303547 223 IFMDQGQIVEQNSPAE 238
Cdd:TIGR03269 240 IWLENGEIKEEGTPDE 255
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
27-235 |
8.83e-26 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 105.59 E-value: 8.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDfHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNL 104
Cdd:TIGR01193 485 YGS-NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGF----SLKDIDrhTLRQFINYLPQEPYI 559
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 FPHlTILENCTLApiwvrKMPKKQAEEVaMHFLKRVKIPEQANKYP-----------GQLSGGQQQRVAIARSLCMNPKI 173
Cdd:TIGR01193 560 FSG-SILENLLLG-----AKENVSQDEI-WAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEgmTMLCVTHEMGFARQVaNRVIFMDQGQIVEQNS 235
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
33-238 |
1.97e-25 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 104.33 E-value: 1.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtNDLKkIDEVRREVGMVFQHFNLFpHLTILE 112
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL-RDYT-LASLRNQVALVSQNVHLF-NDTIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 113 NCTLAPiwVRKMPKKQAEEVA-----MHFLKrvKIPEQANKYPGQ----LSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:PRK11176 436 NIAYAR--TEQYSREQIEEAArmayaMDFIN--KMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSAL 511
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 184 DPE---MIKEVLDTMvglaEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAE 238
Cdd:PRK11176 512 DTEserAIQAALDEL----QKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
18-229 |
4.57e-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: 96.75 E-value: 4.57e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDgteltndlkkidevrrevgm 97
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG-------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 vfqhfnlfphltilenctlapiwvrkmpkkqaeevamhflKRVKIPeqankYPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03221 61 ----------------------------------------STVKIG-----YFEQLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502303547 178 EPTSALDPEMIKEVLDtmvGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQ 229
Cdd:cd03221 96 EPTNHLDLESIEALEE---ALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
18-231 |
1.78e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.40 E-value: 1.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtNDLKKIDEVRREVGM 97
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINY-NKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLAPIWVRK------MPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:PRK09700 165 KVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSV 224
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
36-238 |
3.08e-24 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 101.07 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 36 INLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQkGKIVVDGTELTN-DLKkidEVRREVGMVFQHFNLFpHLTILENC 114
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRElDPE---SWRKHLSWVGQNPQLP-HGTLRDNV 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 115 TLApiwvrkmpKKQA-EEVAMHFLKRVKIPEQANKYP-----------GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:PRK11174 444 LLG--------NPDAsDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 183 LDPEMIKEVLDTMvGLAEEGMTMLCVTHEMGFARQVaNRVIFMDQGQIVEQNSPAE 238
Cdd:PRK11174 516 LDAHSEQLVMQAL-NAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
32-231 |
3.65e-24 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 100.59 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DlkkIDEVRREVGMVFQHFNLFPHlTI 110
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwD---REELGRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENctlapiwVRKMPKKQAEEV-------AMHFLkrvkIPEQANKY-------PGQLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:COG4618 423 AEN-------IARFGDADPEKVvaaaklaGVHEM----ILRLPDGYdtrigegGARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 177 DEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGfARQVANRVIFMDQGQIV 231
Cdd:COG4618 492 DEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQ 545
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
27-232 |
4.62e-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: 96.06 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeLTNDLkkidevrrEVGMVFQhfnlfP 106
Cdd:cd03220 32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGR-VSSLL--------GLGGGFN-----P 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILEN----CTLAPIWVRKMPKKQAE-----EVAMHFLKRVKipeqankypgQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03220 98 ELTGRENiylnGRLLGLSRKEIDEKIDEiiefsELGDFIDLPVK----------TYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
29-230 |
4.90e-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: 96.39 E-value: 4.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndLKKIDEVRREVGMVFQHFNLFPHl 108
Cdd:cd03248 26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS--QYEHKYLHSKVSLVGQEPVLFAR- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILENCTLApiwVRKMPKKQAEEVAMHFLKRVKIPEQANKYP-------GQLSGGQQQRVAIARSLCMNPKIMLFDEPTS 181
Cdd:cd03248 103 SLQDNIAYG---LQSCSFECVKEAAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATS 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 502303547 182 ALDPEMiKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQI 230
Cdd:cd03248 180 ALDAES-EQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
28-211 |
1.07e-23 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 95.17 E-value: 1.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQHFNLFPH 107
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDIST--LKPEIYRQQVSYCAQTPTLFGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 108 lTILENCTLaPIWVRkmpKKQAEEVAM-HFLKRVKIPEQA-NKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:PRK10247 96 -TVYDNLIF-PWQIR---NQQPDPAIFlDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170
|
170 180
....*....|....*....|....*..
gi 502303547 186 EMIKEVLDTMVGLAEE-GMTMLCVTHE 211
Cdd:PRK10247 171 SNKHNVNEIIHRYVREqNIAVLWVTHD 197
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
19-232 |
3.04e-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: 93.36 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ--KGKIVVDGTELTNdlKKIDE-VRREV 95
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEvtEGEILFKGEDITD--LPPEErARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLTIlenctlapiwvrkmpkkqaeevaMHFLKRVkipeqaNKypgQLSGGQQQRVAIARSLCMNPKIML 175
Cdd:cd03217 80 FLAFQYPPEIPGVKN-----------------------ADFLRYV------NE---GFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 176 FDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTH-EMGFARQVANRVIFMDQGQIVE 232
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVK 185
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
32-236 |
4.40e-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: 93.25 E-value: 4.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltnDLKKID--EVRREVGMVFQHFNLFPHlT 109
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----DISTIPleDLRSSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENctLAPIwvrkmpKKQAEEVAMHFLkrvKIPEQANkypgQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPE--- 186
Cdd:cd03369 98 IRSN--LDPF------DEYSDEEIYGAL---RVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAtda 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502303547 187 MIKEVLDTMVglaeEGMTMLCVTHEMgfaRQVA--NRVIFMDQGQIVEQNSP 236
Cdd:cd03369 163 LIQKTIREEF----TNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
5-232 |
8.80e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 96.78 E-value: 8.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 5 PAKKLTVS--ATEVAVEIVNMNKWygDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT 82
Cdd:PRK09700 251 NAMKENVSnlAHETVFEVRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDIS 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 83 -----NDLKK----IDEVRREVGmvfqhfnLFPHLTILENCTLAP------------IWVRKMPKKQAE-EVAMHFLKRV 140
Cdd:PRK09700 329 prsplDAVKKgmayITESRRDNG-------FFPNFSIAQNMAISRslkdggykgamgLFHEVDEQRTAEnQRELLALKCH 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 141 KIpeqaNKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVAN 220
Cdd:PRK09700 402 SV----NQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCD 477
|
250
....*....|..
gi 502303547 221 RVIFMDQGQIVE 232
Cdd:PRK09700 478 RIAVFCEGRLTQ 489
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
43-225 |
1.50e-22 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 96.49 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 43 GERIVIAGPSGSGKSTMIRCI-NRLEEHQkgkivVDGTELTNDLKKIDEVRREVGMVFQHFNLFPHLTILEncTLAPIWV 121
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALaGRIQGNN-----FTGTILANNRKPTKQILKRTGFVTQDDILYPHLTVRE--TLVFCSL 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 122 RKMPKKQAEEVAMHFLKRVkIPEQA----------NKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEV 191
Cdd:PLN03211 167 LRLPKSLTKQEKILVAESV-ISELGltkcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
|
170 180 190
....*....|....*....|....*....|....
gi 502303547 192 LDTMVGLAEEGMTMLCVTHemgfarQVANRVIFM 225
Cdd:PLN03211 246 VLTLGSLAQKGKTIVTSMH------QPSSRVYQM 273
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
32-229 |
2.67e-22 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 90.99 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCInrLEE--HQKGKIVVDGTE--------LTND--------LKKIDEVR- 92
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL--LGEleKLSGSVSVPGSIayvsqepwIQNGtirenilfGKPFDEERy 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 93 REVgmvfqhfnlfphltiLENCTLAPIwVRKMPKKQAEEVamhflkrvkipeqankypGQ----LSGGQQQRVAIARSLC 168
Cdd:cd03250 98 EKV---------------IKACALEPD-LEILPDGDLTEI------------------GEkginLSGGQKQRISLARAVY 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 169 MNPKIMLFDEPTSALDPEMIKEVLDTMV-GLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQ 229
Cdd:cd03250 144 SDADIYLLDDPLSAVDAHVGRHIFENCIlGLLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
32-230 |
1.41e-21 |
|
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: 93.18 E-value: 1.41e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN-DLKKIDevrREVGMVFQHFNLFPHlTI 110
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFG---KHIGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTlapiwvRKMPKKQAEEV-------AMHFLKrVKIPEQANKYPGQ----LSGGQQQRVAIARSLCMNPKIMLFDEP 179
Cdd:TIGR01842 409 AENIA------RFGENADPEKIieaaklaGVHELI-LRLPDGYDTVIGPggatLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 502303547 180 TSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGfARQVANRVIFMDQGQI 230
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-238 |
9.61e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 9.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 10 TVSATEVAVEivnmnkwYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKid 89
Cdd:PRK09536 3 MIDVSDLSVE-------FGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSAR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 90 EVRREVGMVFQH----FNL----------FPHLTILENCTLApiwvrkmpKKQAEEVAMhflKRVKIPEQANKYPGQLSG 155
Cdd:PRK09536 74 AASRRVASVPQDtslsFEFdvrqvvemgrTPHRSRFDTWTET--------DRAAVERAM---ERTGVAQFADRPVTSLSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 156 GQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNS 235
Cdd:PRK09536 143 GERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGP 222
|
...
gi 502303547 236 PAE 238
Cdd:PRK09536 223 PAD 225
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
32-210 |
1.52e-20 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 90.25 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVV-DGTELtndlkkidevrrevgmvfqhfnLF----P 106
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------------LFlpqrP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILencTLA-----PIWVRKMPKKQAEEVamhfLKRVKIP-------EQANkYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:COG4178 436 YLPLG---TLReallyPATAEAFSDAELREA----LEAVGLGhlaerldEEAD-WDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190
....*....|....*....|....*....|....*...
gi 502303547 175 LFDEPTSALDPEMIKEVLDTmvgLAEE--GMTMLCVTH 210
Cdd:COG4178 508 FLDEATSALDEENEAALYQL---LREElpGTTVISVGH 542
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
36-236 |
8.63e-20 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.53 E-value: 8.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 36 INLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLkkiDEVRREVGMVFQHFNLFPHLTILENCT 115
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNL---DAVRQSLGMCPQHNILFHHLTVAEHIL 1025
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 116 L-APIWVRKMPKKQAEEVAMhfLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDT 194
Cdd:TIGR01257 1026 FyAQLKGRSWEEAQLEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDL 1103
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502303547 195 MVGLaEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSP 236
Cdd:TIGR01257 1104 LLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
32-210 |
1.01e-19 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 82.97 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlkkidevRREVGMVFQHfnlfPHLTIL 111
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPE-------------GEDLLFLPQR----PYLPLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 encTLApiwvrkmpkkqaEEVAmhflkrvkipeqankYPGQ--LSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIK 189
Cdd:cd03223 79 ---TLR------------EQLI---------------YPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|.
gi 502303547 190 EVLDTmvgLAEEGMTMLCVTH 210
Cdd:cd03223 129 RLYQL---LKELGITVISVGH 146
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
30-210 |
2.32e-19 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 83.47 E-value: 2.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 30 FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDgteltndlkkidevrrevgmvfqhfnlFPHLT 109
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVD---------------------------VPDNQ 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLAPIWVRKMPKKQAEEVamhfLKRVKIPEQAN--KYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEM 187
Cdd:COG2401 96 FGREASLIDAIGRKGDFKDAVEL----LNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171
|
170 180
....*....|....*....|....
gi 502303547 188 IKEVLDTMVGLAEE-GMTMLCVTH 210
Cdd:COG2401 172 AKRVARNLQKLARRaGITLVVATH 195
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
32-238 |
5.17e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.85 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGErIV-IAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEvRREVGMVF-----QHFNLF 105
Cdd:COG3845 273 ALKDVSLEVRAGE-ILgIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG--LSPRE-RRRLGVAYipedrLGRGLV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 PHLTILENCTLAPIWVRKMPK------KQAEEVAMHFLKR--VKIPEQANKyPGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:COG3845 349 PDMSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEfdVRTPGPDTP-ARSLSGGNQQKVILARELSRDPKLLIAA 427
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG3845 428 QPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
18-244 |
1.35e-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: 84.49 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEH--QKGKIVVDGTELTNDLKKiDEVRREV 95
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHgtWDGEIYWSGSPLKASNIR-DTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLTILENCTLAPIWVRKMPKKQAEEV---AMHFLKRVKIPEQANKYP-GQLSGGQQQRVAIARSLCMNP 171
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMylrAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVeQNSPAEFFDNPQ 244
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV-ATKDMSTMSEDD 232
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
32-232 |
2.45e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 81.27 E-value: 2.45e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ--KGKIVVDGTELTNdlKKIDE-VRREVGMVFQH------- 101
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDILE--LSPDErARAGIFLAFQYpveipgv 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 102 --FNLFphLTILENCTLAPIWVRKMpKKQAEEVAmhflKRVKIPEQ-ANKY--PGqLSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:COG0396 93 svSNFL--RTALNARRGEELSAREF-LKLLKEKM----KELGLDEDfLDRYvnEG-FSGGEKKRNEILQMLLLEPKLAIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 177 DEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHemgFAR----QVANRVIFMDQGQIVE 232
Cdd:COG0396 165 DETDSGLDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVK 221
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
19-210 |
2.96e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.44 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEH--QKGKIVVDGTELTndLKKI-DEVRREV 95
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHgtYEGEIIFEGEELQ--ASNIrDTERAGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLTILENCTLAPIWVRK--MPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:PRK13549 85 AIIHQELALVKELSVLENIFLGNEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARL 164
|
170 180 190
....*....|....*....|....*....|....*..
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTH 210
Cdd:PRK13549 165 LILDEPTASLTESETAVLLDIIRDLKAHGIACIYISH 201
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
27-240 |
4.06e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 81.21 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGMVFQHfnlfP 106
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTI------------LENCTLAPIWV-RKMPKKQAEEVAMHFLKRvkiPEQAnkypgqLSGGQQQRVAIARSLCMNPKI 173
Cdd:PRK13638 87 EQQIfytdidsdiafsLRNLGVPEAEItRRVDEALTLVDAQHFRHQ---PIQC------LSHGQKKRVAIAGALVLQARY 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFF 240
Cdd:PRK13638 158 LLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-238 |
4.79e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 80.65 E-value: 4.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHV---LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQkGKIVVDGTELtNDLKKIDEVRREV---------- 95
Cdd:COG4138 5 DVAVagrLGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPL-SDWSAAELARHRAylsqqqsppf 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GM-VFQHFNLFPHltilenctlapiwvRKMPKKQAEEVAMHFLKRVKIpeqANKYP---GQLSGGQQQRVAIARSLC--- 168
Cdd:COG4138 83 AMpVFQYLALHQP--------------AGASSEAVEQLLAQLAEALGL---EDKLSrplTQLSGGEWQRVRLAAVLLqvw 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 169 --MNP--KIMLFDEPTSALDpemI--KEVLDTMVG-LAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:COG4138 146 ptINPegQLLLLDEPMNSLD---VaqQAALDRLLReLCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
15-230 |
5.83e-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: 82.57 E-value: 5.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNKWYGD-FHVLR--DINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ-KGKIVVDGTELtnDLKK-ID 89
Cdd:TIGR02633 255 DVILEARNLTCWDVInPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPV--DIRNpAQ 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 90 EVRREVGMV---FQHFNLFPHLTILENCTLAPI--WVRKMPKKQAEE--VAMHFLKRVKIPEQANKYP-GQLSGGQQQRV 161
Cdd:TIGR02633 333 AIRAGIAMVpedRKRHGIVPILGVGKNITLSVLksFCFKMRIDAAAElqIIGSAIQRLKVKTASPFLPiGRLSGGNQQKA 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 162 AIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:TIGR02633 413 VLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
32-239 |
6.80e-18 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 83.07 E-value: 6.80e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQHFNLFP----- 106
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK--IGLHDLRFKITIIPQDPVLFSgslrm 1378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLAPIWVrkmpkkqAEEVAmHFLKRV-----KIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTS 181
Cdd:TIGR00957 1379 NLDPFSQYSDEEVWW-------ALELA-HLKTFVsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 502303547 182 ALDPE---MIKEVLDTMVglaeEGMTMLCVTHEMGFARQVaNRVIFMDQGQIVEQNSPAEF 239
Cdd:TIGR00957 1451 AVDLEtdnLIQSTIRTQF----EDCTVLTIAHRLNTIMDY-TRVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
35-230 |
7.09e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 35 DINLKVMRGERIVIAGPSGSGKSTMIRCI-----NRLEehqkGKIVVDGTELT--NDLKKID-------EVRREVGMVfq 100
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfgaypGRWE----GEIFIDGKPVKirNPQQAIAqgiamvpEDRKRDGIV-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 101 hfnlfPHLTILENCTLAPI---WVRKMPKKQAEE-VAMHFLKRVKI----PEQAnkyPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:PRK13549 354 -----PVMGVGKNITLAALdrfTGGSRIDDAAELkTILESIQRLKVktasPELA---IARLSGGNQQKAVLAKCLLLNPK 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:PRK13549 426 ILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
32-210 |
9.07e-18 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 79.15 E-value: 9.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlkKIDEVRREVGmvfqHFN-LFPHLTI 110
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDP--DVAEACHYLG----HRNaMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLapiWVRKmpKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKE 190
Cdd:PRK13539 91 AENLEF---WAAF--LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|
gi 502303547 191 VLDTMVGLAEEGMTMLCVTH 210
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
10-242 |
1.19e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 81.64 E-value: 1.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 10 TVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdLKKID 89
Cdd:PRK15439 4 SDTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCAR-LTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 90 EVRREVGMVFQHFNLFPHLTILENctlapIWVRkMPKKQAEEVAMHFLKR-----VKIPEQAnkypGQLSGGQQQRVAIA 164
Cdd:PRK15439 83 AHQLGIYLVPQEPLLFPNLSVKEN-----ILFG-LPKRQASMQKMKQLLAalgcqLDLDSSA----GSLEVADRQIVEIL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 165 RSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
28-249 |
1.68e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 80.33 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCI-NRLEEhqKGKIVVD-----GTELTN----DLKKIdeVRREVGM 97
Cdd:COG4170 18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAIcGITKD--NWHVTADrfrwnGIDLLKlsprERRKI--IGREIAM 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFN--LFPHLTILE-------NCTL-APIWVRKMPKKQAeevAMHFLKRVKIPEQA---NKYPGQLSGGQQQRVAIA 164
Cdd:COG4170 94 IFQEPSscLDPSAKIGDqlieaipSWTFkGKWWQRFKWRKKR---AIELLHRVGIKDHKdimNSYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 165 RSLCMNPKIMLFDEPTSALDP---EMIKEVLDTMVGLaeEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFD 241
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESttqAQIFRLLARLNQL--QGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILK 248
|
....*...
gi 502303547 242 NPQHERTK 249
Cdd:COG4170 249 SPHHPYTK 256
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
27-231 |
3.27e-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: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTEltnDLKKIDEVRREVGMVF-QHFNLF 105
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV---PWKRRKKFLRRIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 PHLTILENCTL-APIWvrKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:cd03267 108 WDLPVIDSFYLlAAIY--DLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502303547 185 ---PEMIKEVLDTMVglAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:cd03267 186 vvaQENIRNFLKEYN--RERGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-230 |
3.82e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 80.43 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTE---------LTNDLKKIDEVRREVGMVFQhfn 103
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEvvtrspqdgLANGIVYISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 104 lfphLTILENCTLAPIwvRKMPKK------QAEEVAM-HFLK--RVKIPEQaNKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:PRK10762 345 ----MSVKENMSLTAL--RYFSRAggslkhADEQQAVsDFIRlfNIKTPSM-EQAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
27-232 |
5.39e-17 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 80.02 E-value: 5.39e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGD--FHVlRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndLKKIDEVRREVGMVFQHFNL 104
Cdd:PRK10522 332 YQDngFSV-GPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT--AEQPEDYRKLFSAVFTDFHL 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 FPHLTILENctlapiwvrKMPKKQAEEVAMHFLK-RVKIPEQANKYPG-QLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:PRK10522 409 FDQLLGPEG---------KPANPALVEKWLERLKmAHKLELEDGRISNlKLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502303547 183 LDP----EMIKEVLDTMvglAEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVE 232
Cdd:PRK10522 480 QDPhfrrEFYQVLLPLL---QEMGKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
33-232 |
6.90e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 79.45 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEH--QKGKIVVDGTELT-NDLKkiDEVRREVGMVFQHFNLFPHLT 109
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHgsYEGEILFDGEVCRfKDIR--DSEALGIVIIHQELALIPYLS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENctlapIWVRKMPKK-------QAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:NF040905 95 IAEN-----IFLGNERAKrgvidwnETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 502303547 183 LDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:NF040905 170 LNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-233 |
7.21e-17 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 79.76 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 1 MAEAPA-----KKLTVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIV 75
Cdd:PRK10789 294 LAEAPVvkdgsEPVPEGRGELDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIR 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 76 VDGTELTnDLKkIDEVRREVGMVFQHFNLFPHlTILENCTLA-PiwvrKMPKKQAEEVAMhfLKRV-----KIPEQANKY 149
Cdd:PRK10789 374 FHDIPLT-KLQ-LDSWRSRLAVVSQTPFLFSD-TVANNIALGrP----DATQQEIEHVAR--LASVhddilRLPQGYDTE 444
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 150 PGQ----LSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTmvgLAE--EGMTMLCVTHEMGfARQVANRVI 223
Cdd:PRK10789 445 VGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHN---LRQwgEGRTVIISAHRLS-ALTEASEIL 520
|
250
....*....|
gi 502303547 224 FMDQGQIVEQ 233
Cdd:PRK10789 521 VMQHGHIAQR 530
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
31-248 |
8.27e-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: 8.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGtelTNDLKKIDEVRREVGMVF-QHFNLFPHLT 109
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLG---YVPFKRRKEFARRIGVVFgQRSQLWWDLP 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILEN-CTLAPIWvrKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP--- 185
Cdd:COG4586 113 AIDSfRLLKAIY--RIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVvsk 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 186 EMIKEVLDTMVglAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERT 248
Cdd:COG4586 191 EAIREFLKEYN--RERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
33-212 |
1.90e-16 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 1.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTEL--TNDLKKIDEvrrEVGMVFQHFNLFPHLTI 110
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfASTTAALAA---GVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENctlapIWVRKMP-------KKQAEEVAMHFLKRVKI---PEQANKYpgqLSGGQQQRVAIARSLCMNPKIMLFDEPT 180
Cdd:PRK11288 97 AEN-----LYLGQLPhkggivnRRLLNYEAREQLEHLGVdidPDTPLKY---LSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190
....*....|....*....|....*....|..
gi 502303547 181 SALDPEMIKEVLDTMVGLAEEGMTMLCVTHEM 212
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
33-213 |
5.81e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 75.30 E-value: 5.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKidevrREVGMVFQHFNL---FPHLt 109
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK-----NLVAYVPQSEEVdwsFPVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 iLENCTLAPI-----WVRKmPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:PRK15056 97 -VEDVVMMGRyghmgWLRR-AKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174
|
170 180
....*....|....*....|....*....
gi 502303547 185 PEMIKEVLDTMVGLAEEGMTMLCVTHEMG 213
Cdd:PRK15056 175 VKTEARIISLLRELRDEGKTMLVSTHNLG 203
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
32-210 |
1.91e-15 |
|
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: 72.53 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlKKIDEVRREVGMVFQHFNLFPHLTIL 111
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD---FQRDSIARGLLYLGHAPGIKTTLSVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENCTLapiWVRKMPKKQAEEVamhfLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEV 191
Cdd:cd03231 92 ENLRF---WHADHSDEQVEEA----LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164
|
170
....*....|....*....
gi 502303547 192 LDTMVGLAEEGMTMLCVTH 210
Cdd:cd03231 165 AEAMAGHCARGGMVVLTTH 183
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
33-242 |
3.51e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 75.01 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRC-INRLEEHQKGKIVVDGTeltndlkkidevrreVGMVFQHFNLFpHLTIL 111
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGS---------------VAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENCTLAPIWVRKMPKKQAEEVAM-HFLK------RVKIPEQANkypgQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:PLN03232 697 ENILFGSDFESERYWRAIDVTALqHDLDllpgrdLTEIGERGV----NISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 185 PEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVaNRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:PLN03232 773 AHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
33-241 |
3.63e-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: 74.98 E-value: 3.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltndlkkidevrreVGMVFQHF---NLFPHLT 109
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS---------------VAYVPQQAwiqNDSLREN 718
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLAPIWVRKMPKKQAEEVAMHFL---KRVKIPEQANkypgQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPE 186
Cdd:TIGR00957 719 ILFGKALNEKYYQQVLEACALLPDLEILpsgDRTEIGEKGV----NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH 794
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 187 MIKEVLDTMVGlaEEGM----TMLCVTHEMGFARQVaNRVIFMDQGQIVEQNSPAEFFD 241
Cdd:TIGR00957 795 VGKHIFEHVIG--PEGVlknkTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
32-210 |
4.90e-15 |
|
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: 71.24 E-value: 4.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlkKIDEVRREVGMVFQHFN-LFPHLTI 110
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA----EQRDEPHENILYLGHLPgLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCT-LAPIwvrkmpkKQAEEVAMH-FLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMI 188
Cdd:TIGR01189 91 LENLHfWAAI-------HGGAQRTIEdALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGV 163
|
170 180
....*....|....*....|..
gi 502303547 189 KEVLDTMVGLAEEGMTMLCVTH 210
Cdd:TIGR01189 164 ALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
34-230 |
1.11e-14 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.16 E-value: 1.11e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 34 RDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIdevRREVGMVF-----QHFNLFPHL 108
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ---RLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILEN-CTLA----PIWVRkmPKKQAEeVAMHFLKRVKIP-EQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:PRK15439 357 PLAWNvCALThnrrGFWIK--PARENA-VLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 502303547 183 LDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:PRK15439 434 VDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
124-231 |
1.28e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.46 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 124 MPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGM 203
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100
....*....|....*....|....*...
gi 502303547 204 TMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDRGRVI 223
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-214 |
1.81e-14 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 72.35 E-value: 1.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 2 AEAPAKKLTVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINrlEEHQKGkivvdgteL 81
Cdd:PRK10938 245 PDEPSARHALPANEPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT--GDHPQG--------Y 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 82 TNDL----------KKIDEVRREVGMVFQHFnlfpHLTILENCTLAPIWV----------RKMPKKQaEEVAMHFLKRVK 141
Cdd:PRK10938 315 SNDLtlfgrrrgsgETIWDIKKHIGYVSSSL----HLDYRVSTSVRNVILsgffdsigiyQAVSDRQ-QKLAQQWLDILG 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 142 IPEQANKYPGQ-LSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP---EMIKEVLDTMVGlaeEGMTML----------- 206
Cdd:PRK10938 390 IDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLIS---EGETQLlfvshhaedap 466
|
....*....
gi 502303547 207 -CVTHEMGF 214
Cdd:PRK10938 467 aCITHRLEF 475
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
50-238 |
2.38e-14 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 70.59 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 50 GPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIdeVRREVGMVFQHFNLFPHLTILEnctLAPI----W----- 120
Cdd:PRK10575 44 GHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA--FARKVAYLPQQLPAAEGMTVRE---LVAIgrypWhgalg 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 121 -VRKMPKKQAEE-VAMHFLKRVkipeqANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGL 198
Cdd:PRK10575 119 rFGAADREKVEEaISLVGLKPL-----AHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRL 193
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 502303547 199 AEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:PRK10575 194 SQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAE 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
33-233 |
5.33e-14 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 71.19 E-value: 5.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKiDEVRREVGMVFQHFNLFPHLTILE 112
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPK-SSQEAGIGIIHQELNLIPQLTIAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 113 NCTLAPIWVRKMP----KKQAEEvAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL-DPE- 186
Cdd:PRK10762 99 NIFLGREFVNRFGridwKKMYAE-ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTEt 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502303547 187 -----MIKEvldtmvgLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQ-IVEQ 233
Cdd:PRK10762 178 eslfrVIRE-------LKSQGRGIVYISHRLKEIFEICDDVTVFRDGQfIAER 223
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
17-231 |
6.95e-14 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 70.69 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIvvdgteltndlkKIDEvRREVG 96
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV------------KWSE-NANIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQ-HFNLFPH-LTILEnctlapiWVRKMPKKQAEEVAMH-FLKRVKIP-EQANKYPGQLSGGQQQRVAIARSLCMNPK 172
Cdd:PRK15064 386 YYAQdHAYDFENdLTLFD-------WMSQWRQEGDDEQAVRgTLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPN 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 173 IMLFDEPTSALDPEMIkEVLDTmvGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:PRK15064 459 VLVMDEPTNHMDMESI-ESLNM--ALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
40-228 |
7.06e-14 |
|
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: 71.20 E-value: 7.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 40 VMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtndLKKIDEVRREVGMVFQHFNLFPHLTILENCTLAPi 119
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI---LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYA- 2037
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 120 WVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLA 199
Cdd:TIGR01257 2038 RLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSII 2117
|
170 180
....*....|....*....|....*....
gi 502303547 200 EEGMTMLCVTHEMGFARQVANRVIFMDQG 228
Cdd:TIGR01257 2118 REGRAVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
33-184 |
7.38e-14 |
|
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: 68.06 E-value: 7.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCI-NRLEEHQK--GKIVVDGteltNDLKKIDEV-RREVGMVFQHFNLFPHL 108
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVSveGDIHYNG----IPYKEFAEKyPGEIIYVSEEDVHFPTL 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 109 TILEncTLApiWVRKMpkkqaeevamhflkrvkipeQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALD 184
Cdd:cd03233 99 TVRE--TLD--FALRC--------------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
22-231 |
7.94e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 7.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 22 NMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELtnDLKKIDE-VRREVGMVFQ 100
Cdd:PRK10982 3 NISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI--DFKSSKEaLENGISMVHQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 101 HFNLFPHLTILENctlapIWVRKMPKKQ--AEEVAMH-----FLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:PRK10982 81 ELNLVLQRSVMDN-----MWLGRYPTKGmfVDQDKMYrdtkaIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-231 |
8.60e-14 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 70.36 E-value: 8.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKiDEVRREVGMVF------- 99
Cdd:PRK11147 13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARLQQ-DPPRNVEGTVYdfvaegi 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 100 ----QHFNLFPHLTILENCTLAPIWVRKMPKKQAE---EVAMHFLKRVK-IPEQ----ANKYPGQLSGGQQQRVAIARSL 167
Cdd:PRK11147 92 eeqaEYLKRYHDISHLVETDPSEKNLNELAKLQEQldhHNLWQLENRINeVLAQlgldPDAALSSLSGGWLRKAALGRAL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 168 CMNPKIMLFDEPTSALDPEMIkEVLDTMvgLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIV 231
Cdd:PRK11147 172 VSNPDVLLLDEPTNHLDIETI-EWLEGF--LKTFQGSIIFISHDRSFIRNMATRIVDLDRGKLV 232
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
32-242 |
1.01e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 70.78 E-value: 1.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELT----NDLKKIDEVRREVGMVFQ---HFNL 104
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAkfglTDLRRVLSIIPQSPVLFSgtvRFNI 1330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 FPhltiLENCTLAPIWvRKMPKKQAEEVamhfLKRVKIPEQANKYPG--QLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:PLN03232 1331 DP----FSEHNDADLW-EALERAHIKDV----IDRNPFGLDAEVSEGgeNFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 183 LDPEMIKEVLDTmvgLAEE--GMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:PLN03232 1402 VDVRTDSLIQRT---IREEfkSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
36-255 |
1.05e-13 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 69.45 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 36 INLKVMRGERIVIAGPSGSGKSTMIRCInrleehqkGKIVVDGTELTNDLKKIDEV----------RREVG----MVFQH 101
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAI--------CGVTKDNWRVTADRMRFDDIdllrlsprerRKLVGhnvsMIFQE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 102 FN--LFPHLTILENCTLA-PIWVRKMPKKQA----EEVAMHFLKRVKIPEQAN---KYPGQLSGGQQQRVAIARSLCMNP 171
Cdd:PRK15093 98 PQscLDPSERVGRQLMQNiPGWTYKGRWWQRfgwrKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALANQP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 172 KIMLFDEPTSALDPEMIKEVLDTMVGLAE-EGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDNPQHERTKL 250
Cdd:PRK15093 178 RLLIADEPTNAMEPTTQAQIFRLLTRLNQnNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHPYTQA 257
|
....*
gi 502303547 251 FLSQI 255
Cdd:PRK15093 258 LIRAI 262
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
36-231 |
1.36e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.94 E-value: 1.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 36 INLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlKKIDEVRRevGMVF-----QHFNLFPHLTI 110
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR-SPRDAIRA--GIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTlapIWVRK--------MPKKQAEEVAMHFLKRVKI----PEQAnkyPGQLSGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:PRK11288 349 ADNIN---ISARRhhlragclINNRWEAENADRFIRSLNIktpsREQL---IMNLSGGNQQKAILGRWLSEDMKVILLDE 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 179 PTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHE----MGfarqVANRVIFMDQGQIV 231
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRIA 475
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
17-233 |
4.49e-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: 4.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFH-VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIdeVRREV 95
Cdd:PRK10790 340 RIDIDNVSFAYRDDNlVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQH-----FNLFPHLTI------------LENCTLAPiWVRKMPKkqaeevAMHflkrVKIPEQANKypgqLSGGQQ 158
Cdd:PRK10790 418 AMVQQDpvvlaDTFLANVTLgrdiseeqvwqaLETVQLAE-LARSLPD------GLY----TPLGEQGNN----LSVGQK 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 159 QRVAIARSLCMNPKIMLFDEPTSALDP---EMIKEVLdtmvGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQ 233
Cdd:PRK10790 483 QLLALARVLVQTPQILILDEATANIDSgteQAIQQAL----AAVREHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQ 555
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-229 |
6.79e-13 |
|
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: 67.65 E-value: 6.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 20 IVNMNKWY-GDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVvdgteLTNDLKkidevrreVGMV 98
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR-----PQPGIK--------VGYL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 99 FQHFNLFPHLTILENCTLApiwVRKMPKKQAE--EVAMHFL-----------------------------KRVKIPEQAN 147
Cdd:TIGR03719 74 PQEPQLDPTKTVRENVEEG---VAEIKDALDRfnEISAKYAepdadfdklaaeqaelqeiidaadawdldSQLEIAMDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 148 KYP------GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIkEVLDTMvgLAEEGMTMLCVTHEMGFARQVANR 221
Cdd:TIGR03719 151 RCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV-AWLERH--LQEYPGTVVAVTHDRYFLDNVAGW 227
|
....*...
gi 502303547 222 VIFMDQGQ 229
Cdd:TIGR03719 228 ILELDRGR 235
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
40-238 |
7.70e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.11 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 40 VMRGERIVIAGPSGSGKSTMIRCINRLEEHqKGKIVVDGTEL----TNDLKKI-----DEVRREVGM-VFQHFNLFPHlt 109
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLeawsAAELARHraylsQQQTPPFAMpVFQYLTLHQP-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ilENCTLAPiwvrkmPKKQAEEVAmhflKRVKIPEQANKYPGQLSGGQQQRVAIARSLC-----MNP--KIMLFDEPTSA 182
Cdd:PRK03695 96 --DKTRTEA------VASALNEVA----EALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPagQLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 183 LDPEMiKEVLDTMVG-LAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAE 238
Cdd:PRK03695 164 LDVAQ-QAALDRLLSeLCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
19-232 |
8.96e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 67.67 E-value: 8.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRC-INRLEEhQKGKIVVdGTELtndlkkidevrrEVGM 97
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHC-GTKL------------EVAY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQH-FNLFPHLTILENctLApiwvrkmPKKQAEEV---AMHFL----------KRVKIPEQAnkypgqLSGGQQQRVAI 163
Cdd:PRK11147 387 FDQHrAELDPEKTVMDN--LA-------EGKQEVMVngrPRHVLgylqdflfhpKRAMTPVKA------LSGGERNRLLL 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 164 ARSLCMNPKIMLFDEPTSALDPEMIkEVLDTMvgLAEEGMTMLCVTHEMGFarqVANRV----IFMDQGQIVE 232
Cdd:PRK11147 452 ARLFLKPSNLLILDEPTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQF---VDNTVtecwIFEGNGKIGR 518
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
18-211 |
1.29e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 64.97 E-value: 1.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKideVRREVGM 97
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCT---YQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNLFPHLTILENCTLapiwvrkmpKKQAEEVAMHFLKRVKI--PEQANKYP-GQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLY---------DIHFSPGAVGITELCRLfsLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLW 149
|
170 180 190
....*....|....*....|....*....|....*..
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHE 211
Cdd:PRK13540 150 LLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
153-242 |
1.36e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 67.07 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 153 LSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVaNRVIFMDQGQIVE 232
Cdd:PLN03130 741 ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKE 819
|
90
....*....|
gi 502303547 233 QNSPAEFFDN 242
Cdd:PLN03130 820 EGTYEELSNN 829
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
36-232 |
1.52e-12 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 66.75 E-value: 1.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 36 INLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlkKIDEVRREVGMVFQHFNLFPHLTILENCT 115
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD--NREAYRQLFSAVFSDFHLFDRLLGLDGEA 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 116 LapiwvrkmpkkqaEEVAMHFLKRVKIpeqANKYP---G-----QLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP-- 185
Cdd:COG4615 429 D-------------PARARELLERLEL---DHKVSvedGrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAADQDPef 492
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 502303547 186 ------EMIKEvldtmvgLAEEGMTMLCVTH-EMGFarQVANRVIFMDQGQIVE 232
Cdd:COG4615 493 rrvfytELLPE-------LKARGKTVIAISHdDRYF--DLADRVLKMDYGKLVE 537
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
33-232 |
3.12e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 3.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTND--LKKID-------EVRREVGmvfqhfn 103
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHnaNEAINhgfalvtEERRSTG------- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 104 LFPHLTILENCTLAPIWVRKMP---------KKQAEEV--AMhflkRVKIPEQANKYpGQLSGGQQQRVAIARSLCMNPK 172
Cdd:PRK10982 337 IYAYLDIGFNSLISNIRNYKNKvglldnsrmKSDTQWVidSM----RVKTPGHRTQI-GSLSGGNQQKVIIGRWLLTQPE 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 502303547 173 IMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQ---IVE 232
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLvagIVD 474
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-226 |
3.48e-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: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 23 MNKWYGDFHvlrdinLKV-----MRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTndlKKIDEVRREVGM 97
Cdd:cd03237 6 MKKTLGEFT------LEVeggsiSESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS---YKPQYIKADYEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFnLFphlTILENCTLAPIWvrkmpkkqAEEVaMHFLKRVKIPEQANKypgQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:cd03237 77 TVRDL-LS---SITKDFYTHPYF--------KTEI-AKPLQIEQILDREVP---ELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 502303547 178 EPTSALDPE---MIKEVLDTMVGLAEEgmTMLCVTHEMGFARQVANRVIFMD 226
Cdd:cd03237 141 EPSAYLDVEqrlMASKVIRRFAENNEK--TAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
72-224 |
3.95e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.82 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 72 GKIVVDGTELTN-DLKkidEVRREVGMVFQHFNLFpHLTILENCTLAPIWVRKMPKKQAEEVAM--HFLKRV--KIPEQA 146
Cdd:PTZ00265 1277 GKILLDGVDICDyNLK---DLRNLFSIVSQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAidEFIESLpnKYDTNV 1352
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 147 NKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEG-MTMLCVTHEMGFARQVANRVIF 224
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIKRSDKIVVF 1431
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
10-244 |
4.91e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 65.57 E-value: 4.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 10 TVSATEVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKID 89
Cdd:PTZ00243 1303 PVQAGSLVFEGVQMRYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA--YGLR 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 90 EVRREVGMVFQHFNLFPHlTILEN------CTLAPIWvrkmpkKQAEEVAMHflKRV---------KIPEQANKYpgqlS 154
Cdd:PTZ00243 1381 ELRRQFSMIPQDPVLFDG-TVRQNvdpfleASSAEVW------AALELVGLR--ERVasesegidsRVLEGGSNY----S 1447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 155 GGQQQRVAIARSLC-MNPKIMLFDEPTSALDPEMIKEVLDTmVGLAEEGMTMLCVTHEMGFARQVaNRVIFMDQGQIVEQ 233
Cdd:PTZ00243 1448 VGQRQLMCMARALLkKGSGFILMDEATANIDPALDRQIQAT-VMSAFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEM 1525
|
250
....*....|.
gi 502303547 234 NSPAEFFDNPQ 244
Cdd:PTZ00243 1526 GSPRELVMNRQ 1536
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-228 |
6.22e-12 |
|
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: 63.12 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 26 WYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCInrLEEHQK--GKIVVDGTELTNDLKKIDEVRRE--VGMVFQH 101
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQTleGKVHWSNKNESEPSFEATRSRNRysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 102 FNLFpHLTILENCTLAPIWVRKMPKKQAEEVAMH-------FLKRVKIPEQANkypgQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:cd03290 88 PWLL-NATVEENITFGSPFNKQRYKAVTDACSLQpdidllpFGDQTEIGERGI----NLSGGQRQRICVARALYQNTNIV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 175 LFDEPTSALDPEMIKEVLDTMV--GLAEEGMTMLCVTHEMGFARQvANRVIFMDQG 228
Cdd:cd03290 163 FLDDPFSALDIHLSDHLMQEGIlkFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDG 217
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
32-242 |
6.22e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.14 E-value: 6.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTN----DLKKIDEVRREVGMVFQ---HFNL 104
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglmDLRKVLGIIPQAPVLFSgtvRFNL 1333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 105 FP---H-----LTILENCTLAPIwVRKMPKKQAEEVAmhflkrvkipEQANKYpgqlSGGQQQRVAIARSLCMNPKIMLF 176
Cdd:PLN03130 1334 DPfneHndadlWESLERAHLKDV-IRRNSLGLDAEVS----------EAGENF----SVGQRQLLSLARALLRRSKILVL 1398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 177 DEPTSALDPEMIKEVLDTmvgLAEE--GMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:PLN03130 1399 DEATAAVDVRTDALIQKT---IREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
23-223 |
6.87e-12 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 62.20 E-value: 6.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 23 MNKWYGDFHVLRDINlKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIDevrrevgmvfqhf 102
Cdd:cd03222 6 CVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQYID------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 103 nlfphltilenctlapiwvrkmpkkqaeevamhflkrvkipeqankypgqLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:cd03222 72 --------------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 502303547 183 LDPEMIKEVLDTMVGLAEEGM-TMLCVTHEMGFARQVANRVI 223
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH 143
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
32-257 |
7.17e-12 |
|
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: 63.72 E-value: 7.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDG-TELTNDLKKIDEVRREVGMVFQ-HFNLFPHLT 109
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGrISFSSQFSWIMPGTIKENIIFGvSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 ILENCTLApiwvrkmpkkqaEEVAmhflkrvKIPEQANKYPGQ----LSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:cd03291 132 VVKACQLE------------EDIT-------KFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 186 EMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQIV-------EQNSPAEF---------FDNPQHERTK 249
Cdd:cd03291 193 FTEKEIFESCVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYfygtfseLQSLRPDFssklmgydtFDQFSAERRN 271
|
....*...
gi 502303547 250 LFLSQILH 257
Cdd:cd03291 272 SILTETLR 279
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
33-211 |
8.07e-12 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 62.26 E-value: 8.07e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 33 LRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEE--HQKGKIVVDGTELTNDLkkidevRREVGMVFQHFNLFPHLTI 110
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTagVITGEILINGRPLDKNF------QRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 111 LENCTLAPiWVRkmpkkqaeevamhflkrvkipeqankypgQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKE 190
Cdd:cd03232 97 REALRFSA-LLR-----------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|.
gi 502303547 191 VLDTMVGLAEEGMTMLCVTHE 211
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHQ 167
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
29-216 |
9.02e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 64.67 E-value: 9.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltNDLKKIDEV--RREVGMVFQHFNLFP 106
Cdd:PTZ00265 397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS---HNLKDINLKwwRSKIGVVSQDPLLFS 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 H---------------LTILEN------------------CTLAP----------------IWVRKMPKKQAEEVAMHFL 137
Cdd:PTZ00265 474 NsiknnikyslyslkdLEALSNyynedgndsqenknkrnsCRAKCagdlndmsnttdsnelIEMRKNYQTIKDSEVVDVS 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 138 KRVKIPEQANKYP-----------GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPE---MIKEVLDTMVGlaEEGM 203
Cdd:PTZ00265 554 KKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKseyLVQKTINNLKG--NENR 631
|
250
....*....|...
gi 502303547 204 TMLCVTHEMGFAR 216
Cdd:PTZ00265 632 ITIIIAHRLSTIR 644
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
32-251 |
1.13e-11 |
|
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: 63.33 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEeHQKGKIVVDGteLTNDLKKIDEVRREVGMVFQHFNLFPHlTIL 111
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLL-NTEGDIQIDG--VSWNSVPLQKWRKAFGVIPQKVFIFSG-TFR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENCTLAPIWVRKMPKKQAEEVAmhfLKRVkipeqANKYPGQL-----------SGGQQQRVAIARSLCMNPKIMLFDEPT 180
Cdd:cd03289 95 KNLDPYGKWSDEEIWKVAEEVG---LKSV-----IEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPS 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 181 SALDPEMIKeVLDTMVGLAEEGMTMLCVTHEMGfARQVANRVIFMDQGQIVEQNSPAEFFDNPQH--------ERTKLF 251
Cdd:cd03289 167 AHLDPITYQ-VIRKTLKQAFADCTVILSEHRIE-AMLECQRFLVIEENKVRQYDSIQKLLNEKSHfkqaispsDRLKLF 243
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
29-215 |
1.32e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 62.13 E-value: 1.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVL-RDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlKKIDEVRREVgmvfqHFNLF-- 105
Cdd:PRK13538 12 DERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQG-------EPIRRQRDEY-----HQDLLyl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 -------PHLTILENctLApiWVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDE 178
Cdd:PRK13538 80 ghqpgikTELTALEN--LR--FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|....*...
gi 502303547 179 PTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFA 215
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQgGMVILTTHQDLPVA 193
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-185 |
1.55e-11 |
|
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: 64.16 E-value: 1.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEhQKGKIVVDGteLTNDLKKIDEVRREVGMVFQHF--------- 102
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDG--VSWNSVTLQTWRKAFGVIPQKVfifsgtfrk 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 103 NLFPHltilENCTLAPIWvrkmpkKQAEEVAMHflkrvKIPEQankYPGQL-----------SGGQQQRVAIARSLCMNP 171
Cdd:TIGR01271 1311 NLDPY----EQWSDEEIW------KVAEEVGLK-----SVIEQ---FPDKLdfvlvdggyvlSNGHKQLMCLARSILSKA 1372
|
170
....*....|....
gi 502303547 172 KIMLFDEPTSALDP 185
Cdd:TIGR01271 1373 KILLLDEPSAHLDP 1386
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
14-184 |
2.02e-11 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 62.05 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 14 TEVAVEIVNMNkwYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIvvdgteltndlKKIDEVRr 93
Cdd:PRK09544 3 SLVSLENVSVS--FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKLR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 94 eVGMVFQHFNLFPHLtilenctlaPIWVRKM----PKKQAEEVaMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCM 169
Cdd:PRK09544 69 -IGYVPQKLYLDTTL---------PLTVNRFlrlrPGTKKEDI-LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
|
170
....*....|....*
gi 502303547 170 NPKIMLFDEPTSALD 184
Cdd:PRK09544 138 RPQLLVLDEPTQGVD 152
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
12-238 |
4.64e-11 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 62.45 E-value: 4.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 12 SATEVAVEIVNMNKWYGDFHVLRDINLKVMRGErivIAGPSGS---GKSTMIRCINRLEEHQKGKIVVDGTELT-NDLkk 87
Cdd:NF033858 261 DDDEPAIEARGLTMRFGDFTAVDHVSFRIRRGE---IFGFLGSngcGKSTTMKMLTGLLPASEGEAWLFGQPVDaGDI-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 88 idEVRREVGMVFQHFNLFPHLTILENCTL-APIWvrKMPKKQAEE-VA-MhfLKRVKIPEQANKYPGQLSGGQQQRVAIA 164
Cdd:NF033858 336 --ATRRRVGYMSQAFSLYGELTVRQNLELhARLF--HLPAAEIAArVAeM--LERFDLADVADALPDSLPLGIRQRLSLA 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 165 RSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLA-EEGMTMLCVTHEMGFArQVANRVIFMDQGQIVEQNSPAE 238
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVDPVARDMFWRLLIELSrEDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
32-240 |
5.49e-11 |
|
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: 61.08 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNdlKKIDEVRREVGMVFQ---------HF 102
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK--LPLHTLRSRLSIILQdpilfsgsiRF 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 103 NLFPHLTilenCTLAPIWvrkmpkkQAEEVAMhfLKRVkipeqANKYPGQL-----------SGGQQQRVAIARSLCMNP 171
Cdd:cd03288 114 NLDPECK----CTDDRLW-------EALEIAQ--LKNM-----VKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKS 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 172 KIMLFDEPTSALDpeMIKE-VLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFF 240
Cdd:cd03288 176 SILIMDEATASID--MATEnILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
28-242 |
5.59e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.22 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 28 GDFH-VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTeltndlkkidevrreVGMVFQHFNLFP 106
Cdd:PRK13545 34 GEYHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS---------------AALIAISSGLNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTILENCTLAPIwVRKMPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPE 186
Cdd:PRK13545 99 QLTGIENIELKGL-MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQT 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 187 MIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSPAEFFDN 242
Cdd:PRK13545 178 FTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
32-188 |
6.15e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 6.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDlkkidEVRREVGMVFQHFNLFPHLTIL 111
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG-----DRSRFMAYLGHLPGLKADLSTL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 EN----CTLAPIWVRKMPKKQaeevamhfLKRVKIPEQANKYPGQLSGGQQQRVAIARsLCMNPK-IMLFDEPTSALDPE 186
Cdd:PRK13543 101 ENlhflCGLHGRRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALAR-LWLSPApLWLLDEPYANLDLE 171
|
..
gi 502303547 187 MI 188
Cdd:PRK13543 172 GI 173
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
32-245 |
6.92e-11 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 61.00 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCinrLEEHQKGKIVVDGTELTND-------LKKIDEVR----REV----- 95
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKA---LAGDLTGGGAPRGARVTGDvtlngepLAAIDAPRlarlRAVlpqaa 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 --GMVFQHFNL-----FPHltilenctlapiwVRK--MPKKQAEEVAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARS 166
Cdd:PRK13547 93 qpAFAFSAREIvllgrYPH-------------ARRagALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 167 LCM---------NPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVIFMDQGQIVEQNSP 236
Cdd:PRK13547 160 LAQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239
|
....*....
gi 502303547 237 AEFFdNPQH 245
Cdd:PRK13547 240 ADVL-TPAH 247
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
19-232 |
9.01e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 60.43 E-value: 9.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 19 EIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ--KGKIVVDGTELTnDLKKIDEVRREVG 96
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESIL-DLEPEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 97 MVFQHFNLFPHLTILENCTLA--------------PIWVRKMPKKQAEEVAM--HFLKRvkipeqaNKYPGqLSGGQQQR 160
Cdd:CHL00131 88 LAFQYPIEIPGVSNADFLRLAynskrkfqglpeldPLEFLEIINEKLKLVGMdpSFLSR-------NVNEG-FSGGEKKR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 161 VAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHemgFARQ----VANRVIFMDQGQIVE 232
Cdd:CHL00131 160 NEILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIK 232
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
12-223 |
2.53e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.21 E-value: 2.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 12 SATEVAVEIVNMNKWYGDFHvlrdinLKVM-----RGERIVIAGPSGSGKSTMIRCInrleehqKGKIVVDGTELTNDLK 86
Cdd:PRK13409 335 SERETLVEYPDLTKKLGDFS------LEVEggeiyEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDEGEVDPELK 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 87 ---KIDEVRREVGMvfqhfnlfphlTILEnctlapiWVRKMPKK------QAEevamhFLKRVKIPEQANKYPGQLSGGQ 157
Cdd:PRK13409 402 isyKPQYIKPDYDG-----------TVED-------LLRSITDDlgssyyKSE-----IIKPLQLERLLDKNVKDLSGGE 458
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 158 QQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVI 223
Cdd:PRK13409 459 LQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEErEATALVVDHDIYMIDYISDRLM 525
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-231 |
2.72e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 2.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNKW---YGDFHVLRDINLKVMRGERIVIAGPSGSGkstmircinRLE-----------EHQKGKIVVDGTE 80
Cdd:NF040905 255 EVVFEVKNWTVYhplHPERKVVDDVSLNVRRGEIVGIAGLMGAG---------RTElamsvfgrsygRNISGTVFKDGKE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 81 LtnDLKKID-----------EVRREVGMVFQHfnlfphlTILENCTLAPIwvRKMPKK----QAEE--VAMHFLKRVKIp 143
Cdd:NF040905 326 V--DVSTVSdaidaglayvtEDRKGYGLNLID-------DIKRNITLANL--GKVSRRgvidENEEikVAEEYRKKMNI- 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 144 eqanKYP------GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQ 217
Cdd:NF040905 394 ----KTPsvfqkvGNLSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLG 469
|
250
....*....|....
gi 502303547 218 VANRVIFMDQGQIV 231
Cdd:NF040905 470 MCDRIYVMNEGRIT 483
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
50-211 |
2.82e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.12 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 50 GPSGSGKSTMIRCinrLEEHQKGKIVVDGTELTNDLKKIDEVRREVGMVFQHFNLFPHLTILENCTLA-----PIWVRKM 124
Cdd:TIGR00956 796 GASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSaylrqPKSVSKS 872
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 125 PKKQAEEVAMHFLKRVKIPEQANKYPGQ-LSGGQQQRVAIARSLCMNPKIMLF-DEPTSALDPEMIKEVLDTMVGLAEEG 202
Cdd:TIGR00956 873 EKMEYVEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLADHG 952
|
....*....
gi 502303547 203 MTMLCVTHE 211
Cdd:TIGR00956 953 QAILCTIHQ 961
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
15-241 |
4.56e-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: 59.18 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 15 EVAVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTEltnDLKKIDEVRRe 94
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETV---KLAYVDQSRD- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 vgmvfqhfNLFPHLTilenctlapIWvrkmpkkqaEEVA----MHFLKRVKIPEQA------------NKYPGQLSGGQQ 158
Cdd:TIGR03719 396 --------ALDPNKT---------VW---------EEISggldIIKLGKREIPSRAyvgrfnfkgsdqQKKVGQLSGGER 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 159 QRVAIARSLCMNPKIMLFDEPTSALDPEMIK---EVLDTMVGLAeegmtmLCVTHEMGFARQVANRVI-FmdqgqivEQN 234
Cdd:TIGR03719 450 NRVHLAKTLKSGGNVLLLDEPTNDLDVETLRaleEALLNFAGCA------VVISHDRWFLDRIATHILaF-------EGD 516
|
....*..
gi 502303547 235 SPAEFFD 241
Cdd:TIGR03719 517 SHVEWFE 523
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
31-229 |
5.54e-10 |
|
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: 56.95 E-value: 5.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIrciNRLEEHQKGKIVVDGTEL--TNDLKKIDEVRR--EVGmvfqhfnlfp 106
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKSTLV---NEGLYASGKARLISFLPKfsRNKLIFIDQLQFliDVG---------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 hltiLENCTLApiwvRKMPkkqaeevamhflkrvkipeqankypgQLSGGQQQRVAIARSLCMNPK--IMLFDEPTSALD 184
Cdd:cd03238 76 ----LGYLTLG----QKLS--------------------------TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 502303547 185 PEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQ 229
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGS 165
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
43-212 |
6.19e-10 |
|
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: 58.15 E-value: 6.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 43 GERIVIAGPSGSGKSTMIRCI--------NRLEEHQKGKIVVD---GTELTNDLKKIDEVRREVGMVFQHFNLFPHL--- 108
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILagklkpnlGKFDDPPDWDEILDefrGSELQNYFTKLLEGDVKVIVKPQYVDLIPKAvkg 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILENCTlapiwvRKMPKKQAEEVamhfLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDpemI 188
Cdd:cd03236 106 KVGELLK------KKDERGKLDEL----VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD---I 172
|
170 180
....*....|....*....|....*..
gi 502303547 189 KEVLD---TMVGLAEEGMTMLCVTHEM 212
Cdd:cd03236 173 KQRLNaarLIRELAEDDNYVLVVEHDL 199
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
32-257 |
8.21e-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: 58.77 E-value: 8.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKI--------------VVDGTELTNDLkkidevrreVGM 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIkhsgrisfspqtswIMPGTIKDNII---------FGL 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 98 VFQHFNlfpHLTILENCTLapiwvrkmpkkqAEEVAmhflkrvKIPEQANKYPGQ----LSGGQQQRVAIARSLCMNPKI 173
Cdd:TIGR01271 512 SYDEYR---YTSVIKACQL------------EEDIA-------LFPEKDKTVLGEggitLSGGQRARISLARAVYKDADL 569
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 174 MLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQIV-------EQNSPAEF------- 239
Cdd:TIGR01271 570 YLLDSPFTHLDVVTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYfygtfseLQAKRPDFsslllgl 648
|
250 260
....*....|....*....|
gi 502303547 240 --FDNPQHERTKLFLSQILH 257
Cdd:TIGR01271 649 eaFDNFSAERRNSILTETLR 668
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
11-223 |
3.78e-09 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 56.72 E-value: 3.78e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 11 VSATEVAVEIVNMNKWYGDFHvlrdinLKV-----MRGERIVIAGPSGSGKSTMIRCINrleehqkGKIVVDGTELTNDL 85
Cdd:COG1245 335 EKEEETLVEYPDLTKSYGGFS------LEVeggeiREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEVDEDL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 86 K---KIDEVRREVGMVFQHFnLFPHLTilenctlapiwvRKMPKKQAEEvamHFLKRVKIPEQANKYPGQLSGGQQQRVA 162
Cdd:COG1245 402 KisyKPQYISPDYDGTVEEF-LRSANT------------DDFGSSYYKT---EIIKPLGLEKLLDKNVKDLSGGELQRVA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 502303547 163 IARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-GMTMLCVTHEMGFARQVANRVI 223
Cdd:COG1245 466 IAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENrGKTAMVVDHDIYLIDYISDRLM 527
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
47-211 |
5.03e-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: 54.54 E-value: 5.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 47 VIAGPSGSGKSTMIRCIN-----RLEEHQKGKIVVDgteltnDLKKIDEVRREVGMVFQHFN-----LFPHLTILENCtl 116
Cdd:cd03240 26 LIVGQNGAGKTTIIEALKyaltgELPPNSKGGAHDP------KLIREGEVRAQVKLAFENANgkkytITRSLAILENV-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 117 apIWVRKmpkkqaEEVamhflkRVKIPEQankyPGQLSGGQQQ------RVAIARSLCMNPKIMLFDEPTSALDPEMIKE 190
Cdd:cd03240 98 --IFCHQ------GES------NWPLLDM----RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEE 159
|
170 180
....*....|....*....|...
gi 502303547 191 VLDTMVG--LAEEGMTMLCVTHE 211
Cdd:cd03240 160 SLAEIIEerKSQKNFQLIVITHD 182
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
30-255 |
7.06e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.27 E-value: 7.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 30 FHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCI-NRLEEHQKGK---IVVDGTELtNDLKKidEVRREVGMVFQHFNLF 105
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIaSNTDGFHIGVegvITYDGITP-EEIKK--HYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 PHLTILENCTLA---------PIWV-RKMPKKQAEEVAMHF--LKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKI 173
Cdd:TIGR00956 151 PHLTVGETLDFAarcktpqnrPDGVsREEYAKHIADVYMATygLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKI 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 174 MLFDEPTSALDP----EMIKeVLDTMVGLAEegMTMLCVTHEmgfARQVA----NRVIFMDQGQIVEQNS---PAEFFDN 242
Cdd:TIGR00956 231 QCWDNATRGLDSatalEFIR-ALKTSANILD--TTPLVAIYQ---CSQDAyelfDKVIVLYEGYQIYFGPadkAKQYFEK 304
|
250
....*....|....*...
gi 502303547 243 -----PQHERTKLFLSQI 255
Cdd:TIGR00956 305 mgfkcPDRQTTADFLTSL 322
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
42-224 |
1.12e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.76 E-value: 1.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 42 RGERIVIAGPSGSGKSTMIRCI-NRLEEHQKGKIVVDGTELTNDLKKIDEVrrevgmvfqhfnlfphltilenctlapiw 120
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 121 vrkmpkkqaeevamhflkrvkipEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVG--- 197
Cdd:smart00382 52 -----------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrll 108
|
170 180 190
....*....|....*....|....*....|
gi 502303547 198 ---LAEEGMTMLCVTHEMGFARQVANRVIF 224
Cdd:smart00382 109 lllKSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
31-223 |
2.07e-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: 53.03 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMI----------RCINRLEE------HQKGKIVVDGTE-----LTNDLKKID 89
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAyarqflGQMDKPDVDSIEglspaIAIDQKTTS 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 90 E-VRREVGMVFQHFNLFPHLtilenctLAPIWVRKmpkkqaeevAMHFLKRVKIPE-QANKYPGQLSGGQQQRVAIARSL 167
Cdd:cd03270 89 RnPRSTVGTVTEIYDYLRLL-------FARVGIRE---------RLGFLVDVGLGYlTLSRSAPTLSGGEAQRIRLATQI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 502303547 168 CMNPK--IMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVI 223
Cdd:cd03270 153 GSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVI 209
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
31-236 |
3.66e-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: 3.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMI-----RCINRLEEHQKGKI----VVDGTELTNDLKKIDE----------- 90
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLHLKKEQPgnhdRIEGLEHIDKVIVIDQspigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 91 -----VRREVGMVF------QHFN------LFPHLTILEnctlapiwVRKMPKKQAEEvamhFLKrvKIPEQANKYP--- 150
Cdd:cd03271 89 atytgVFDEIRELFcevckgKRYNretlevRYKGKSIAD--------VLDMTVEEALE----FFE--NIPKIARKLQtlc 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 151 ---------GQ----LSGGQQQRVAIARSLCM---NPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGF 214
Cdd:cd03271 155 dvglgyiklGQpattLSGGEAQRIKLAKELSKrstGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDV 234
|
250 260
....*....|....*....|....*...
gi 502303547 215 ARqVANRVIFMDQ------GQIVEQNSP 236
Cdd:cd03271 235 IK-CADWIIDLGPeggdggGQVVASGTP 261
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
48-212 |
4.19e-08 |
|
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: 53.63 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 48 IAGPSGSGKSTMIRcinrleehqkgkiVVDGtELTNDLKKIDEvrrEVG--MVFQHFN---LFPHLTILENCTL----AP 118
Cdd:COG1245 104 ILGPNGIGKSTALK-------------ILSG-ELKPNLGDYDE---EPSwdEVLKRFRgteLQDYFKKLANGEIkvahKP 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 119 IWVRKMPK----------KQAEE--VAMHFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDpe 186
Cdd:COG1245 167 QYVDLIPKvfkgtvrellEKVDErgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD-- 244
|
170 180
....*....|....*....|....*....
gi 502303547 187 mIKE---VLDTMVGLAEEGMTMLCVTHEM 212
Cdd:COG1245 245 -IYQrlnVARLIRELAEEGKYVLVVEHDL 272
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
29-232 |
4.31e-08 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 52.51 E-value: 4.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 29 DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGteltndlkkidevrrEVGMVFQHFNLFPHL 108
Cdd:PRK13546 36 TFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAISAGLSGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 109 TILENCTLAPI---WVRKMPKKQAEEVAMHFLKRVKIPEQANKYpgqlSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP 185
Cdd:PRK13546 101 TGIENIEFKMLcmgFKRKEIKAMTPKIIEFSELGEFIYQPVKKY----SSGMRAKLGFSINITVNPDILVIDEALSVGDQ 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502303547 186 EMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRVIFMDQGQIVE 232
Cdd:PRK13546 177 TFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKD 223
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
32-211 |
9.42e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 52.54 E-value: 9.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIrciNRLEEHQKGKIVVDGTELTNDLKKIDEVRREVGMVFQHFNLFPHLTIL 111
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLM---DVLAGRKTGGYIEGDIRISGFPKKQETFARISGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENCTLAPIWvrKMPKKQAEEVAMHFLKRV-KIPEQAN------KYPG--QLSGGQQQRVAIARSLCMNPKIMLFDEPTSA 182
Cdd:PLN03140 972 ESLIYSAFL--RLPKEVSKEEKMMFVDEVmELVELDNlkdaivGLPGvtGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*....
gi 502303547 183 LDPEMIKEVLDTMVGLAEEGMTMLCVTHE 211
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
32-243 |
3.27e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 50.93 E-value: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDgteltndlkkidevrREVGMVfqhfnlfPHLTIL 111
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------------RSIAYV-------PQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENCTlapiwVRKMPKKQAEEVAMHFLKRVKIPE-QAN--KYPG-----------QLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:PTZ00243 733 MNAT-----VRGNILFFDEEDAARLADAVRVSQlEADlaQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQGQIVEQNSPAEFFDNP 243
Cdd:PTZ00243 808 DPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
47-210 |
4.71e-07 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 48.51 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 47 VIAGPSGSGKSTMIRCInrleehqkgkivvdgteltndlkkidevrrEVGMVFQHFNLFPHLTILENCTLApiwvrkmpk 126
Cdd:cd03227 25 IITGPNGSGKSTILDAI------------------------------GLALGGAQSATRRRSGVKAGCIVA--------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 127 kqAEEVAMHFLKrvkipeqankypGQLSGGQQQRVAIARSL----CMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEG 202
Cdd:cd03227 66 --AVSAELIFTR------------LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKG 131
|
....*...
gi 502303547 203 MTMLCVTH 210
Cdd:cd03227 132 AQVIVITH 139
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
18-210 |
5.23e-07 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 49.40 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 18 VEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQ--KGKIVVDGTELTnDLKKIDEVRREV 95
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDYEvtGGTVEFKGKDLL-ELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 96 GMVFQHFNLFPHLT---ILENCTLApiwVRKMpKKQAEEVAMHFLKRVKIPEQANKYPGQL---------SGGQQQRVAI 163
Cdd:PRK09580 81 FMAFQYPVEIPGVSnqfFLQTALNA---VRSY-RGQEPLDRFDFQDLMEEKIALLKMPEDLltrsvnvgfSGGEKKRNDI 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 502303547 164 ARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTH 210
Cdd:PRK09580 157 LQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
21-229 |
5.25e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 5.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 21 VNMNKWYG-DFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVvdgteLTNDLKkidevrreVGMVF 99
Cdd:PRK11819 10 NRVSKVVPpKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR-----PAPGIK--------VGYLP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 100 QHFNLFPHLTILENCTLApiwVRKMPKKQAE--EVAMHF----------------LK-------------RVKIPEQANK 148
Cdd:PRK11819 77 QEPQLDPEKTVRENVEEG---VAEVKAALDRfnEIYAAYaepdadfdalaaeqgeLQeiidaadawdldsQLEIAMDALR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 149 YP------GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIkEVLDTMvgLAEEGMTMLCVTHEMGFARQVANRV 222
Cdd:PRK11819 154 CPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV-AWLEQF--LHDYPGTVVAVTHDRYFLDNVAGWI 230
|
....*..
gi 502303547 223 IFMDQGQ 229
Cdd:PRK11819 231 LELDRGR 237
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
32-210 |
1.37e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.98 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEhqkgkivVDGTELTNDLKKidevrrevgmvfqhfNLF-----P 106
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWP-------VYGGRLTKPAKG---------------KLFyvpqrP 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 107 HLTI--LENCTLAPIWVRKMPKK---QAEEVAM-------HFLKRVKIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIM 174
Cdd:TIGR00954 525 YMTLgtLRDQIIYPDSSEDMKRRglsDKDLEQIldnvqltHILEREGGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFA 604
|
170 180 190
....*....|....*....|....*....|....*..
gi 502303547 175 LFDEPTSALDPEMikevLDTMVGLAEE-GMTMLCVTH 210
Cdd:TIGR00954 605 ILDECTSAVSVDV----EGYMYRLCREfGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
143-249 |
1.67e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 1.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 143 PEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDpemIKEVLDTMVGLAEEGMTMLCVTHEMGFARQVANRV 222
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
90 100
....*....|....*....|....*..
gi 502303547 223 IFMDQGQIVEQNSPAEFFDNPQHERTK 249
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERTREEQLK 438
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-186 |
1.88e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 16 VAVEIVNMNKWYGDFHVLRDINLKVMRGErIV-IAGPSGSGKSTMIRCINRLEEHQKGKIVVdGTelTNDLKKIDEVRRe 94
Cdd:PRK11819 323 KVIEAENLSKSFGDRLLIDDLSFSLPPGG-IVgIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GE--TVKLAYVDQSRD- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 95 vgmvfqhfNLFPHLTILENCT--LAPIWV--RKMPKKqAEEVAMHFlkrvKIPEQaNKYPGQLSGGQQQRVAIARSLCMN 170
Cdd:PRK11819 398 --------ALDPNKTVWEEISggLDIIKVgnREIPSR-AYVGRFNF----KGGDQ-QKKVGVLSGGERNRLHLAKTLKQG 463
|
170
....*....|....*.
gi 502303547 171 PKIMLFDEPTSALDPE 186
Cdd:PRK11819 464 GNVLLLDEPTNDLDVE 479
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
42-212 |
2.76e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 47.88 E-value: 2.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 42 RGERIVIAGPSGSGKSTMIRCI--------NRLEEHQKGKIVVD---GTELTNDLKKIDEVRREVGMVFQHFNLFPHLT- 109
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILsgelipnlGDYEEEPSWDEVLKrfrGTELQNYFKKLYNGEIKVVHKPQYVDLIPKVFk 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 110 -----ILENctlapIWVRKMPKKQAEEVAM-HFLKRvKIpeqankypGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSAL 183
Cdd:PRK13409 178 gkvreLLKK-----VDERGKLDEVVERLGLeNILDR-DI--------SELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243
|
170 180 190
....*....|....*....|....*....|..
gi 502303547 184 DpemIKE---VLDTMVGLAeEGMTMLCVTHEM 212
Cdd:PRK13409 244 D---IRQrlnVARLIRELA-EGKYVLVVEHDL 271
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
27-230 |
2.95e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.86 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 27 YGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIvvdgtELTNDLKkidevrreVGMVFQHFNLF- 105
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-----GLAKGIK--------LGYFAQHQLEFl 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 106 -------PHLTilencTLAPiwvrKMPKKQAEEVAMHF-LKRVKIPEQAnkypGQLSGGQQQRVAIARSLCMNPKIMLFD 177
Cdd:PRK10636 389 radesplQHLA-----RLAP----QELEQKLRDYLGGFgFQGDKVTEET----RRFSGGEKARLVLALIVWQRPNLLLLD 455
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 502303547 178 EPTSALDPEMIKEVLDTMVGLaeEGmTMLCVTHEMGFARQVANRVIFMDQGQI 230
Cdd:PRK10636 456 EPTNHLDLDMRQALTEALIDF--EG-ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
153-238 |
4.82e-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: 47.32 E-value: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 153 LSGGQQQRVAIARSL---CMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFARQvANRVIFMDQ-- 227
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYIIDLGPeg 908
|
90
....*....|....*
gi 502303547 228 ----GQIVEQNSPAE 238
Cdd:TIGR00630 909 gdggGTVVASGTPEE 923
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-238 |
1.60e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 45.89 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 17 AVEIVNMNKWYGDFHVLRDINLKVMRGERIVIAGPSGSGKSTMI------RCInrleehQKGKIVVdgteLTNDLKKIDE 90
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLsliagaRKI------QQGRVEV----LGGDMADARH 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 91 vRREVG-----MVfQHF--NLFPHLTILEN------------------------CT-LAPiwvrkmpkkqaeevamhFLK 138
Cdd:NF033858 71 -RRAVCpriayMP-QGLgkNLYPTLSVFENldffgrlfgqdaaerrrridellrATgLAP-----------------FAD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 139 RvkipeqankyP-GQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDP-------EMIKEVLDTMvglaeEGMTMLCVTH 210
Cdd:NF033858 132 R----------PaGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDPlsrrqfwELIDRIRAER-----PGMSVLVATA 196
|
250 260 270
....*....|....*....|....*....|..
gi 502303547 211 EM----GFARQVAnrvifMDQGQIVEQNSPAE 238
Cdd:NF033858 197 YMeeaeRFDWLVA-----MDAGRVLATGTPAE 223
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
153-257 |
1.63e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 45.98 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 153 LSGGQQQRVAIARSLC--MNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTHEMGFArQVANRVIFMDQ--- 227
Cdd:PRK00635 477 LSGGEQERTALAKHLGaeLIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMI-SLADRIIDIGPgag 555
|
90 100 110
....*....|....*....|....*....|...
gi 502303547 228 ---GQIVEQNSPAEFFDNpQHERTKLFLSQILH 257
Cdd:PRK00635 556 ifgGEVLFNGSPREFLAK-SDSLTAKYLRQELT 587
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
32-210 |
2.52e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 32 VLRDINLKVMRGERIVIAGPSGSGKSTMIRCINRLEEHQKGKIVVDGTELTNDLKKIdevrreVGMVFQHFNLFPHLTIL 111
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY------CTYIGHNLGLKLEMTVF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 112 ENCTLapiWVRKMPKKQAEEVAMHFLKrvkIPEQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEV 191
Cdd:PRK13541 89 ENLKF---WSEIYNSAETLYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLL 162
|
170
....*....|....*....
gi 502303547 192 LDTMVGLAEEGMTMLCVTH 210
Cdd:PRK13541 163 NNLIVMKANSGGIVLLSSH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
31-223 |
4.82e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.43 E-value: 4.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTMIR-----CINRL-EEHQKGKIVVDGTEL------TNDL------------- 85
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpAVEEFiEQGFCSNLSIQWGAIsrlvhiTRDLpgrsqrsipltyi 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 86 KKIDEVR---------REVGMVFQHFNL------------FPHLTILENCTLAP-------------IWVRKMPKKQAEE 131
Cdd:PRK00635 689 KAFDDLRelfaeqprsKRLGLTKSHFSFntplgacaecqgLGSITTTDNRTSIPcpsclgkrflpqvLEVRYKGKNIADI 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 132 VAM-------HFLKRVKIPEQANKY------------P-GQLSGGQQQRVAIARSLCM---NPKIMLFDEPTSALDPEMI 188
Cdd:PRK00635 769 LEMtayeaekFFLDEPSIHEKIHALcslgldylplgrPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDI 848
|
250 260 270
....*....|....*....|....*....|....*
gi 502303547 189 KEVLDTMVGLAEEGMTMLCVTHEMGFARqVANRVI 223
Cdd:PRK00635 849 KALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVL 882
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
129-230 |
1.00e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 1.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 129 AEEVAMHFLKRVKIP-EQANKYPGQLSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTmvgLAEEGMTMLC 207
Cdd:PRK15064 131 AEARAGELLLGVGIPeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDV---LNERNSTMII 207
|
90 100
....*....|....*....|...
gi 502303547 208 VTHEMGFARQVANRVIFMDQGQI 230
Cdd:PRK15064 208 ISHDRHFLNSVCTHMADLDYGEL 230
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
150-210 |
2.00e-04 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 41.99 E-value: 2.00e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 502303547 150 PGQLSGGQQQ---RVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEEGMTMLCVTH 210
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
31-58 |
2.75e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.75e-04
10 20
....*....|....*....|....*...
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKST 58
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
153-211 |
3.46e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 41.77 E-value: 3.46e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 153 LSGGQQQRVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVgLAEEGMTMlcVTHE 211
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLV-LFQGGVLM--VSHD 683
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
126-254 |
9.01e-04 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 40.38 E-value: 9.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 126 KKQAEEVAMHFLKRVKI----------PEQAnkyPGQLSGGQQQRVAIARSLC--MNPKIMLFDEPTSALDPEMIKEVLD 193
Cdd:TIGR00630 455 KKIAEEVLKEIRERLGFlidvgldylsLSRA---AGTLSGGEAQRIRLATQIGsgLTGVLYVLDEPSIGLHQRDNRRLIN 531
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 502303547 194 TMVGLAEEGMTMLCVTHEMGFARqVANRVIFMDQ------GQIVEQNSPAEFFDNPqHERTKLFLSQ 254
Cdd:TIGR00630 532 TLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIGPgagehgGEVVASGTPEEILANP-DSLTGQYLSG 596
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
31-59 |
1.04e-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: 40.00 E-value: 1.04e-03
10 20
....*....|....*....|....*....
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKSTM 59
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
31-58 |
1.99e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.29 E-value: 1.99e-03
10 20
....*....|....*....|....*...
gi 502303547 31 HVLRDINLKVMRGERIVIAGPSGSGKST 58
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSS 41
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
45-63 |
3.05e-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: 37.50 E-value: 3.05e-03
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
151-214 |
4.48e-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: 38.10 E-value: 4.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 502303547 151 GQLSGGQQQ------RVAIARSLCMNPKIMLFDEPTSALDPEMIKEVLDTMVGLAEE-----GMTMLCVTHEMGF 214
Cdd:TIGR00606 1198 GRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENIESLAHALVEIIKSrsqqrNFQLLVITHDEDF 1272
|
|
| TrwB_TraG_TraD_VirD4 |
cd01127 |
TrwB/TraG/TraD/VirD4 family of bacterial conjugation proteins; The TraG/TraD/VirD4 family are ... |
46-76 |
4.57e-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: 4.57e-03
10 20 30
....*....|....*....|....*....|.
gi 502303547 46 IVIAGPSGSGKSTMIRCINRLEEHQKGKIVV 76
Cdd:cd01127 2 TLVLGTTGSGKTTSIVIPLLDQAARGGSVII 32
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
151-196 |
4.67e-03 |
|
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.
Pssm-ID: 463921 [Multi-domain] Cd Length: 90 Bit Score: 35.29 E-value: 4.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 502303547 151 GQLSGGQQQR---VAIARSLCM----------NPKIMLFDEPTSALDPEMIKEVLDTMV 196
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLR 89
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
46-75 |
5.36e-03 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 37.38 E-value: 5.36e-03
10 20 30
....*....|....*....|....*....|....
gi 502303547 46 IVIAGPSGSGKST----MIRCINRleeHQKGKIV 75
Cdd:COG2805 128 VLVTGPTGSGKSTtlaaMIDYINE---TRAKHII 158
|
|
| GMPK |
cd00071 |
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), ... |
46-65 |
6.32e-03 |
|
Guanosine monophosphate kinase (GMPK, EC 2.7.4.8), also known as guanylate kinase (GKase), catalyzes the reversible phosphoryl transfer from adenosine triphosphate (ATP) to guanosine monophosphate (GMP) to yield adenosine diphosphate (ADP) and guanosine diphosphate (GDP). It plays an essential role in the biosynthesis of guanosine triphosphate (GTP). This enzyme is also important for the activation of some antiviral and anticancer agents, such as acyclovir, ganciclovir, carbovir, and thiopurines.
Pssm-ID: 238026 Cd Length: 137 Bit Score: 35.97 E-value: 6.32e-03
|
| AAA |
cd00009 |
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ... |
46-92 |
7.56e-03 |
|
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.
Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 35.97 E-value: 7.56e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 502303547 46 IVIAGPSGSGKSTMIRCI-NRLEEHQKGKIVVDGTELTNDLKKIDEVR 92
Cdd:cd00009 22 LLLYGPPGTGKTTLARAIaNELFRPGAPFLYLNASDLLEGLVVAELFG 69
|
|
| ExeA |
COG3267 |
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ... |
40-69 |
8.19e-03 |
|
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];
Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 36.69 E-value: 8.19e-03
10 20 30
....*....|....*....|....*....|..
gi 502303547 40 VMRGER-IVIAGPSGSGKSTMIRC-INRLEEH 69
Cdd:COG3267 39 LAQGGGfVVLTGEVGTGKTTLLRRlLERLPDD 70
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
154-232 |
8.30e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 37.46 E-value: 8.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 502303547 154 SGGQQQRVAIARSLCMNPKIMLFDEPTSALDpemikevLDTMVGLAE-----EGmTMLCVTHEMGFARQVANRVIFMDQG 228
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLD-------LDAVIWLEKwlksyQG-TLILISHDRDFLDPIVDKIIHIEQQ 222
|
....
gi 502303547 229 QIVE 232
Cdd:PRK10636 223 SLFE 226
|
|
| Gmk |
COG0194 |
Guanylate kinase [Nucleotide transport and metabolism]; |
46-69 |
8.35e-03 |
|
Guanylate kinase [Nucleotide transport and metabolism];
Pssm-ID: 439964 Cd Length: 190 Bit Score: 36.20 E-value: 8.35e-03
10 20
....*....|....*....|....
gi 502303547 46 IVIAGPSGSGKSTMIRCInrLEEH 69
Cdd:COG0194 5 IVLSGPSGAGKTTLVKAL--LERD 26
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
46-96 |
9.28e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 35.58 E-value: 9.28e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 502303547 46 IVIAGPSGSGKSTMIRcinrleEHQKGKIVVDgteltndlkkIDEVRREVG 96
Cdd:COG4639 5 VVLIGLPGSGKSTFAR------RLFAPTEVVS----------SDDIRALLG 39
|
|
| gmk |
PRK00300 |
guanylate kinase; Provisional |
41-63 |
9.30e-03 |
|
guanylate kinase; Provisional
Pssm-ID: 234719 Cd Length: 205 Bit Score: 36.22 E-value: 9.30e-03
|
| |
