|
Name |
Accession |
Description |
Interval |
E-value |
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-244 |
1.92e-176 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 484.11 E-value: 1.92e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIRRKVG 85
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLGQI 244
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRAFLSKV 239
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-219 |
6.86e-142 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 396.13 E-value: 6.86e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIRRKVGM 86
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-241 |
4.02e-117 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 335.23 E-value: 4.02e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAI--IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT------- 71
Cdd:COG4598 1 MTDTAPpaLEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdg 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 72 ----DDVKAVEKIRRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQ 147
Cdd:COG4598 81 elvpADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 148 QRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG4598 161 QRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAE 240
|
250
....*....|....
gi 2504588632 228 FFENPKSERTRQFL 241
Cdd:COG4598 241 VFGNPKSERLRQFL 254
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-241 |
1.68e-115 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 330.13 E-value: 1.68e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIRRKVG 85
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIRQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:PRK09493 81 MVFQQFYLFPHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-241 |
6.06e-98 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 285.75 E-value: 6.06e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG----IELTDDVKAVEKIRR 82
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdFSKTPSDKAIRELRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSpAEFFENPKSERTRQFL 241
Cdd:PRK11124 163 LLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD-ASCFTQPQTEAFKNYL 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-241 |
1.96e-96 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 281.90 E-value: 1.96e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIEL----TDDVKAVEKIRR 82
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqKPSEKAIRLLRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSpAEFFENPKSERTRQFL 241
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTEAFAHYL 240
|
|
| ectoine_ehuA |
TIGR03005 |
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ... |
7-246 |
9.58e-95 |
|
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.
Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 278.25 E-value: 9.58e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-----------DVK 75
Cdd:TIGR03005 1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHmpgrngplvpaDEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 76 AVEKIRRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARA 155
Cdd:TIGR03005 81 HLRQMRNKIGMVFQSFNLFPHKTVLDNVTEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 156 LCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKS 234
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEhDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240
|
250
....*....|..
gi 2504588632 235 ERTRQFLGQILE 246
Cdd:TIGR03005 241 ERTREFLSKVIA 252
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-247 |
3.12e-92 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 274.65 E-value: 3.12e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNS----YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKI 80
Cdd:COG1135 1 MIELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENVAL-PLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQ 239
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRR 239
|
....*...
gi 2504588632 240 FLGQILEH 247
Cdd:COG1135 240 FLPTVLND 247
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
5-245 |
1.45e-90 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 267.39 E-value: 1.45e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIE------LTDDVKAVE 78
Cdd:PRK11264 2 SAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarsLSQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCM 158
Cdd:PRK11264 82 QLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 159 RPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTR 238
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTR 241
|
....*..
gi 2504588632 239 QFLGQIL 245
Cdd:PRK11264 242 QFLEKFL 248
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-221 |
4.36e-85 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 252.66 E-value: 4.36e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWY----NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVE 78
Cdd:COG1136 2 SPLLELRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSlSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRR-KVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALC 157
Cdd:COG1136 82 RLRRrHIGFVFQFFNLLPELTALENVAL-PLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQvADSIVFMAEGSIIE 221
Cdd:COG1136 161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-241 |
1.22e-84 |
|
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: 251.82 E-value: 1.22e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 2 TENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKI 80
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:COG1127 81 RRRIGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPkSERTRQ 239
Cdd:COG1127 161 EILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQ 239
|
..
gi 2504588632 240 FL 241
Cdd:COG1127 240 FL 241
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-241 |
4.18e-84 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 251.43 E-value: 4.18e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTEN--AIIELRKVgkwYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT------- 71
Cdd:PRK10619 1 MSENklNVIDLHKR---YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdg 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 72 ----DDVKAVEKIRRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAH-KFPGQLSGGQ 146
Cdd:PRK10619 78 qlkvADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 147 QQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPA 226
Cdd:PRK10619 158 QQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPE 237
|
250
....*....|....*
gi 2504588632 227 EFFENPKSERTRQFL 241
Cdd:PRK10619 238 QLFGNPQSPRLQQFL 252
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
6-241 |
7.40e-84 |
|
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: 250.29 E-value: 7.40e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL-----EAHQTGHIVVDGIELTDDVKAVEKI 80
Cdd:TIGR00972 1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRSLNRMndlvpGVRIEGKVLFDGQDIYDKKIDVVEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPhLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQ----AHKFPGQLSGGQQQRVAIARAL 156
Cdd:TIGR00972 81 RRRVGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELDEIVEESLKKAALWDEvkdrLHDSALGLSGGQQQRLCIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 157 CMRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSER 236
Cdd:TIGR00972 160 AVEPEVLLLDEPTSALDPIATGKIEELIQELK-KKYTIVIVTHNMQQAARISDRTAFFYDGELVEYGPTEQIFTNPKEKR 238
|
....*
gi 2504588632 237 TRQFL 241
Cdd:TIGR00972 239 TEDYI 243
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
5-244 |
7.28e-82 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 248.86 E-value: 7.28e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVEKIRRKV 84
Cdd:COG3842 4 PALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDG----RDVTGLPPEKRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQN----LTlapiwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:COG3842 80 GMVFQDYALFPHLTVAENvafgLR-----MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 161 EIMLFDEPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSER 236
Cdd:COG3842 155 RVLLLDEPLSALDAklreEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRF 231
|
....*...
gi 2504588632 237 TRQFLGQI 244
Cdd:COG3842 232 VADFIGEA 239
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-233 |
9.50e-81 |
|
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: 241.85 E-value: 9.50e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVG 85
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK--KNLRELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQN-FN-LFpHLTVLQNLTLAPIwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:COG1122 79 LVFQNpDDqLF-APTVEEDVAFGPE-NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPK 233
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-228 |
1.23e-80 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 242.27 E-value: 1.23e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT-DDVKAVEKIRR 82
Cdd:COG3638 1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTaLRGRALRRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQNFNLFPHLTVLQN-LT--LA--PIW--VRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARA 155
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNvLAgrLGrtSTWrsLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 156 LCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:COG3638 161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-233 |
4.68e-80 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 240.18 E-value: 4.68e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWY----NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKI 80
Cdd:cd03258 1 MIELKNVSKVFgdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVAL-PLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPK 233
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-219 |
1.87e-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: 238.16 E-value: 1.87e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY----NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIR 81
Cdd:cd03255 1 IELKNLSKTYggggEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKlSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RK-VGMVFQNFNLFPHLTVLQNLTLAPIwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLL-LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQvADSIVFMAEGSI 219
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-223 |
4.42e-78 |
|
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: 234.34 E-value: 4.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVEKIRRKVGM 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDG----RDVTGVPPERRNIGM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03259 77 VFQDYALFPHLTVAENIAF-GLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 167 EPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03259 156 EPLSALDAklreELREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-245 |
4.63e-78 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 238.93 E-value: 4.63e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY----NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIR 81
Cdd:PRK11153 2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RKVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPE 161
Cdd:PRK11153 82 RQIGMIFQHFNLLSSRTVFDNVAL-PLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 162 IMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQF 240
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
|
....*
gi 2504588632 241 LGQIL 245
Cdd:PRK11153 241 IQSTL 245
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-241 |
6.20e-77 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 240.96 E-value: 6.20e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSY-----HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEK 79
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 80 IRRKVGMVFQNFN--LFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRI-PDQAHKFPGQLSGGQQQRVAIARAL 156
Cdd:COG1123 340 LRRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 157 CMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSE 235
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499
|
....*.
gi 2504588632 236 RTRQFL 241
Cdd:COG1123 500 YTRALL 505
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-217 |
9.88e-77 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 229.77 E-value: 9.88e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIRRKVGM 86
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLApiwvrgmakseieeiammylkrvripdqahkfpgqLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03229 81 VFQDFALFPHLTVLENIALG-----------------------------------LSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 167 EPTSALDPEMVKEVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLqAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-241 |
2.43e-75 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 229.15 E-value: 2.43e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 2 TENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL-----EAHQTGHIVVDGIELTDDVKA 76
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipGARVEGEILLDGEDIYDPDVD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 77 VEKIRRKVGMVFQNFNLFPHlTVLQNLTLAPIwVRGMA-KSEIEEIAMMYLKRVRIPDQA----HKFPGQLSGGQQQRVA 151
Cdd:COG1117 87 VVELRRRVGMVFQKPNPFPK-SIYDNVAYGLR-LHGIKsKSELDEIVEESLRKAALWDEVkdrlKKSALGLSGGQQQRLC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 152 IARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEgMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:COG1117 165 IARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTN 243
|
250
....*....|
gi 2504588632 232 PKSERTRQFL 241
Cdd:COG1117 244 PKDKRTEDYI 253
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-228 |
4.55e-75 |
|
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: 227.06 E-value: 4.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQ-----TGHIVVDGIELTDDVKAVEKIR 81
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RKVGMVFQNFNLFPhLTVLQNLTLAPiWVRGMA-KSEIEEIAMMYLKRVRIPDQAHK--FPGQLSGGQQQRVAIARALCM 158
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGL-RLHGIKlKEELDERVEEALRKAALWDEVKDrlHALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 159 RPEIMLFDEPTSALDPEMVKEVLDVMTELAGEgMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-228 |
4.98e-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: 227.45 E-value: 4.98e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDD-VKAVEKIRRKV 84
Cdd:cd03256 1 IEVENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLkGKALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTLA-----PIWvRGMAK--SEIE-EIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARAL 156
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGrlgrrSTW-RSLFGlfPKEEkQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 157 CMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-242 |
1.19e-74 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 230.42 E-value: 1.19e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEkirRKVGM 86
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRE---RRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQN----LTlapiwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:COG1118 80 VFQHYALFPHMTVAENiafgLR-----VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 163 MLFDEPTSALD----PEMVKEVLDVMTELAGegmTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTR 238
Cdd:COG1118 155 LLLDEPFGALDakvrKELRRWLRRLHDELGG---TTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVA 231
|
....
gi 2504588632 239 QFLG 242
Cdd:COG1118 232 RFLG 235
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-227 |
1.60e-74 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 225.70 E-value: 1.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRRK 83
Cdd:COG2884 1 MIRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlKRREIPYLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:COG2884 81 IGVVFQDFRLLPDRTVYENVAL-PLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG2884 160 LADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-221 |
1.01e-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: 224.97 E-value: 1.01e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTEN-AIIELRKVGKWYNS----YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvK 75
Cdd:COG1116 1 MSAAaPALELRGVSKRFPTggggVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG-------K 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 76 AVEKIRRKVGMVFQNFNLFPHLTVLQNLTLAPIwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARA 155
Cdd:COG1116 74 PVTGPGPDRGVVFQEPALLPWLTVLDNVALGLE-LRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 156 LCMRPEIMLFDEPTSALDP----EMVKEVLDVMTElagEGMTMVCVTHEMGFARQVADSIVFMAE--GSIIE 221
Cdd:COG1116 153 LANDPEVLLMDEPFGALDAltreRLQDELLRLWQE---TGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
5-242 |
1.98e-73 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 227.26 E-value: 1.98e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVEKIRRKV 84
Cdd:COG3839 2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGG----RDVTDLPPKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAF-PLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 165 FDEPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEmgfarQV-----ADSIVFMAEGSIIESGSPAEFFENPKSE 235
Cdd:COG3839 157 LDEPLSNLDAklrvEMRAEIKRLHRRL---GTTTIYVTHD-----QVeamtlADRIAVMNDGRIQQVGTPEELYDRPANL 228
|
....*..
gi 2504588632 236 RTRQFLG 242
Cdd:COG3839 229 FVAGFIG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-228 |
3.88e-73 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 222.63 E-value: 3.88e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekiRRKVGM 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV---RRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:COG1131 78 VPQEPALYPDLTVRENLRFF-ARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:COG1131 157 EPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-240 |
5.02e-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: 222.38 E-value: 5.02e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKA-VEKIRRKVG 85
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAeLYRLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTLaPIWVRG-MAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:cd03261 81 MLFQSGALFDSLTVFENVAF-PLREHTrLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPkSERTRQF 240
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQF 235
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-228 |
9.23e-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: 216.78 E-value: 9.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNS-YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRRK 83
Cdd:TIGR02315 1 MLEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlRGKKLRKLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNL---------TLAPIWvrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIAR 154
Cdd:TIGR02315 81 IGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLL--GRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIAR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 155 ALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:TIGR02315 159 ALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSEL 233
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
21-240 |
1.01e-70 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 217.51 E-value: 1.01e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRRK-VGMVFQNFNLFPHLT 98
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmSRKELRELRRKkISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDP---- 174
Cdd:cd03294 119 VLENVAF-GLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPlirr 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 175 EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQF 240
Cdd:cd03294 198 EMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREF 260
|
|
| ProV |
COG4175 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
21-240 |
1.39e-69 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 218.43 E-value: 1.39e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRR-KVGMVFQNFNLFPHLT 98
Cdd:COG4175 42 GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKlSKKELRELRRkKMSMVFQHFALLPHRT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDP---- 174
Cdd:COG4175 122 VLENVAF-GLEIQGVPKAERRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirr 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 175 EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQF 240
Cdd:COG4175 201 EMQDELLELQAKL---KKTIVFITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADF 263
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-242 |
8.67e-69 |
|
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: 211.97 E-value: 8.67e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYH----ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRR 82
Cdd:COG1124 2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR--RRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQN----FNlfPHLTVLQnlTLA-PIWVRGMAKSEiEEIAMMyLKRVRIP-DQAHKFPGQLSGGQQQRVAIARAL 156
Cdd:COG1124 80 RVQMVFQDpyasLH--PRHTVDR--ILAePLRIHGLPDRE-ERIAEL-LEQVGLPpSFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 157 CMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSE 235
Cdd:COG1124 154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
|
....*..
gi 2504588632 236 RTRQFLG 242
Cdd:COG1124 234 YTRELLA 240
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-243 |
1.36e-68 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 211.39 E-value: 1.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYH-ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVG 85
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIRE--QDPVELRRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTLAPIwVRGMAKSEIEEIAMMYLKRVRIPDQ--AHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:cd03295 79 YVIQQIGLFPHMTVEENIALVPK-LLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 164 LFDEPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQ 239
Cdd:cd03295 158 LMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234
|
....
gi 2504588632 240 FLGQ 243
Cdd:cd03295 235 FVGA 238
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-217 |
1.90e-68 |
|
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: 209.63 E-value: 1.90e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 8 ELRKVGKWYNSYH--ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVG 85
Cdd:cd03225 1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTK--LSLKELRRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNL-FPHLTVLQNLTLAPIwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:cd03225 79 LVFQNPDDqFFGPTVEEEVAFGLE-NLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:cd03225 158 LDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-221 |
5.47e-68 |
|
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: 208.87 E-value: 5.47e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY----NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvKAVEKIRR 82
Cdd:cd03293 1 LEVRNVSKTYggggGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-------EPVTGPGP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:cd03293 74 DRGYVFQQDALLPWLTVLDNVAL-GLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 163 MLFDEPTSALDP----EMVKEVLDVMTElagEGMTMVCVTHEMGFARQVADSIVFMAE--GSIIE 221
Cdd:cd03293 153 LLLDEPFSALDAltreQLQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-242 |
6.54e-68 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 209.02 E-value: 6.54e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkaVEKIRRKVGM 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN----LPPHKRPVNT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03300 77 VFQNYALFPHLTVFENIAF-GLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLD 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLG 242
Cdd:cd03300 156 EPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-223 |
7.43e-68 |
|
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: 208.90 E-value: 7.43e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWY----NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIR 81
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RK-VGMVFQN----FNlfPHLTVLQNLTlAPIWVRGM--AKSEIEEIAMMYLKRVRIPDQ-AHKFPGQLSGGQQQRVAIA 153
Cdd:cd03257 81 RKeIQMVFQDpmssLN--PRMTIGEQIA-EPLRIHGKlsKKEARKEAVLLLLVGVGLPEEvLNRYPHELSGGQRQRVAIA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 154 RALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03257 158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
7-243 |
1.06e-67 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 211.10 E-value: 1.06e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYH-ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGiELTDDVKAVEkIRRKVG 85
Cdd:COG1125 2 IEFENVTKRYPDGTvAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDG-EDIRDLDPVE-LRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTLAPIwVRGMAKSEIEEIAMMYLKRVRI-PDQ-AHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:COG1125 80 YVIQQIGLFPHMTVAENIATVPR-LLGWDKERIRARVDELLELVGLdPEEyRDRYPHELSGGQQQRVGVARALAADPPIL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 164 LFDEPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQ 239
Cdd:COG1125 159 LMDEPFGALDPitreQLQDELLRLQREL---GKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVAD 235
|
....
gi 2504588632 240 FLGQ 243
Cdd:COG1125 236 FVGA 239
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
7-244 |
3.41e-66 |
|
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: 208.74 E-value: 3.41e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAvekiRRKVGM 86
Cdd:TIGR03265 5 LSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ----KRDYGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLT--LAPiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:TIGR03265 81 VFQSYALFPNLTVADNIAygLKN---RGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 165 FDEPTSALDPEmVKEVLdvMTELAG----EGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQF 240
Cdd:TIGR03265 158 LDEPLSALDAR-VREHL--RTEIRQlqrrLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADF 234
|
....
gi 2504588632 241 LGQI 244
Cdd:TIGR03265 235 VGEV 238
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-229 |
6.47e-65 |
|
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: 202.66 E-value: 6.47e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIElTDDVKAVEKIRRKV 84
Cdd:TIGR04520 1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD-TLDEENLWEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQN-FNLFPHLTV-------LQNLtlapiwvrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARAL 156
Cdd:TIGR04520 80 GMVFQNpDNQFVGATVeddvafgLENL--------GVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 157 CMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFF 229
Cdd:TIGR04520 152 AMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIF 224
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
20-234 |
8.66e-65 |
|
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: 8.66e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL---EAHQTGHIVVDGIELTDdvkAVEKIR-RKVGMVFQNF--NL 93
Cdd:COG1123 20 PAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLE---LSEALRgRRIGMVFQDPmtQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 FPhLTVLQNLTLAPIwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALD 173
Cdd:COG1123 97 NP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 174 PEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKS 234
Cdd:COG1123 175 VTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA 236
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-243 |
7.18e-64 |
|
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: 199.10 E-value: 7.18e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVEKIRRKVGM 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGG----EDATDVPVQERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQN----LTLAPIWVRGmAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:cd03296 79 VFQHYALFRHMTVFDNvafgLRVKPRSERP-PEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFL 237
|
..
gi 2504588632 242 GQ 243
Cdd:cd03296 238 GE 239
|
|
| proV |
TIGR01186 |
glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ... |
21-244 |
1.74e-62 |
|
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: 199.69 E-value: 1.74e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT--DDVKAVEKIRRKVGMVFQNFNLFPHLT 98
Cdd:TIGR01186 8 GVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMkqSPVELREVRRKKIGMVFQQFALFPHMT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLAPiWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVK 178
Cdd:TIGR01186 88 ILQNTSLGP-ELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSALDPLIRD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 179 EVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLGQI 244
Cdd:TIGR01186 167 SMQDELKKLqATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKV 233
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-233 |
3.30e-62 |
|
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: 197.58 E-value: 3.30e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSY----HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLE---AHQTGHIVVDGIELTD-DVKAV 77
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLpppGITSGEILFDGEDLLKlSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 78 EKIR-RKVGMVFQN----FNlfPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPD---QAHKFPGQLSGGQQQR 149
Cdd:COG0444 81 RKIRgREIQMIFQDpmtsLN--PVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 150 VAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*
gi 2504588632 229 FENPK 233
Cdd:COG0444 239 FENPR 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-233 |
5.18e-62 |
|
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: 194.19 E-value: 5.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdVKAVEKIRRKVGM 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-LPPHEIARLGIGR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLAPIWVRG---------MAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALC 157
Cdd:cd03219 80 TFQIPRLFPELTVLENVMVAAQARTGsglllararREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPK 233
Cdd:cd03219 160 TDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
7-243 |
5.41e-61 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 191.51 E-value: 5.41e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHAlrDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAvekiRRKVGM 86
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPA----ERPVSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQN--LTLAPiwvrGM-----AKSEIEEIAmmylKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMR 159
Cdd:COG3840 76 LFQENNLFPHLTVAQNigLGLRP----GLkltaeQRAQVEQAL----ERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 160 PEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTR 238
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALA 227
|
....*
gi 2504588632 239 QFLGQ 243
Cdd:COG3840 228 AYLGI 232
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
7-233 |
2.59e-60 |
|
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: 191.13 E-value: 2.59e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYN-----SYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT-DDVKAVEKI 80
Cdd:TIGR04521 1 IKLKNVSYIYQpgtpfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITaKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQnfnlFPH-----LTVL-------QNLtlapiwvrGMAKSEIEEIAMMYLKRVRIP-DQAHKFPGQLSGGQQ 147
Cdd:TIGR04521 81 RKKVGLVFQ----FPEhqlfeETVYkdiafgpKNL--------GLSEEEAEERVKEALELVGLDeEYLERSPFELSGGQM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 148 QRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPA 226
Cdd:TIGR04521 149 RRVAIAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPR 228
|
....*..
gi 2504588632 227 EFFENPK 233
Cdd:TIGR04521 229 EVFSDVD 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-247 |
1.90e-59 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 187.99 E-value: 1.90e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvKAVEKI 80
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG-------KPPRRA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNL---FPhLTVLQnLTLAPIWVR----GMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIA 153
Cdd:COG1121 74 RRRIGYVPQRAEVdwdFP-ITVRD-VVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 154 RALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGsIIESGSPAEFFENPK 233
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPEN 230
|
250
....*....|....
gi 2504588632 234 SERTRQFLGQILEH 247
Cdd:COG1121 231 LSRAYGGPVALLAH 244
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-244 |
4.19e-59 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 190.68 E-value: 4.19e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVEKIRRKVGM 86
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHG----TDVSRLHARDRKVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQN----LTLAPIWVRGMAKsEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK10851 79 VFQHYALFRHMTVFDNiafgLTVLPRRERPNAA-AIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK10851 158 LLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFM 237
|
...
gi 2504588632 242 GQI 244
Cdd:PRK10851 238 GEV 240
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
6-217 |
1.79e-58 |
|
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: 184.37 E-value: 1.79e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYN-SYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRRK 83
Cdd:TIGR02673 1 MIEFHNVSKAYPgGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRlRGRQLPLLRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVAL-PLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:TIGR02673 160 LADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRVAHRVIILDDG 213
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-217 |
6.35e-58 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 183.09 E-value: 6.35e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGM 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSA--MPPPEWRRQVAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHlTVLQNLTLaPIWVRGMAKSEieEIAMMYLKRVRIPDQA-HKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPF-PFQLRERKFDR--ERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:COG4619 155 DEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-227 |
1.18e-57 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 183.71 E-value: 1.18e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdVKAVEkIRRKVG 85
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLAS-LSRRE-LARRIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTL--APiWVRGMAK--SEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPE 161
Cdd:COG1120 79 YVPQEPPAPFGLTVRELVALgrYP-HLGLFGRpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 162 IMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG1120 158 LLLLDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
5-233 |
2.87e-57 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 182.93 E-value: 2.87e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKv 84
Cdd:COG0411 3 PLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITG--LPPHRIARL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMV--FQNFNLFPHLTVLQNLTLA--------------PIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQ 148
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLVAaharlgrgllaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 149 RVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239
|
....*.
gi 2504588632 228 FFENPK 233
Cdd:COG0411 240 VRADPR 245
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-231 |
1.66e-56 |
|
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: 180.44 E-value: 1.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltDDVKAVEKIRRKVGM 86
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGE---DVRKEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYF-AELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
5-242 |
2.16e-56 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 179.79 E-value: 2.16e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdVKAVEKIRRKV 84
Cdd:COG0410 2 PMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITG-LPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEiEEIAMMY-----LKRvRIPDQAhkfpGQLSGGQQQRVAIARALCMR 159
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVR-ADLERVYelfprLKE-RRRQRA----GTLSGGEQQMLAIGRALMSR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 160 PEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPksERTRQ 239
Cdd:COG0410 155 PKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADP--EVREA 232
|
...
gi 2504588632 240 FLG 242
Cdd:COG0410 233 YLG 235
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-244 |
2.51e-56 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 184.00 E-value: 2.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkaVEKI 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITH----VPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:PRK09452 85 NRHVNTVFQSYALFPHMTVFENVAFG-LRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQ 239
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVAR 243
|
....*
gi 2504588632 240 FLGQI 244
Cdd:PRK09452 244 FIGEI 248
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-228 |
2.65e-56 |
|
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: 179.17 E-value: 2.65e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdVKAVEKIRRKVGM 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITG-LPPHERARAGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLApIWVRGMAKSEiEEIAMMY-----LKRVRipdqaHKFPGQLSGGQQQRVAIARALCMRPE 161
Cdd:cd03224 80 VPEGRRIFPELTVEENLLLG-AYARRRAKRK-ARLERVYelfprLKERR-----KQLAGTLSGGEQQMLAIARALMSRPK 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 162 IMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:cd03224 153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-221 |
5.88e-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: 178.78 E-value: 5.88e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNS----YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVE 78
Cdd:COG4181 6 APIIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlDEDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIR-RKVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAksEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALC 157
Cdd:COG4181 86 RLRaRHVGFVFQSFQLLPTLTALENVML-PLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFA 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQvADSIVFMAEGSIIE 221
Cdd:COG4181 163 TEPAILFADEPTGNLDAATGEQIIDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAGRLVE 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-241 |
1.69e-55 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 178.11 E-value: 1.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL-----EAHQTGHIVVDGIEL-TDDVKAVEkI 80
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIySPDVDPIE-V 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLTLApIWVRGMAKS--EIEEIAMMYLKRV----RIPDQAHKFPGQLSGGQQQRVAIAR 154
Cdd:PRK14267 84 RREVGMVFQYPNPFPHLTIYDNVAIG-VKLNGLVKSkkELDERVEWALKKAalwdEVKDRLNDYPSNLSGGQRQRLVIAR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 155 ALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEgMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKS 234
Cdd:PRK14267 163 ALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
|
....*..
gi 2504588632 235 ERTRQFL 241
Cdd:PRK14267 242 ELTEKYV 248
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-219 |
2.19e-55 |
|
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: 175.28 E-value: 2.19e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVkavEKIRRKVGM 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP---EEVKRRIGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLtlapiwvrgmakseieeiammylkrvripdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03230 78 LPEEPSLYENLTVRENL-------------------------------------KLSGGMKQRLALAQALLHDPELLILD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:cd03230 121 EPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-242 |
7.60e-55 |
|
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: 175.99 E-value: 7.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHaLRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkaVEKIRRKVGM 86
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN----LPPEKRDISY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03299 76 VPQNYALFPHMTVYKNIAYG-LKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 167 EPTSALDPEmVKEVLDVMTELAGE--GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLG 242
Cdd:cd03299 155 EPFSALDVR-TKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLG 231
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-199 |
1.08e-53 |
|
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: 172.21 E-value: 1.08e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRRKV 84
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlRGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFA-LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
|
170 180 190
....*....|....*....|....*....|....*
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTH 199
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-244 |
4.80e-53 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 175.79 E-value: 4.80e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkaVEKIRRKVG 85
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSH----VPPYQRPIN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTLAPIWVRgMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:PRK11607 95 MMFQSYALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 166 DEPTSALDPE----MVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK11607 174 DEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFI 250
|
...
gi 2504588632 242 GQI 244
Cdd:PRK11607 251 GSV 253
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
9-214 |
1.24e-52 |
|
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: 169.33 E-value: 1.24e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 9 LRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT--DDVKAVEKIRRKVGM 86
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPplNSKKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLAPIWVRGmAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGLKYKKL-SKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQvADSIVFM 214
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQ-ADRVIEL 206
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-223 |
1.82e-52 |
|
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: 168.97 E-value: 1.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkaVEKIRRKVGM 86
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTD----LPPKDRDIAM 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03301 77 VFQNYALYPHMTVYDNIAF-GLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 167 EPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03301 156 EPLSNLDAklrvQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-217 |
1.93e-52 |
|
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: 167.04 E-value: 1.93e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 8 ELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMV 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAK--LPLEELRRRIGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 88 FQnfnlfphltvlqnltlapiwvrgmakseieeiammylkrvripdqahkfpgqLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:cd00267 79 PQ----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2504588632 168 PTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-230 |
4.71e-52 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 170.20 E-value: 4.71e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENaIIELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVE 78
Cdd:PRK13635 1 MKEE-IIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSE--ETVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKVGMVFQN-FNLFPHLTV-------LQNltlapiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRV 150
Cdd:PRK13635 78 DVRRQVGMVFQNpDNQFVGATVqddvafgLEN--------IGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 151 AIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGM-TMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFF 229
Cdd:PRK13635 150 AIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIF 228
|
.
gi 2504588632 230 E 230
Cdd:PRK13635 229 K 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-241 |
1.40e-51 |
|
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: 175.26 E-value: 1.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL----EAHQTGHIVVDGIELTD-DVKAVEKIR-RKVGMVFQ---- 89
Cdd:COG4172 24 EAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGlSERELRRIRgNRIAMIFQepmt 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 90 --NfnlfPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHK---FPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:COG4172 104 slN----PLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYTRKLL 257
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
39-244 |
1.73e-51 |
|
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: 170.37 E-value: 1.73e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 39 GPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkaVEKIRRKVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEI 118
Cdd:TIGR01187 3 GPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTN----VPPHLRHINMVFQSYALFPHMTVEENVAF-GLKMRKVPRAEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 119 EEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALD----PEMVKEVLDVMTELageGMTM 194
Cdd:TIGR01187 78 KPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDkklrDQMQLELKTIQEQL---GITF 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2504588632 195 VCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLGQI 244
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEI 204
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-247 |
8.67e-51 |
|
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: 169.13 E-value: 8.67e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 24 DVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVK----AVEkiRRKVGMVFQNFNLFPHLTV 99
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARgiflPPH--RRRIGYVFQEARLFPHLSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLApIW--VRGMAKSEIEEIAMMY-----LKRvripdqahkFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:COG4148 95 RGNLLYG-RKraPRAERRISFDEVVELLgighlLDR---------RPATLSGGERQRVAIGRALLSSPRLLLMDEPLAAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 173 DPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQ-------FLGQI 244
Cdd:COG4148 165 DLARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGgeeagsvLEATV 244
|
...
gi 2504588632 245 LEH 247
Cdd:COG4148 245 AAH 247
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-217 |
1.23e-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: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNS--YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkAVEKIRRKV 84
Cdd:cd03228 1 IEFKNVSFSYPGrpKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDL--DLESLRKNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFpHLTVLQNLtlapiwvrgmakseieeiammylkrvripdqahkfpgqLSGGQQQRVAIARALCMRPEIML 164
Cdd:cd03228 79 AYVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGeGMTMVCVTHEMGFARQvADSIVFMAEG 217
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRD-ADRIIVLDDG 170
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
7-227 |
1.42e-50 |
|
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: 175.41 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVekiRRK 83
Cdd:COG2274 474 IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASL---RRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFpHLTVLQNLTLapiWVRGMAKSEIEEIAMMYlkrvripdQAHKF----P-----------GQLSGGQQQ 148
Cdd:COG2274 551 IGVVLQDVFLF-SGTIRENITL---GDPDATDEEIIEAARLA--------GLHDFiealPmgydtvvgeggSNLSGGQRQ 618
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 149 RVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGeGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAE 227
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTIRL-ADRIIVLDKGRIVEDGTHEE 695
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.71e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 165.93 E-value: 1.71e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 2 TENAIIELRKVGKWYNSYH--ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkAVEK 79
Cdd:PRK13632 3 NKSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKE--NLKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 80 IRRKVGMVFQN-FNLFPHLTV-------LQNLTLAPiwvrgmakSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVA 151
Cdd:PRK13632 81 IRKKIGIIFQNpDNQFIGATVeddiafgLENKKVPP--------KKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 152 IARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGM-TMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFE 230
Cdd:PRK13632 153 IASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILN 231
|
.
gi 2504588632 231 N 231
Cdd:PRK13632 232 N 232
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-236 |
6.14e-50 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 164.87 E-value: 6.14e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNS-YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIRRKV 84
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFN--LFPHlTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK13639 81 GIVFQNPDdqLFAP-TVEEDVAFGPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSER 236
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-170 |
1.25e-49 |
|
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: 159.74 E-value: 1.25e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKavEKIRRKVGMVFQNFNLFPHLTVLQ 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER--KSLRKEIGYVFQDPQLFPRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 102 NLTLAPIwVRGMAKSEIEEIAMMYLKRVRIPDQAH----KFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTS 170
Cdd:pfam00005 79 NLRLGLL-LKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
20-241 |
1.30e-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: 170.25 E-value: 1.30e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQtGHIVVDGIELTD-DVKAVEKIRRKVGMVFQN----FNlf 94
Cdd:COG4172 300 KAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGlSRRALRPLRRRMQVVFQDpfgsLS-- 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 95 PHLTVLQNLT-----LAPiwvrGMAKSEIEEIAMMYLKRVRI-PDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEP 168
Cdd:COG4172 377 PRMTVGQIIAeglrvHGP----GLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEP 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 169 TSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:COG4172 453 TSALDVSVQAQILDLLRDLQREhGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALL 526
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
20-233 |
1.74e-49 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 164.90 E-value: 1.74e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRRKVGMVFQN----FNlf 94
Cdd:COG4608 32 KAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGlSGRELRPLRRRMQMVFQDpyasLN-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 95 PHLTVLQNLTlAPIWVRGMA-KSEIEEIAMMYLKRVRI-PDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:COG4608 110 PRMTVGDIIA-EPLRIHGLAsKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 173 DPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPK 233
Cdd:COG4608 189 DVSIQAQVLNLLEDLQDElGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-243 |
3.11e-49 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 164.89 E-value: 3.11e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKi 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH--RSIQQ- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 rRKVGMVFQNFNLFPHLTVLQNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:PRK11432 78 -RDICMVFQSYALFPHMSLGENVGYG-LKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQ 239
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMAS 235
|
....
gi 2504588632 240 FLGQ 243
Cdd:PRK11432 236 FMGD 239
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
21-241 |
6.40e-49 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 165.59 E-value: 6.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT--DDVKAVEKIRRKVGMVFQNFNLFPHLT 98
Cdd:PRK10070 43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkiSDAELREVRRKKIAMVFQSFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVK 178
Cdd:PRK10070 123 VLDNTAFG-MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRT 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 179 EVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK10070 202 EMQDELVKLqAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFF 265
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-241 |
1.41e-48 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 160.46 E-value: 1.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL-----EAHQTGHIVVDGIELTDdvKAVEK 79
Cdd:PRK14247 2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFK--MDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 80 IRRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRGM-AKSEIEEIAMMYLKRVR----IPDQAHKFPGQLSGGQQQRVAIAR 154
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVkSKKELQERVRWALEKAQlwdeVKDRLDAPAGKLSGGQQQRLCIAR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 155 ALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEgMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKS 234
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRH 238
|
....*..
gi 2504588632 235 ERTRQFL 241
Cdd:PRK14247 239 ELTEKYV 245
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
21-241 |
1.54e-48 |
|
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: 168.02 E-value: 1.54e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkAVEKIRRKVGMVFQNfnlfPHL--- 97
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDL--DEDDLRRRIAVVPQR----PHLfdt 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNLTLApiwvRGMAkSEIEEIAMmyLKRVRIPDQAHKFPG-----------QLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:COG4987 424 TLRENLRLA----RPDA-TDEELWAA--LERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLALARALLRDAPILLLD 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEM-GFARqvADSIVFMAEGSIIESGSPAEFFENPksERTRQFL 241
Cdd:COG4987 497 EPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLaGLER--MDRILVLEDGRIVEQGTHEELLAQN--GRYRQLY 567
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
7-223 |
2.45e-48 |
|
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: 158.43 E-value: 2.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNsyHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltdDVKAVEKIRRKVGM 86
Cdd:cd03298 1 VRLDKIRFSYG--EQPMHFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGV----DVTAAPPADRPVSM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLApiWVRGMAKSEIEEIAM-MYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLG--LSPGLKLTAEDRQAIeVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-241 |
3.23e-48 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 159.56 E-value: 3.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTEnAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL-----EAHQTGHIVVDGIEL----T 71
Cdd:PRK14239 1 MTE-PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIysprT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 72 DDVKavekIRRKVGMVFQNFNLFPhLTVLQNLTLApIWVRGMA-KSEIEEIAMMYLKRVRI----PDQAHKFPGQLSGGQ 146
Cdd:PRK14239 80 DTVD----LRKEIGMVFQQPNPFP-MSIYENVVYG-LRLKGIKdKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 147 QQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPA 226
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLK-DDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232
|
250
....*....|....*
gi 2504588632 227 EFFENPKSERTRQFL 241
Cdd:PRK14239 233 QMFMNPKHKETEDYI 247
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-227 |
5.18e-48 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 166.49 E-value: 5.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkAVEKIRRKVGMVFQNFNLFpHLTVL 100
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDL--TLESLRRQIGVVPQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLAPIWVrgmAKSEIEEIAmmylKRVRIPDQAHKFPG-----------QLSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:COG1132 432 ENIRYGRPDA---TDEEVEEAA----KAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEAT 504
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 170 SALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAE 227
Cdd:COG1132 505 SALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEE 560
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-223 |
6.31e-48 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 156.44 E-value: 6.31e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 8 ELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELtDDVKAVEkIRRKVGMV 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDL-ASLSPKE-LARKIAYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 88 FQNfnlfphltvlqnltlapiwvrgmakseieeiammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:cd03214 79 PQA-----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDE 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 168 PTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03214 124 PTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ATP_DarD |
NF038007 |
darobactin export ABC transporter ATP-binding protein; |
21-219 |
4.16e-47 |
|
darobactin export ABC transporter ATP-binding protein;
Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 155.65 E-value: 4.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdVKAVEKI---RRKVGMVFQNFNLFPHL 97
Cdd:NF038007 20 VLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTN-LSYSQKIilrRELIGYIFQSFNLIPHL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMV 177
Cdd:NF038007 99 SIFDNVAL-PLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSKNA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2504588632 178 KEVLDVMTELAGEGMTMVCVTHEMGfARQVADSIVFMAEGSI 219
Cdd:NF038007 178 RAVLQQLKYINQKGTTIIMVTHSDE-ASTYGNRIINMKDGKL 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-242 |
1.13e-46 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 159.04 E-value: 1.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkaVEKIRRKV 84
Cdd:PRK11000 2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMND----VPPAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQN----LTLApiwvrGMAKSEIEeiammylKRV----RIPDQAH---KFPGQLSGGQQQRVAIA 153
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENmsfgLKLA-----GAKKEEIN-------QRVnqvaEVLQLAHlldRKPKALSGGQRQRVAIG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 154 RALCMRPEIMLFDEPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFF 229
Cdd:PRK11000 146 RTLVAEPSVFLLDEPLSNLDAalrvQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELY 222
|
250
....*....|...
gi 2504588632 230 ENPKSERTRQFLG 242
Cdd:PRK11000 223 HYPANRFVAGFIG 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-227 |
1.75e-46 |
|
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: 154.20 E-value: 1.75e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKwYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKaveKIRRKVG 85
Cdd:cd03263 3 IRNLTKTYK-KGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK---AARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTL-APIwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFyARL--KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELaGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:cd03263 157 LDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-231 |
1.91e-46 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 156.02 E-value: 1.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 17 NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIElTDDVKAVEKIRRKVGMVFQN-FNLFP 95
Cdd:PRK13633 21 TEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD-TSDEENLWDIRNKAGMVFQNpDNQIV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 96 HLTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPE 175
Cdd:PRK13633 100 ATIVEEDVAFGPENL-GIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPS 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 176 MVKEVLDVMTELAGE-GMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:PRK13633 179 GRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
31-223 |
2.93e-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: 153.22 E-value: 2.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 31 KGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKaveKI-----RRKVGMVFQNFNLFPHLTVLQNLTL 105
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRK---KInlppqQRKIGLVFQQYALFPHLNVRENLAF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 106 ApiwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMT 185
Cdd:cd03297 99 G---LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELK 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 2504588632 186 ELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03297 176 QIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
16-215 |
1.15e-45 |
|
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: 151.53 E-value: 1.15e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 16 YNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvKAVEKIRRKVGMVFQNFNL-- 93
Cdd:cd03235 9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFG-------KPLEKERKRIGYVPQRRSIdr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 -FPhLTVLQ----NLTLAPIWVRGMAKSEIEEIAMMyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEP 168
Cdd:cd03235 82 dFP-ISVRDvvlmGLYGHKGLFRRLSKADKAKVDEA-LERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2504588632 169 TSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMA 215
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN 206
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-241 |
1.22e-45 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 153.40 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 3 ENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLE-----AHQTGHIVVDGIELTD-DVKA 76
Cdd:PRK14243 7 TETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNLYApDVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 77 VEkIRRKVGMVFQNFNLFPHlTVLQNLTLAPiWVRGMaKSEIEEIAMMYLKRVRIPDQAH---KFPGQ-LSGGQQQRVAI 152
Cdd:PRK14243 87 VE-VRRRIGMVFQKPNPFPK-SIYDNIAYGA-RINGY-KGDMDELVERSLRQAALWDEVKdklKQSGLsLSGGQQQRLCI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 153 ARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELaGEGMTMVCVTHEMGFARQVADSIVFMA---------EGSIIESG 223
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHEL-KEQYTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFD 241
|
250
....*....|....*...
gi 2504588632 224 SPAEFFENPKSERTRQFL 241
Cdd:PRK14243 242 RTEKIFNSPQQQATRDYV 259
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
7-232 |
1.22e-45 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 154.02 E-value: 1.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYN-----SYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKA--VEK 79
Cdd:PRK13634 3 ITFQKVEHRYQyktpfERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkkLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 80 IRRKVGMVFQnfnlFPHL-----TVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIP-DQAHKFPGQLSGGQQQRVAIA 153
Cdd:PRK13634 83 LRKKVGIVFQ----FPEHqlfeeTVEKDICFGPMNF-GVSEEDAKQKAREMIELVGLPeELLARSPFELSGGQMRRVAIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 154 RALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:PRK13634 158 GVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-227 |
1.98e-45 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 151.66 E-value: 1.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 26 SLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAvekiRRKVGMVFQNFNLFPHLTVLQN--L 103
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS----RRPVSMLFQENNLFSHLTVAQNigL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 104 TLAP-IWVRGMAKSEIEEIAmmylKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLD 182
Cdd:PRK10771 95 GLNPgLKLNAAQREKLHAIA----RQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2504588632 183 VMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:PRK10771 171 LVSQVCQErQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
7-231 |
2.11e-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: 2.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVG-KWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkAVEKIRRKVG 85
Cdd:COG4988 337 IELEDVSfSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDL--DPASWRRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFpHLTVLQNLTLApiwvRGMA-KSEIEEIammyLKRVRIPDQAHKFPG-----------QLSGGQQQRVAIA 153
Cdd:COG4988 415 WVPQNPYLF-AGTIRENLRLG----RPDAsDEELEAA----LEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 154 RALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-231 |
5.42e-45 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 152.12 E-value: 5.42e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIRRKVGMVFQ--NFNLFPHlT 98
Cdd:PRK13637 22 ALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDIRKKVGLVFQypEYQLFEE-T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLAPIwVRGMAKSEIEE--IAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEM 176
Cdd:PRK13637 101 IEKDIAFGPI-NLGLSEEEIENrvKRAMNIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 177 VKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:PRK13637 180 RDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-223 |
1.03e-44 |
|
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: 149.27 E-value: 1.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVcGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltDDVKAVEKIRRKVGM 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQ---DVLKQPQKLRRRIGY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNL-TLApiWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:cd03264 77 LPQEFGVYPNFTVREFLdYIA--WLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELaGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSEL-GEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-244 |
1.30e-44 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 150.58 E-value: 1.30e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG--IELTDDVKAVE--KIRRKVGMVFQNFNLFPHL 97
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvLYFGKDIFQIDaiKLRKEVGMVFQQPNPFPHL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNLTLaPIWVRGMA-KSEIEEIAMMYLKRV----RIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:PRK14246 106 SIYDNIAY-PLKSHGIKeKREIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 173 DPEMVKEVLDVMTELAGEgMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQF-LGQI 244
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYvIGRI 256
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-233 |
4.85e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 150.24 E-value: 4.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNS-----YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHI-------------VVDGI 68
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdeknkkktKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 69 ELTDDV---------KAVEKIRRKVGMVFQ--NFNLFPHlTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQ-AH 136
Cdd:PRK13651 83 VLEKLViqktrfkkiKKIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLDESyLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 137 KFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAE 216
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|....*..
gi 2504588632 217 GSIIESGSPAEFFENPK 233
Cdd:PRK13651 241 GKIIKDGDTYDILSDNK 257
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-225 |
5.43e-44 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 149.50 E-value: 5.43e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTddvKAVEK-IR 81
Cdd:PRK13647 2 DNIIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVN---AENEKwVR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RKVGMVFQNFN--LFPhLTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMR 159
Cdd:PRK13647 79 SKVGLVFQDPDdqVFS-STVWDDVAFGPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 160 PEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSP 225
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK 222
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-228 |
6.54e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.41 E-value: 6.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 3 ENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG--IELTDDVKAvekI 80
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDA---Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRG--MAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCM 158
Cdd:COG1129 78 AAGIAIIHQELNLVPNLSVAENIFLGREPRRGglIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 159 RPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:COG1129 158 DARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
14-227 |
9.25e-44 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 149.46 E-value: 9.25e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 14 KWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltDDVKAVEKIRRKVGMVFQNFNL 93
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGY---DVVREPRKVRRSIGIVPQYASV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 FPHLTVLQNLTL-APIWvrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:TIGR01188 78 DEDLTGRENLEMmGRLY--GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 173 DPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEE 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
8-241 |
2.54e-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: 146.13 E-value: 2.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 8 ELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvKAVEKIRRKVGMV 87
Cdd:TIGR03410 2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKL-PPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 88 FQNFNLFPHLTVLQNLTLApIWVRGMAKSEI-EEIAMMY--LKRVRipdqaHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTG-LAALPRRSRKIpDEIYELFpvLKEML-----GRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFEnpksERTRQFL 241
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDE----DKVRRYL 228
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-230 |
2.62e-43 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 147.58 E-value: 2.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDV--KAVEKIRRKVGMVFQnfnlFPHL- 97
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSknKDIKQIRKKVGLVFQ----FPESq 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 ----TVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQA-HKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:PRK13649 98 lfeeTVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 173 DPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFE 230
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQ 234
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-247 |
2.77e-43 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 149.49 E-value: 2.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 24 DVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKI--RRKVGMVFQNFNLFPHLTVLQ 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPpeKRRIGYVFQEARLFPHLSVRG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLtlapiwVRGMAKSEIEEIAMMYLKRVRIPDQAH---KFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVK 178
Cdd:TIGR02142 95 NL------RYGMKRARPSERRISFERVIELLGIGHllgRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 179 EVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENP------KSERTRQFLGQILEH 247
Cdd:TIGR02142 169 EILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPdlpwlaREDQGSLIEGVVAEH 244
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-225 |
2.88e-43 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 146.93 E-value: 2.88e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSY----HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvKAVEKI 80
Cdd:COG4525 2 SMLTVRHVSVRYPGGgqpqPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG-------VPVTGP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:COG4525 75 GADRGVVFQKDALLPWLNVLDNVAF-GLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 161 EIMLFDEPTSALDP---EMVKE-VLDVMTElagEGMTMVCVTHEMgfarqvaDSIVFMAEGSIIESGSP 225
Cdd:COG4525 154 RFLLMDEPFGALDAltrEQMQElLLDVWQR---TGKGVFLITHSV-------EEALFLATRLVVMSPGP 212
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
16-219 |
6.27e-43 |
|
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: 144.62 E-value: 6.27e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 16 YNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltdDVKAVEKIRRKVGMVFQNFNLFP 95
Cdd:TIGR01277 8 YEYEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQ----SHTGLAPYQRPVSMLFQENNLFA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 96 HLTVLQNLTLA---PIWVRGMAKSEIEEIAmmylKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:TIGR01277 84 HLTVRQNIGLGlhpGLKLNAEQQEKVVDAA----QQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2504588632 173 DPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:TIGR01277 160 DPLLREEMLALVKQLCSErQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-228 |
1.08e-42 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 145.54 E-value: 1.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL-------EAHQT--GHIVVDGIELTDDVKa 76
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgdksaGSHIEllGRTVQREGRLARDIR- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 77 veKIRRKVGMVFQNFNLFPHLTVLQNLTLA-----PIW---VRGMAKSEIEEiAMMYLKRVRIPDQAHKFPGQLSGGQQQ 148
Cdd:PRK09984 83 --KSRANTGYIFQQFNLVNRLSVLENVLIGalgstPFWrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 149 RVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:PRK09984 160 RVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
.
gi 2504588632 228 F 228
Cdd:PRK09984 240 F 240
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
21-204 |
1.24e-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: 143.33 E-value: 1.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIRRKVGMVFQNFN--LFpHLT 98
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLLERRQRVGLVFQDPDdqLF-AAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVK 178
Cdd:TIGR01166 86 VDQDVAFGPLNL-GLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAGRE 164
|
170 180
....*....|....*....|....*.
gi 2504588632 179 EVLDVMTELAGEGMTMVCVTHEMGFA 204
Cdd:TIGR01166 165 QMLAILRRLRAEGMTVVISTHDVDLA 190
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
5-234 |
1.29e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 148.07 E-value: 1.29e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVEKIRRK 83
Cdd:PRK11650 2 AGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG----RVVNELEPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNLTLApIWVRGMAKSEIE----EIAMM-----YLKRvripdqahKfPGQLSGGQQQRVAIAR 154
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYG-LKIRGMPKAEIEervaEAARIlelepLLDR--------K-PRELSGGQRQRVAMGR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 155 ALCMRPEIMLFDEPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFE 230
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLDAklrvQMRLEIQRLHRRL---KTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYE 224
|
....
gi 2504588632 231 NPKS 234
Cdd:PRK11650 225 KPAS 228
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-233 |
6.78e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 144.20 E-value: 6.78e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDV--KAVEKIRRKVGMVFQnfnlFPHL-- 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETgnKNLKKLRKKVSLVFQ----FPEAql 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 ---TVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQ-AHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALD 173
Cdd:PRK13641 99 fenTVLKDVEFGPKNF-GFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 174 PEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPK 233
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
5-229 |
7.20e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 144.10 E-value: 7.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNS---YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkAVEKIR 81
Cdd:PRK13650 3 NIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEE--NVWDIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RKVGMVFQN-FNLFPHLTV-------LQNltlapiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIA 153
Cdd:PRK13650 81 HKIGMVFQNpDNQFVGATVeddvafgLEN--------KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 154 RALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGfarQVA--DSIVFMAEGSIIESGSPAEFF 229
Cdd:PRK13650 153 GAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLD---EVAlsDRVLVMKNGQVESTSTPRELF 228
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-227 |
7.64e-42 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 144.48 E-value: 7.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVkavekiRRKVG 85
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED------RRRIG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLT-LAPIwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:COG4152 75 YLPEERGLYPKMKVGEQLVyLARL--KGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG4152 153 LDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-232 |
9.37e-42 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 143.79 E-value: 9.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL---EAHQTGHIVVDGIELTDdvKAVE 78
Cdd:PRK13640 3 DNIVEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLllpDDNPNSKITVDGITLTA--KTVW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKVGMVFQN-FNLFPHLTV-------LQNltlapiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRV 150
Cdd:PRK13640 81 DIREKVGIVFQNpDNQFVGATVgddvafgLEN--------RAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 151 AIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFF 229
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEANM-ADQVLVLDDGKLLAQGSPVEIF 231
|
...
gi 2504588632 230 ENP 232
Cdd:PRK13640 232 SKV 234
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-227 |
1.92e-41 |
|
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: 141.60 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVgkwYNSYH----ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltdDVKAV--EKI 80
Cdd:cd03253 1 IEFENV---TFAYDpgrpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQ----DIREVtlDSL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFpHLTVLQNLTLAPIwvrGMAKSEIEEIAmmylKRVRIPDQAHKFPGQ-----------LSGGQQQR 149
Cdd:cd03253 74 RRAIGVVPQDTVLF-NDTIGYNIRYGRP---DATDEEVIEAA----KAAQIHDKIMRFPDGydtivgerglkLSGGEKQR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 150 VAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEMgfaRQV--ADSIVFMAEGSIIESGSPAE 227
Cdd:cd03253 146 VAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRL---STIvnADKIIVLKDGRIVERGTHEE 221
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-200 |
5.62e-41 |
|
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: 139.54 E-value: 5.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVkavEKIRRKV 84
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAR---EDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTL-APIWVRGMAKSEIEEIammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFwAALYGLRADREAIDEA----LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHE 200
Cdd:COG4133 154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-232 |
1.20e-40 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 141.91 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 17 NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDD--------------VKAVEKIRR 82
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKknnhelitnpyskkIKNFKELRR 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQ--NFNLFPHlTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQ-AHKFPGQLSGGQQQRVAIARALCMR 159
Cdd:PRK13631 117 RVSMVFQfpEYQLFKD-TIEKDIMFGPVAL-GVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQ 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 160 PEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:PRK13631 195 PEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-223 |
1.20e-40 |
|
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: 138.50 E-value: 1.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekirRKVGM 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----RRIGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNL-TLAPIwvRGMAKSEIEEIammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:cd03268 77 LIEAPGFYPNLTARENLrLLARL--LGIRKKRIDEV----LDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLIL 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03268 151 DEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-227 |
2.22e-40 |
|
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: 138.90 E-value: 2.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltdDVKAVE--KIRRKVGMVFQNFNLFpHLT 98
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGH----DVRDYTlaSLRRQIGLVSQDVFLF-NDT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLApiwVRGMAKSEIEEIA-MMYLKRV--RIPDQAHKFPGQ----LSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:cd03251 92 VAENIAYG---RPGATREEVEEAArAANAHEFimELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 172 LDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAE 227
Cdd:cd03251 169 LDTESERLVQAALERLM-KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEE 222
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-227 |
2.26e-40 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 146.79 E-value: 2.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNS----YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVE 78
Cdd:PRK10535 2 TALLELKDIRRSYPSgeeqVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATlDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRK-VGMVFQNFNLFPHLTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALC 157
Cdd:PRK10535 82 QLRREhFGFIFQRYHLLSHLTAAQNVEVPAVYA-GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQvADSIVFMAEGSIIeSGSPAE 227
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV-RNPPAQ 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-227 |
3.69e-40 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 144.40 E-value: 3.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG--IELTDDVKAvekIRRK 83
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDA---IALG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNLTLA----PIWVRGMAK--SEIEEIAMMYlkRVRIPDQAHkfPGQLSGGQQQRVAIARALC 157
Cdd:COG3845 82 IGMVHQHFMLVPNLTVAENIVLGleptKGGRLDRKAarARIRELSERY--GLDVDPDAK--VEDLSVGEQQRVEILKALY 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG3845 158 RGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
22-217 |
4.97e-40 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 137.98 E-value: 4.97e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkavEKIRRKVgmVFQNFNLFPHLTVLQ 101
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-----PGPDRMV--VFQNYSLLPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTLAPIWV-RGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEV 180
Cdd:TIGR01184 74 NIALAVDRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2504588632 181 LDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:TIGR01184 154 QEELMQIWEEhRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-223 |
7.38e-40 |
|
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: 136.64 E-value: 7.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkavekIRRKVGM 86
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA------ARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLT-LAPIwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLAQL--KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03269 153 DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
18-241 |
1.35e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 137.66 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 18 SYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT--DDVKAVEKIRrkvgMVFQNFN--L 93
Cdd:COG4167 25 QFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEygDYKYRCKHIR----MIFQDPNtsL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 FPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRI-PDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:COG4167 101 NPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARALILQPKIIIADEALAAL 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 173 DPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:COG4167 181 DMSVRSQIINLMLELQEKlGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHEVTKRLI 250
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-220 |
2.09e-39 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 135.46 E-value: 2.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVEKiRRKVGMVFQN--FNLFPHlTV 99
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG----KPIKAKER-RKSIGYVMQDvdYQLFTD-SV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLapiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKE 179
Cdd:cd03226 90 REELLL-----GLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMER 164
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2504588632 180 VLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSII 220
Cdd:cd03226 165 VGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-218 |
2.10e-39 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 136.02 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNSYH-------ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVD-GIELTDDVK 75
Cdd:COG4778 2 TTLLEVENLSKTFTLHLqggkrlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 76 AVEK----IRRK-VGMVFQNFNLFPHLTVLQnLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQ-AHKFPGQLSGGQQQR 149
Cdd:COG4778 82 ASPReilaLRRRtIGYVSQFLRVIPRVSALD-VVAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 150 VAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGS 218
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-242 |
2.20e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 138.94 E-value: 2.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEK-IRRKVGMVFQN--FNLFPH 96
Cdd:PRK11308 29 KALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKlLRQKIQIVFQNpyGSLNPR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 LTVLQNLTlAPIWVR-GMAKSEIEE--IAMMylKRVRI-PDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:PRK11308 109 KKVGQILE-EPLLINtSLSAAERREkaLAMM--AKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 173 DPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLG 242
Cdd:PRK11308 186 DVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLS 256
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
6-242 |
5.19e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 136.66 E-value: 5.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIElTDDVKAVEKIRRKV 84
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGID-TGDFSKLQGIRKLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNL-FPHLTVLQ-------NLTLAPIWVRGMAKSEIEEIAmmyLKRVRipdqaHKFPGQLSGGQQQRVAIARAL 156
Cdd:PRK13644 80 GIVFQNPETqFVGRTVEEdlafgpeNLCLPPIEIRKRVDRALAEIG---LEKYR-----HRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 157 CMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGfARQVADSIVFMAEGSIIESGSPaeffENPKSER 236
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLEGEP----ENVLSDV 226
|
....*.
gi 2504588632 237 TRQFLG 242
Cdd:PRK13644 227 SLQTLG 232
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-227 |
5.21e-39 |
|
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: 134.80 E-value: 5.21e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltDDVKAVEKIRRKVGM 86
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGH---DVVREPREVRRRIGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTL-APIWvrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:cd03265 78 VFQDLSVDDELTGWENLYIhARLY--GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:cd03265 156 DEPTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-231 |
9.18e-39 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 136.29 E-value: 9.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 19 YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIEL---TDDVKAVEKIRRKVGMVFQ--NFNL 93
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanLKKIKEVKRLRKEIGLVFQfpEYQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 FPHlTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIP-DQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:PRK13645 104 FQE-TIEKDIAFGPVNL-GENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 173 DPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
22-199 |
1.87e-38 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 132.99 E-value: 1.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCIN-RLEAHQT--GHIVVDGIELTDdvKAVEkiRRKVGMVFQNFNLFPHLT 98
Cdd:COG4136 17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAFSasGEVLLNGRRLTA--LPAE--QRRIGILFQDDLLFPHLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLA-PiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMV 177
Cdd:COG4136 93 VGENLAFAlP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169
|
170 180
....*....|....*....|...
gi 2504588632 178 KEVLD-VMTELAGEGMTMVCVTH 199
Cdd:COG4136 170 AQFREfVFEQIRQRGIPALLVTH 192
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-230 |
2.01e-38 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 133.50 E-value: 2.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYH-ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltdDVKAVEKI--RRK 83
Cdd:cd03254 3 IEFENVNFSYDEKKpVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGI----DIRDISRKslRSM 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHlTVLQNLTLApiwvRGMAKSEIEEIAmmyLKRVRIPDQAHKFP-----------GQLSGGQQQRVAI 152
Cdd:cd03254 79 IGVVLQDTFLFSG-TIMENIRLG----RPNATDEEVIEA---AKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAI 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 153 ARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFE 230
Cdd:cd03254 151 ARAMLRDPKILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-241 |
2.21e-38 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 134.39 E-value: 2.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL-----EAHQTGHIVVDGIELTDDVKAVEKIR 81
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RKVGMVFQNFNLFPhLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQA----HKFPGQLSGGQQQRVAIARALC 157
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIkhkiHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 158 MRPEIMLFDEPTSALDP--EMVKEVLDVMTELAGEgMTMVCVTHEMGFARQVADSIVFMAE-----GSIIESGSPAEFFE 230
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPiaSMKVESLIQSLRLRSE-LTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTKKIFN 245
|
250
....*....|.
gi 2504588632 231 NPKSERTRQFL 241
Cdd:PRK14258 246 SPHDSRTREYV 256
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-220 |
2.95e-38 |
|
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: 131.01 E-value: 2.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT-DDVKavEKIRRKVG 85
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPR--DARRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQnfnlfphltvlqnltlapiwvrgmakseieeiammylkrvripdqahkfpgqLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:cd03216 79 MVYQ----------------------------------------------------LSVGERQMVEIARALARNARLLIL 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSII 220
Cdd:cd03216 107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
6-232 |
6.01e-38 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 133.77 E-value: 6.01e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYN-SYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKV 84
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK--ENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFN--LFPHlTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK13652 81 GLVFQNPDdqIFSP-TVEQDIAFGPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-227 |
6.27e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 132.93 E-value: 6.27e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELtDDVKAVEKIRRKvGMVFQNFNL-FPhLTVL 100
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL-AAWSPWELARRR-AVLPQHSSLaFP-FTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 Q--NLTLAPiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALC-------MRPEIMLFDEPTSA 171
Cdd:COG4559 94 EvvALGRAP---HGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLFLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 172 LDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG4559 171 LDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEE 226
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-223 |
1.26e-37 |
|
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: 131.34 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltDDVKAVEKIRRKVGMVFQNFNLFPHLTV 99
Cdd:cd03266 19 QAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGF---DVVKEPAEARRRLGFVSDSTGLYDRLTA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLT-------LApiwvRGMAKSEIEEIAmmylKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:cd03266 96 RENLEyfaglygLK----GDELTARLEELA----DRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 173 DPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03266 168 DVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-246 |
1.39e-37 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 133.05 E-value: 1.39e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 3 ENAIIELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIR 81
Cdd:PRK13636 2 EDYILKVEELNYNYsDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RKVGMVFQ--NFNLFPhLTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMR 159
Cdd:PRK13636 82 ESVGMVFQdpDNQLFS-ASVYQDVSFGAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 160 PEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTR 238
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLRKV 239
|
250
....*....|..
gi 2504588632 239 QF----LGQILE 246
Cdd:PRK13636 240 NLrlprIGHLME 251
|
|
| NHLM_micro_ABC2 |
TIGR03797 |
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ... |
7-227 |
6.13e-37 |
|
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: 137.40 E-value: 6.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVekiRRK 83
Cdd:TIGR03797 452 IEVDRVTFRYrpDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGlDVQAV---RRQ 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHlTVLQNLTlapiwvrGMAKSEIEEiAMMYLKRVRIPDQAHKFP-----------GQLSGGQQQRVAI 152
Cdd:TIGR03797 529 LGVVLQNGRLMSG-SIFENIA-------GGAPLTLDE-AWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQRLLI 599
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 153 ARALCMRPEIMLFDEPTSALDPEMvKEVldVMTELAGEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAE 227
Cdd:TIGR03797 600 ARALVRKPRILLFDEATSALDNRT-QAI--VSESLERLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-229 |
1.23e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 130.67 E-value: 1.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 19 YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVK--AVEKIRRKVGMVFQnfnlFPH 96
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkYIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 L-----TVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIP-DQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTS 170
Cdd:PRK13646 96 SqlfedTVEREIIFGPKNF-KMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 171 ALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFF 229
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
22-231 |
2.04e-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: 128.43 E-value: 2.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVK--AVEKIRRKVGMVFQNFNLFPhLTV 99
Cdd:cd03249 19 LKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDG----VDIRdlNLRWLRSQIGLVSQEPVLFD-GTI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLApiwVRGMAKSEIEEIAMMYLkrvripdqAHKF----P-----------GQLSGGQQQRVAIARALCMRPEIML 164
Cdd:cd03249 94 AENIRYG---KPDATDEEVEEAAKKAN--------IHDFimslPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 165 FDEPTSALDPE---MVKEVLDvmteLAGEGMTMVCVTHEMGfARQVADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:cd03249 163 LDEATSALDAEsekLVQEALD----RAMKGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
21-227 |
2.42e-36 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 128.37 E-value: 2.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTddVKAVEKIRRKVGMVFQNFNLFpHLTVL 100
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA--LADPAWLRRQVGVVLQENVLF-NRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLAPiwvRGMAKSEIEEIAMMYlkrvripdQAHKFPGQ---------------LSGGQQQRVAIARALCMRPEIMLF 165
Cdd:cd03252 94 DNIALAD---PGMSMERVIEAAKLA--------GAHDFISElpegydtivgeqgagLSGGQRQRIAIARALIHNPRILIF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAE 227
Cdd:cd03252 163 DEATSALDYESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDE 222
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
6-230 |
3.52e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 129.47 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYN-----SYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKA--VE 78
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQkeIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKVGMVFQ--NFNLFPHlTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQA-HKFPGQLSGGQQQRVAIARA 155
Cdd:PRK13643 81 PVRKKVGVVFQfpESQLFEE-TVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 156 LCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFE 230
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQ 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
22-227 |
1.60e-35 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 126.81 E-value: 1.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQtGHIVVDGIELTDdVKAVEKIRRKvGMVFQNFNL-FPhLTV 99
Cdd:PRK13548 18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGELSPDS-GEVRLNGRPLAD-WSPAELARRR-AVLPQHSSLsFP-FTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQ--NLTLAPiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALC------MRPEIMLFDEPTSA 171
Cdd:PRK13548 94 EEvvAMGRAP---HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 172 LDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:PRK13548 171 LDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-234 |
1.65e-35 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 127.17 E-value: 1.65e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNS--YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKavE 78
Cdd:PRK13648 2 EDKNSIIVFKNVSFQYQSdaSFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF--E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKVGMVFQN-FNLFPHLTV-------LQNltlapiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRV 150
Cdd:PRK13648 80 KLRKHIGIVFQNpDNQFVGSIVkydvafgLEN--------HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 151 AIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFF 229
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEhNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230
|
....*
gi 2504588632 230 ENPKS 234
Cdd:PRK13648 231 DHAEE 235
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
6-230 |
2.86e-35 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 126.35 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvKAVEKIRRKVG 85
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-------KPVEGPGAERG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:PRK11248 74 VVFQNEGLLPWRNVQDNVAFG-LQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 166 DEPTSALDP---EMVKEVLdvMTELAGEGMTMVCVTHEMGFArqvadsiVFMAEGSIIESGSPAEFFE 230
Cdd:PRK11248 153 DEPFGALDAftrEQMQTLL--LKLWQETGKQVLLITHDIEEA-------VFMATELVLLSPGPGRVVE 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
22-223 |
4.82e-35 |
|
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: 123.82 E-value: 4.82e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCIN--RLEAHQTGHIVVDGIELTDDvkaveKIRRKVGMVFQNFNLFPHLTV 99
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDKR-----SFRKIIGYVPQDDILHPTLTV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLtlapiwvrgmakseieeiamMYLKRVRipdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKE 179
Cdd:cd03213 100 RETL--------------------MFAAKLR----------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQ 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2504588632 180 VLDVMTELAGEGMTMVCVTH----EMgFarQVADSIVFMAEGSIIESG 223
Cdd:cd03213 150 VMSLLRRLADTGRTIICSIHqpssEI-F--ELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-223 |
8.09e-35 |
|
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: 123.85 E-value: 8.09e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNS--YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekIRRKV 84
Cdd:cd03245 3 IEFRNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD--LRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFpHLTVLQNLTLApiwvRGMAKSE-IEEIAMMYLKRVRIPDQAHKFPGQ-------LSGGQQQRVAIARAL 156
Cdd:cd03245 81 GYVPQDVTLF-YGTLRDNITLG----APLADDErILRAAELAGVTDFVNKHPNGLDLQigergrgLSGGQRQAVALARAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 157 CMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGeGMTMVCVTHEMGFArQVADSIVFMAEGSIIESG 223
Cdd:cd03245 156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLLG-DKTLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-227 |
1.65e-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: 1.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRlEAHQT--GHIVVDGIEL--TDdvkaVEK 79
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLPPTygNDVRLFGERRggED----VWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 80 IRRKVGMV----FQNFNlfPHLTVLQ--------NLTLapiWVRgmAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQ 147
Cdd:COG1119 76 LRKRIGLVspalQLRFP--RDETVLDvvlsgffdSIGL---YRE--PTDEQRERARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 148 QRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEG-MTMVCVTH---EM--GFARqvadsIVFMAEGSIIE 221
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHhveEIppGITH-----VLLLKDGRVVA 223
|
....*.
gi 2504588632 222 SGSPAE 227
Cdd:COG1119 224 AGPKEE 229
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-207 |
2.32e-34 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 123.39 E-value: 2.32e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIR-RKVGMVFQNFNLFPHLTV 99
Cdd:PRK11629 25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKlSSAAKAELRnQKLGFIYQFHHLLPDFTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKE 179
Cdd:PRK11629 105 LENVAM-PLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|....*....
gi 2504588632 180 VLDVMTEL-AGEGMTMVCVTHEMGFARQV 207
Cdd:PRK11629 184 IFQLLGELnRLQGTAFLVVTHDLQLAKRM 212
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-242 |
2.46e-34 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 124.44 E-value: 2.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHI----VVDGIELTDDVKAVEKIRRKVGMVFQNFNLFPhL 97
Cdd:PRK14271 37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRysgdVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFP-M 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNL-------TLAP-IWVRGMAKSEIEEIAMMYLKRVRIPDQahkfPGQLSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:PRK14271 116 SIMDNVlagvrahKLVPrKEFRGVAQARLTEVGLWDAVKDRLSDS----PFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 170 SALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLG 242
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLA-DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVA 263
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
6-217 |
2.55e-34 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 122.68 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRRK 83
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRlKNREVPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAI-PLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:PRK10908 160 LADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-247 |
2.92e-34 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 125.76 E-value: 2.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 39 GPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAV----EKirRKVGMVFQNFNLFPHLTVLQNLTLapiwvrGMA 114
Cdd:PRK11144 31 GRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGIclppEK--RRIGYVFQDARLFPHYKVRGNLRY------GMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 115 KSEIEEiammYLKRVRIPDQAH---KFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE- 190
Cdd:PRK11144 103 KSMVAQ----FDKIVALLGIEPlldRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREi 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 191 GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFEN-------PKSERTRQFLGQILEH 247
Cdd:PRK11144 179 NIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASsamrpwlPKEEQSSILKVTVLEH 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
9-219 |
8.15e-34 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 122.48 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 9 LRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkAVEKIRrkvgMVF 88
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE---AREDTR----LMF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 89 QNFNLFPHLTVLQNLTLApiwVRGMAKSEieeiAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEP 168
Cdd:PRK11247 88 QDARLLPWKKVIDNVGLG---LKGQWRDA----ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 169 TSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
7-230 |
2.83e-33 |
|
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: 126.37 E-value: 2.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKV 84
Cdd:TIGR02203 331 VEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLAD--YTLASLRRQV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHlTVLQNLTLAPIwvRGMAKSEIEE-IAMMYLKRV--RIPDQAHKFPGQ----LSGGQQQRVAIARALC 157
Cdd:TIGR02203 409 ALVSQDVVLFND-TIANNIAYGRT--EQADRAEIERaLAAAYAQDFvdKLPLGLDTPIGEngvlLSGGQRQRLAIARALL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGfARQVADSIVFMAEGSIIESGSPAEFFE 230
Cdd:TIGR02203 486 KDAPILILDEATSALDNESERLVQAALERLM-QGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| type_I_sec_HlyB |
TIGR01846 |
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ... |
22-227 |
3.32e-33 |
|
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 126.78 E-value: 3.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIEL--TDDVKavekIRRKVGMVFQNFNLFPHlTV 99
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLaiADPAW----LRRQMGVVLQENVLFSR-SI 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLA-PiwvrGMAKSEIEEIAMMYLKRVRIPDQAHKFP-------GQLSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:TIGR01846 548 RDNIALCnP----GAPFEHVIHAAKLAGAHDFISELPQGYNtevgekgANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 172 LDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAE 227
Cdd:TIGR01846 624 LDYESEALIMRNMREIC-RGRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEE 677
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
7-230 |
4.06e-33 |
|
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: 126.52 E-value: 4.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT--DdvkaVEKIRR 82
Cdd:TIGR03375 464 IEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiD----PADLRR 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQNFNLFpHLTVLQNLTLApiwVRGMAKSEIEEIA-----------------MMYLKRVRipdqahkfpgQLSGG 145
Cdd:TIGR03375 540 NIGYVPQDPRLF-YGTLRDNIALG---APYADDEEILRAAelagvtefvrrhpdgldMQIGERGR----------SLSGG 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 146 QQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQVaDSIVFMAEGSIIESGSP 225
Cdd:TIGR03375 606 QRQAVALARALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLV-DRIIVMDNGRIVADGPK 683
|
....*
gi 2504588632 226 AEFFE 230
Cdd:TIGR03375 684 DQVLE 688
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-229 |
7.02e-33 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 120.58 E-value: 7.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTddVKAVEKIRRKVGMVFQN-FNLFPHLTVL 100
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT--AENVWNLRRKIGMVFQNpDNQFVGATVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLApIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEV 180
Cdd:PRK13642 101 DDVAFG-MENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2504588632 181 LDVMTELAGE-GMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFF 229
Cdd:PRK13642 180 MRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-244 |
7.44e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 120.25 E-value: 7.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVEK- 79
Cdd:PRK11831 2 QSVANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDG----ENIPAMSRs 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 80 ----IRRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARA 155
Cdd:PRK11831 78 rlytVRKRMSMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 156 LCMRPEIMLFDEPTSALDPEMVKEVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPkS 234
Cdd:PRK11831 158 IALEPDLIMFDEPFVGQDPITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP-D 236
|
250
....*....|
gi 2504588632 235 ERTRQFLGQI 244
Cdd:PRK11831 237 PRVRQFLDGI 246
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-219 |
1.16e-32 |
|
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: 116.93 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMVFQNFNLFPHlTVLQ 101
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ--WDPNELGDHVGYLPQDDELFSG-SIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLtlapiwvrgmakseieeiammylkrvripdqahkfpgqLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVL 181
Cdd:cd03246 95 NI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 2504588632 182 DVMTELAGEGMTMVCVTHEMGFARQvADSIVFMAEGSI 219
Cdd:cd03246 137 QAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-204 |
1.20e-32 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 118.73 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIEL----RKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVK 75
Cdd:PRK10584 1 MPAENIVEVhhlkKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 76 AVEKIR-RKVGMVFQNFNLFPHLTVLQNLTLaPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIAR 154
Cdd:PRK10584 81 ARAKLRaKHVGFVFQSFMLIPTLNALENVEL-PALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 155 ALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFA 204
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLA 210
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-238 |
1.61e-32 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 120.97 E-value: 1.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAVEKIRRKVGMVFQN--FNLFPHL 97
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmKDDEWRAVRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNL-----TLAPiwvrGMAKSEIEE--IAMMyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTS 170
Cdd:PRK15079 116 TIGEIIaeplrTYHP----KLSRQEVKDrvKAMM-LKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 171 ALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTR 238
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTK 259
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-223 |
1.89e-32 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 118.88 E-value: 1.89e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG--IELTDDVKAVE 78
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKV-----GMVFQNfnlfPhltvLQNLTL-----APIWVRGMAKSE-----IEEIAMMYLKRVRI-PDQAHKFPGQL 142
Cdd:PRK11701 81 AERRRLlrtewGFVHQH----P----RDGLRMqvsagGNIGERLMAVGArhygdIRATAGDWLERVEIdAARIDDLPTTF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 143 SGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIE 221
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRVVE 232
|
..
gi 2504588632 222 SG 223
Cdd:PRK11701 233 SG 234
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
10-223 |
3.39e-32 |
|
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: 117.37 E-value: 3.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 10 RKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQT--GHIVVDGIELTDDvkaveKIRRKVGM 86
Cdd:cd03234 11 LKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGGTtsGQILFNGQPRKPD-----QFQKCVAY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLAPIWV--RGMAKSEIEEI-AMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:cd03234 86 VRQDDILLPGLTVRETLTYTAILRlpRKSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMG---FarQVADSIVFMAEGSIIESG 223
Cdd:cd03234 166 ILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRsdlF--RLFDRILLLSSGEIVYSG 226
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
24-241 |
4.27e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.89 E-value: 4.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 24 DVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL-----EAHQTGHIVVDGIELTD-DVKAVEKIR-RKVGMVFQN--FNLF 94
Cdd:PRK15134 27 DVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHaSEQTLRGVRgNKIAMIFQEpmVSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 95 PHLTVLQNLTLAPIWVRGM----AKSEIeeiaMMYLKRVRIPDQAHK---FPGQLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:PRK15134 107 PLHTLEKQLYEVLSLHRGMrreaARGEI----LNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 168 PTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLL 257
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-242 |
4.99e-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: 116.87 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdVKAVEKIRRKVGM 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITK-LPMHKRARLGIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLtLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03218 80 LPQEASIFRKLTVEENI-LAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTrqFLG 242
Cdd:cd03218 159 EPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKV--YLG 232
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
21-232 |
5.94e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 5.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKvGMV--FQNFNLFPHLT 98
Cdd:PRK11300 20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEG--LPGHQIARM-GVVrtFQHVRLFREMT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLA----------------PIWVRgmAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK11300 97 VIENLLVAqhqqlktglfsgllktPAFRR--AESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-241 |
7.77e-32 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 122.12 E-value: 7.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQtGHIVVDGIELTD-DVKAVEKIRRKVGMVFQNFN--LFPH 96
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNlNRRQLLPVRHRIQVVFQDPNssLNPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 LTVLQnltlapIWVRGM---------AKSEIEEIAMMylKRVRI-PDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:PRK15134 379 LNVLQ------IIEEGLrvhqptlsaAQREQQVIAVM--EEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILD 450
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK15134 451 EPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLL 526
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-212 |
8.47e-32 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 115.41 E-value: 8.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 16 YNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG----------IELTDDVKAveKIRRKVG 85
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpqrSEVPDSLPL--TVRDLVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MvfqnfNLFPHLTVLQNLTLApiwvrgmAKSEIEEIammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:NF040873 80 M-----GRWARRGLWRRLTRD-------DRAAVDDA----LERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQvADSIV 212
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRR-ADPCV 189
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-221 |
2.13e-31 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 116.32 E-value: 2.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEK-IRRKVGMVFQN----FNlfPH 96
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKaFRRDIQMVFQDsisaVN--PR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 LTV-------LQNLTlapiwvrGMAKSEIEEIAMMYLKRVRIPDQ-AHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEP 168
Cdd:PRK10419 106 KTVreiirepLRHLL-------SLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEA 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 169 TSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIE 221
Cdd:PRK10419 179 VSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVE 232
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
21-214 |
3.26e-31 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 120.08 E-value: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekIRRKVGMVFQNFNLFPHlTVL 100
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADS--WRDQIAWVPQHPFLFAG-TIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLApiwVRGMAKSEIEEIAMM-YLKRV--RIPDQAHKFPGQ----LSGGQQQRVAIARALCMRPEIMLFDEPTSALD 173
Cdd:TIGR02857 414 ENIRLA---RPDASDAEIREALERaGLDEFvaALPQGLDTPIGEggagLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2504588632 174 PEMVKEVLDVMTELAgEGMTMVCVTHEMGFARqVADSIVFM 214
Cdd:TIGR02857 491 AETEAEVLEALRALA-QGRTVLLVTHRLALAA-LADRIVVL 529
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
18-227 |
6.83e-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: 119.92 E-value: 6.83e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 18 SYHA----LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltdDVKAV--EKIRRKVGMVFQNf 91
Cdd:COG5265 366 GYDPerpiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQ----DIRDVtqASLRAAIGIVPQD- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 92 nlfphlTVLQNLTLA-------PiwvrGMAKSEIEEIAmmylKRVRI-------PDQAHKFPGQ----LSGGQQQRVAIA 153
Cdd:COG5265 441 ------TVLFNDTIAyniaygrP----DASEEEVEAAA----RAAQIhdfieslPDGYDTRVGErglkLSGGEKQRVAIA 506
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 154 RALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCVTHemgfaR----QVADSIVFMAEGSIIESGSPAE 227
Cdd:COG5265 507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH-----RlstiVDADEILVLEAGRIVERGTHAE 578
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-227 |
8.09e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 114.41 E-value: 8.09e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD---DVKAvekirRK 83
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtpsRELA-----KR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQ------------NLTLAPiwvrgmaKSEIEEiAMMYLKrvrIPDQAHKFPGQLSGGQQQRVA 151
Cdd:COG4604 77 LAILRQENHINSRLTVRElvafgrfpyskgRLTAED-------REIIDE-AIAYLD---LEDLADRYLDELSGGQRQRAF 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 152 IARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG4604 146 IAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-230 |
9.76e-31 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 116.47 E-value: 9.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekiRRKVGM 86
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA---RARIGV 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTlapIWVR--GMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:PRK13536 119 VPQFDNLDLEFTVRENLL---VFGRyfGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFE 230
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
15-241 |
1.76e-30 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 114.12 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 15 WYNSYH--ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT--DDVKAVEKIRrkvgMVFQN 90
Cdd:PRK15112 20 WFRRQTveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIR----MIFQD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 91 --FNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRI-PDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:PRK15112 96 psTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 168 PTSALDPEMVKEVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK15112 176 ALASLDMSMRSQLINLMLELqEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKRLI 250
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
4-233 |
2.31e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.82 E-value: 2.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD---DVKAveki 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHlpmHKRA---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLtLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:COG1137 77 RLGIGYLPQEASIFRKLTVEDNI-LAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNP 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTmVCVT----HEMgfaRQVADSIVFMAEGSIIESGSPAEFFENPK 233
Cdd:COG1137 156 KFILLDEPFAGVDPIAVADIQKIIRHLKERGIG-VLITdhnvRET---LGICDRAYIISEGKVLAEGTPEEILNNPL 228
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-220 |
2.54e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 113.26 E-value: 2.54e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNS-----YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKI 80
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTK--LPEYKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNL--FPHLTVLQNLTLA------PIWVRGMAKSEIEEIAMmYLKRV------RIPDQAhkfpGQLSGGQ 146
Cdd:COG1101 79 AKYIGRVFQDPMMgtAPSMTIEENLALAyrrgkrRGLRRGLTKKRRELFRE-LLATLglglenRLDTKV----GLLSGGQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 147 QQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSII 220
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEEnNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
7-199 |
2.81e-30 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 117.85 E-value: 2.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVG-KWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVG 85
Cdd:TIGR02868 335 LELRDLSaGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSS--LDQDEVRRRVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFpHLTVLQNLTLApiwvRGMAKSEieEIAMMyLKRVRIPDQAHKFPG-----------QLSGGQQQRVAIAR 154
Cdd:TIGR02868 413 VCAQDAHLF-DTTVRENLRLA----RPDATDE--ELWAA-LERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALAR 484
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2504588632 155 ALCMRPEIMLFDEPTSALDPEMVKEVLDVMTElAGEGMTMVCVTH 199
Cdd:TIGR02868 485 ALLADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
7-224 |
3.27e-30 |
|
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: 112.11 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTddvkavEKIRRKVGM 86
Cdd:TIGR03740 1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT------RKDLHKIGS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTVLQNLTLAPIwVRGMAKSEIEEIammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:TIGR03740 75 LIESPPLYENLTARENLKVHTT-LLGLPDSRIDEV----LNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGS 224
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGK 207
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-224 |
3.72e-30 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 117.75 E-value: 3.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY-NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVG 85
Cdd:PRK13657 335 VEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRT--VTRASLRRNIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHlTVLQNLTLapiwvrGMAKSEIEEIaMMYLKRVripdQAHKF---------------PGQLSGGQQQRV 150
Cdd:PRK13657 413 VVFQDAGLFNR-SIEDNIRV------GRPDATDEEM-RAAAERA----QAHDFierkpdgydtvvgerGRQLSGGERQRL 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 151 AIARALCMRPEIMLFDEPTSALDPEM---VKEVLD-VMtelagEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGS 224
Cdd:PRK13657 481 AIARALLKDPPILILDEATSALDVETeakVKAALDeLM-----KGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS 552
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-241 |
6.18e-30 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 113.68 E-value: 6.18e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 19 YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHqTGHIVVDGIEL--TDDVKAVEKIRRK-----VGMVFQN- 90
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFngQDLQRISEKERRNlvgaeVAMIFQDp 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 91 -FNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQAHK---FPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:PRK11022 99 mTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELA-GEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALL 254
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
20-244 |
8.40e-30 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 116.88 E-value: 8.40e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG--IELTDDVKaVEKIRRKVGMVFQN--FNLFP 95
Cdd:PRK10261 338 HAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGqrIDTLSPGK-LQALRRDIQFIFQDpyASLDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 96 HLTVLQNLtLAPIWVRGMAKSEI--EEIAMMyLKRVRI-PDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:PRK10261 417 RQTVGDSI-MEPLRVHGLLPGKAaaARVAWL-LERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 173 DPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLGQI 244
Cdd:PRK10261 495 DVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAV 567
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-223 |
1.02e-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: 109.32 E-value: 1.02e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 17 NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAvekIRRKVGMVFQNFNLFpH 96
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA---LSSLISVLNQRPYLF-D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 LTVLQNLTLapiwvrgmakseieeiammylkrvripdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEM 176
Cdd:cd03247 89 TTLRNNLGR-----------------------------------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPIT 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2504588632 177 VKEVLDVMTELAgEGMTMVCVTHEM-GFARqvADSIVFMAEGSIIESG 223
Cdd:cd03247 134 ERQLLSLIFEVL-KDKTLIWITHHLtGIEH--MDKILFLENGKIIMQG 178
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-221 |
1.13e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 115.93 E-value: 1.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVdGIELtddvkavekirrKVG 85
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------------KIG 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNF-NLFPHLTVLQnltlapiWVRGMAKSEIEEIAMMYLKRVRI-PDQAHKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:COG0488 382 YFDQHQeELDPDKTVLD-------ELRDGAPGGTEQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSPPNVL 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 164 LFDEPTSALDPEMvKEVL-DVMTELAGegmTMVCVTHEMGFARQVADSIVFMAEGSIIE 221
Cdd:COG0488 455 LLDEPTNHLDIET-LEALeEALDDFPG---TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-224 |
1.26e-29 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 116.08 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekIRRKVGMVFQNFNLFPHlTV 99
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA--LRQAISVVSQRVHLFSA-TL 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLApiwvrgmAKSEIEEIAMMYLKRVRIPDQAHKFPG----------QLSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:PRK11160 431 RDNLLLA-------APNASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPT 503
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 170 SALDPEMVKEVLDVMTELAgEGMTMVCVTHemgfaRQVA----DSIVFMAEGSIIESGS 224
Cdd:PRK11160 504 EGLDAETERQILELLAEHA-QNKTVLMITH-----RLTGleqfDRICVMDNGQIIEQGT 556
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
21-244 |
2.16e-29 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 115.72 E-value: 2.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG----------IELTDDVKA-VEKIR-RKVGMVF 88
Cdd:PRK10261 31 AVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAqMRHVRgADMAMIF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 89 QN--FNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPDQA---HKFPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:PRK10261 111 QEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPAVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLG 242
Cdd:PRK10261 191 IADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPYTRALLA 270
|
..
gi 2504588632 243 QI 244
Cdd:PRK10261 271 AV 272
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
16-227 |
3.57e-29 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 110.46 E-value: 3.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 16 YNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMVFQNFNLFP 95
Cdd:PRK10253 17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQH--YASKEVARRIGLLAQNATTPG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 96 HLTVlQNLTL------APIWVRGmaKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:PRK10253 95 DITV-QELVArgryphQPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 170 SALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:PRK10253 172 TWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKE 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-227 |
4.45e-29 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 109.79 E-value: 4.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTEnaIIELRKVGKWYNSYH----------------------ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAH 58
Cdd:COG1134 1 MSS--MIEVENVSKSYRLYHepsrslkelllrrrrtrreefwALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 59 QTGHIVVDG-----IELtddvkavekirrkvGMVFQnfnlfPHLTVLQNLTL-APIWvrGMAKSEIEEiammylkrvRIP 132
Cdd:COG1134 79 TSGRVEVNGrvsalLEL--------------GAGFH-----PELTGRENIYLnGRLL--GLSRKEIDE---------KFD 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 133 DQA-----HKF---P-GQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGF 203
Cdd:COG1134 129 EIVefaelGDFidqPvKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGA 208
|
250 260
....*....|....*....|....
gi 2504588632 204 ARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG1134 209 VRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-245 |
5.09e-29 |
|
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: 109.92 E-value: 5.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVD--GIELTDDVKAVEKIRR 82
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYImrSGAELELYQLSEAERR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KV-----GMVFQNFNLFPHLTVLQNltlAPIWVRGMA-----KSEIEEIAMMYLKRVRI-PDQAHKFPGQLSGGQQQRVA 151
Cdd:TIGR02323 82 RLmrtewGFVHQNPRDGLRMRVSAG---ANIGERLMAigarhYGNIRATAQDWLEEVEIdPTRIDDLPRAFSGGMQQRLQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 152 IARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFE 230
Cdd:TIGR02323 159 IARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDlGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLD 238
|
250
....*....|....*
gi 2504588632 231 NPKSERTRQFLGQIL 245
Cdd:TIGR02323 239 DPQHPYTQLLVSSIL 253
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
7-225 |
1.17e-28 |
|
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: 107.96 E-value: 1.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKV 84
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISK--IGLHDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHlTVLQNltLAPIwvrgmAKSEIEEIaMMYLKRVRIPDQAHKFPGQL-----------SGGQQQRVAIA 153
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSN--LDPF-----GEYSDEEL-WQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 154 RALCMRPEIMLFDEPTSALDPE---MVKEVLdvMTELAgeGMTMVCVTHEMgfaRQVADS--IVFMAEGSIIESGSP 225
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPEtdaLIQKTI--REAFK--DCTVLTIAHRL---DTIIDSdrILVLDKGRVVEFDSP 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
5-230 |
1.81e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 109.51 E-value: 1.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTddvKAVEKIRRKV 84
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP---SRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTlapIWVR--GMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK13537 83 GVVPQFDNLDPDFTVRENLL---VFGRyfGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFE 230
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-230 |
2.79e-28 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 112.20 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 3 ENAIIELRKVGKWYNSY-----HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVV----DGIELTD- 72
Cdd:TIGR03269 276 GEPIIKVRNVSKRYISVdrgvvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKp 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 73 DVKAVEKIRRKVGMVFQNFNLFPHLTVLQNLTLApiwvrgMAKSEIEEIAMM----YLKRVRIPDQA-----HKFPGQLS 143
Cdd:TIGR03269 356 GPDGRGRAKRYIGILHQEYDLYPHRTVLDNLTEA------IGLELPDELARMkaviTLKMVGFDEEKaeeilDKYPDELS 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 144 GGQQQRVAIARALCMRPEIMLFDEPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:TIGR03269 430 EGERHRVALAQVLIKEPRIVILDEPTGTMDPitkvDVTHSILKAREEM---EQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
250
....*....|.
gi 2504588632 220 IESGSPAEFFE 230
Cdd:TIGR03269 507 VKIGDPEEIVE 517
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-219 |
4.77e-28 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 105.21 E-value: 4.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAvEKIRRKVGMV---FQNFNLFPHL 97
Cdd:cd03215 15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPR-DAIRAGIAYVpedRKREGLVLDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNLTLapiwvrgmakseieeiammylkrvripdqahkfPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMV 177
Cdd:cd03215 94 SVAENIAL---------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAK 140
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2504588632 178 KEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:cd03215 141 AEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
22-232 |
8.03e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.35 E-value: 8.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAvekIRRKVGMVFQNFNLFPHlTVL 100
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHY---LHRQVALVGQEPVLFSG-SVR 572
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLapiwvrGMAKSEIEEIaMMYLKRVRIPDQAHKFP-----------GQLSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:TIGR00958 573 ENIAY------GLTDTPDEEI-MAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 170 SALDPEMVKEVLDVMTElagEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:TIGR00958 646 SALDAECEQLLQESRSR---ASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
20-220 |
8.07e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 110.49 E-value: 8.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTddVKAVEK-IRRKVGMVFQN---FNLFP 95
Cdd:COG1129 266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVR--IRSPRDaIRAGIAYVPEDrkgEGLVL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 96 HLTVLQNLTLAPI-------WVRgmaKSEIEEIAMMYLKRVRI----PDQAhkfPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:COG1129 344 DLSIRENITLASLdrlsrggLLD---RRRERALAEEYIKRLRIktpsPEQP---VGNLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 165 FDEPTSALDpemV---KEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSII 220
Cdd:COG1129 418 LDEPTRGID---VgakAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-231 |
1.12e-27 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 105.73 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 3 ENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdVKAVEKIRR 82
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITD-WQTAKIMRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQNFNLFPHLTVLQNLTLAPIWVRgmAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGGFFAE--RDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:PRK11614 159 LLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
22-227 |
1.30e-27 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 108.78 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAVE--KIRRKVGMVFQN----FNL-- 93
Cdd:PRK09536 19 LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAG----DDVEALSarAASRRVASVPQDtslsFEFdv 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 --------FPHLTVLQNLTLAPIWV--RGMAKSEIEEIAmmylkrvripDQAHKfpgQLSGGQQQRVAIARALCMRPEIM 163
Cdd:PRK09536 95 rqvvemgrTPHRSRFDTWTETDRAAveRAMERTGVAQFA----------DRPVT---SLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
22-227 |
1.99e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.48 E-value: 1.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkavekirrkvgmvFQNFNLFPHLTVLQ 101
Cdd:PRK11231 18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISM---------------LSSRQLARRLALLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTLAP--IWVR--------------GMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:PRK11231 83 QHHLTPegITVRelvaygrspwlslwGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-230 |
4.12e-27 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 108.95 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMVFQNFNLFpHLTVL 100
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRD--YTLASLRNQVALVSQNVHLF-NDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLAPiwVRGMAKSEIEEIAMM-----YLKRvrIPDQAHKFPGQ----LSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:PRK11176 435 NNIAYAR--TEQYSREQIEEAARMayamdFINK--MDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILDEATSA 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 172 LDPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFE 230
Cdd:PRK11176 511 LDTESERAIQAALDELQ-KNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
21-232 |
6.02e-27 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 105.96 E-value: 6.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEA---HQTGHIVVDGIE-LTDDVKAVEKIR-RKVGMVFQN--FNL 93
Cdd:PRK09473 31 AVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAangRIGGSATFNGREiLNLPEKELNKLRaEQISMIFQDpmTSL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 FPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMYLKRVRIPdQAHK----FPGQLSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:PRK09473 111 NPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMP-EARKrmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADEPT 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 170 SALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:PRK09473 190 TALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
20-245 |
1.98e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.06 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIrciNRLEAHQTGHIVVDGIELTDDVKA-VEKIRRKVGMVFQNFNLFPHLT 98
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLLNGMPIdAKEMRAISAYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLA-----PiwvRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQ------LSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:TIGR00955 116 VREHLMFQahlrmP---RRVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDE 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 168 PTSALDPEMVKEVLDVMTELAGEGMTMVCVTH-------EMgFarqvaDSIVFMAEGSIIESGSP---AEFFEN-----P 232
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHqpsselfEL-F-----DKIILMAEGRVAYLGSPdqaVPFFSDlghpcP 266
|
250
....*....|...
gi 2504588632 233 KSERTRQFLGQIL 245
Cdd:TIGR00955 267 ENYNPADFYVQVL 279
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-223 |
7.04e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 105.25 E-value: 7.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTddvKAVEKIRRK--V 84
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYN---KLDHKLAAQlgI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTLAPIWVRGMAK------SEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCM 158
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLYIGRHLTKKVCGvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 159 RPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-227 |
1.04e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.93 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 25 VSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQtGHIVVDGIELTDdvKAVEKIRRKVGMVFQNFNLFpHLTVLQNLT 104
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRE--LDPESWRKHLSWVGQNPQLP-HGTLRDNVL 444
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 105 LA-------PIWvRGMAKSEIEEiammYLKRV------RIPDQAhkfpGQLSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:PRK11174 445 LGnpdasdeQLQ-QALENAWVSE----FLPLLpqgldtPIGDQA----AGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 172 LDPEMVKEVLDVMTElAGEGMTMVCVTHEMGFARQVaDSIVFMAEGSIIESGSPAE 227
Cdd:PRK11174 516 LDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAE 569
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
5-243 |
2.36e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 99.97 E-value: 2.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDgielTDDVKAV---EKIR 81
Cdd:PRK10895 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID----DEDISLLplhARAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 82 RKVGMVFQNFNLFPHLTVLQNLtLAPIWVR-GMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:PRK10895 78 RGIGYLPQEASIFRRLSVYDNL-MAVLQIRdDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTrqF 240
Cdd:PRK10895 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRV--Y 234
|
...
gi 2504588632 241 LGQ 243
Cdd:PRK10895 235 LGE 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-239 |
3.51e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 9 LRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvkavekiRRKVGMVF 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-------------GLRIGYLP 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 89 QNFNLFPHLTVLQNLT--LAPIW--VRGMAK-------------------------------SEIEEIammyLKRVRIPD 133
Cdd:COG0488 68 QEPPLDDDLTVLDTVLdgDAELRalEAELEEleaklaepdedlerlaelqeefealggweaeARAEEI----LSGLGFPE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 134 QAHKFP-GQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVK--EvldvmTELAGEGMTMVCVTHEMGFARQVADS 210
Cdd:COG0488 144 EDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwlE-----EFLKNYPGTVLVVSHDRYFLDRVATR 218
|
250 260
....*....|....*....|....*....
gi 2504588632 211 IVFMAEGSIIESGSPAEFFENPKSERTRQ 239
Cdd:COG0488 219 ILELDRGKLTLYPGNYSAYLEQRAERLEQ 247
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
22-199 |
5.70e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 102.96 E-value: 5.70e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVV-DGIELtddvkavekirrkvgmvfqnfnLF----PH 96
Cdd:COG4178 379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV----------------------LFlpqrPY 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 L---TVLQNLTLaPIWVRGMAKSEIEEIammyLKRVRIPDQAHKF------PGQLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:COG4178 437 LplgTLREALLY-PATAEAFSDAELREA----LEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDE 511
|
170 180 190
....*....|....*....|....*....|..
gi 2504588632 168 PTSALDPEMVKEVLDVMTElAGEGMTMVCVTH 199
Cdd:COG4178 512 ATSALDEENEAALYQLLRE-ELPGTTVISVGH 542
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-231 |
8.23e-25 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.93 E-value: 8.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTEnAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQT--GHIVVDGIELT-DDVKAV 77
Cdd:PRK13549 1 MME-YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEELQaSNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 78 EkiRRKVGMVFQNFNLFPHLTVLQNLTLAPIWVRG--MAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARA 155
Cdd:PRK13549 80 E--RAGIAIIHQELALVKELSVLENIFLGNEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 156 LCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFEN 231
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTED 233
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
21-224 |
2.02e-24 |
|
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: 101.35 E-value: 2.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekIRRKVGMVFQNFNLFPHlTVL 100
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT--LRQFINYLPQEPYIFSG-SIL 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLAPiwVRGMAKSEIEEIammyLKRVRIPDQAHKFP-----------GQLSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:TIGR01193 566 ENLLLGA--KENVSQDEIWAA----CEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILDEST 639
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 170 SALDPEMVKEVLDVMTELAGEgmTMVCVTHEMGFARQVaDSIVFMAEGSIIESGS 224
Cdd:TIGR01193 640 SNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-200 |
2.53e-24 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 96.71 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltDDVKAV--E 78
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG----EDISTLkpE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKVGMVFQNFNLFPHlTVLQNLTLaPIWVRGMAKSEIEEIAmmYLKRVRIPDQA-HKFPGQLSGGQQQRVAIARALC 157
Cdd:PRK10247 78 IYRQQVSYCAQTPTLFGD-TVYDNLIF-PWQIRNQQPDPAIFLD--DLERFALPDTIlTKNIAELSGGEKQRISLIRNLQ 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHE 200
Cdd:PRK10247 154 FMPKVLLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHD 197
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-217 |
4.97e-24 |
|
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: 99.90 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQT--GHIVVDGIEL-TDDVKAVEkiRR 82
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLkASNIRDTE--RA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQNFNLFPHLTVLQNLTLA-PIWVRG--MAKSEIEEIAMMYLKRVRIPDQAHKFP-GQLSGGQQQRVAIARALCM 158
Cdd:TIGR02633 79 GIVIIHQELTLVPELSVAENIFLGnEITLPGgrMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 159 RPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:TIGR02633 159 QARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDG 217
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
22-230 |
1.15e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 99.05 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT--DDvkavEKIRRKVGMVFQNFNLFPHlTV 99
Cdd:COG4618 348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDR----EELGRHIGYLPQDVELFDG-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNltlapIwVR-GMAKSE-IEEIAmmylKRVRIPDQAHKFP-----------GQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:COG4618 423 AEN-----I-ARfGDADPEkVVAAA----KLAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVLD 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGfARQVADSIVFMAEGSIIESGSPAEFFE 230
Cdd:COG4618 493 EPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
22-219 |
1.37e-23 |
|
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: 94.85 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMVFQNFNLFPHlTVLQ 101
Cdd:cd03248 30 LQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQ--YEHKYLHSKVSLVGQEPVLFAR-SLQD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTLapiwvrGMAKSEIEEI---AMMYLKRVRIPDQAHKFP-------GQLSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:cd03248 107 NIAY------GLQSCSFECVkeaAQKAHAHSFISELASGYDtevgekgSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2504588632 172 LDPEMVKEVLDVMTElAGEGMTMVCVTHEMGFARQvADSIVFMAEGSI 219
Cdd:cd03248 181 LDAESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
21-218 |
1.67e-23 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 94.07 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQtGHIVVDGieltddvkavekirrKVGMVFQNfnlfPHL-- 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALlGELEKLS-GSVSVPG---------------SIAYVSQE----PWIqn 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 -TVLQNLTLApiwvrgmakSEIEEiaMMYLKRVR----IPDQAhKFPGQ-----------LSGGQQQRVAIARALCMRPE 161
Cdd:cd03250 80 gTIRENILFG---------KPFDE--ERYEKVIKacalEPDLE-ILPDGdlteigekginLSGGQKQRISLARAVYSDAD 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 162 IMLFDEPTSALDPEMVKEVLD--VMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGS 218
Cdd:cd03250 148 IYLLDDPLSAVDAHVGRHIFEncILGLLL-NNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
23-241 |
1.75e-23 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 95.15 E-value: 1.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 23 RDVSLSIGKGEKVVVCGPSGSGKStmIRCINRLE-----AHQT-GHIVVDGIELtddvkAVEKIR-RKVGMVFQN----F 91
Cdd:PRK10418 20 HGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGilpagVRQTaGRVLLDGKPV-----APCALRgRKIATIMQNprsaF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 92 NlfPHLTVLQNL--TLApiwVRGMAKSEIEEIAMMylKRVRIPDQA---HKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:PRK10418 93 N--PLHTMHTHAreTCL---ALGKPADDATLTAAL--EAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFL 241
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
7-223 |
4.59e-23 |
|
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: 93.37 E-value: 4.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYH----------------------ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIV 64
Cdd:cd03220 1 IELENVSKSYPTYKggssslkklgilgrkgevgefwALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 65 VDG-----IELtddvkavekirrkvGMVFQnfnlfPHLTVLQNLTLAPIWvRGMAKSEI----EEIAMM------YLKRV 129
Cdd:cd03220 81 VRGrvsslLGL--------------GGGFN-----PELTGRENIYLNGRL-LGLSRKEIdekiDEIIEFselgdfIDLPV 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 130 RipdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVAD 209
Cdd:cd03220 141 K----------TYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCD 210
|
250
....*....|....
gi 2504588632 210 SIVFMAEGSIIESG 223
Cdd:cd03220 211 RALVLEKGKIRFDG 224
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-227 |
5.42e-23 |
|
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: 97.18 E-value: 5.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQ--TGHIV-------------------- 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 65 -------------VDGIELTDDVKAveKIRRKVGMVFQ-NFNLFPHLTVLQNLtLAPIWVRGMAKSEIEEIAMMYLKRVR 130
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLSDKLRR--RIRKRIAIMLQrTFALYGDDTVLDNV-LEALEEIGYEGKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 131 IPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELA-GEGMTMVCVTHEMGFARQVAD 209
Cdd:TIGR03269 158 LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVkASGISMVLTSHWPEVIEDLSD 237
|
250
....*....|....*...
gi 2504588632 210 SIVFMAEGSIIESGSPAE 227
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDE 255
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
22-225 |
8.71e-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: 91.82 E-value: 8.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQT--GHIVVDGIELTDdVKAVEKIRRKVGMVFQNfnlfphltv 99
Cdd:cd03217 16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKYEVteGEILFKGEDITD-LPPEERARLGIFLAFQY--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 lqnltlaPIwvrgmaksEIEEIAMM-YLKRVRIpdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVK 178
Cdd:cd03217 86 -------PP--------EIPGVKNAdFLRYVNE---------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2504588632 179 EVLDVMTELAGEGMTMVCVTH-EMGFARQVADSIVFMAEGSIIESGSP 225
Cdd:cd03217 142 LVAEVINKLREEGKSVLIITHyQRLLDYIKPDRVHVLYDGRIVKSGDK 189
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
22-199 |
8.74e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 92.24 E-value: 8.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDG--IELTDDVKAVEKIRRKVGMVfqnfnlfPHLTV 99
Cdd:PRK13539 18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGgdIDDPDVAEACHYLGHRNAMK-------PALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLapiW--VRGMAKSEIEEIammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMV 177
Cdd:PRK13539 91 AENLEF---WaaFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|...
gi 2504588632 178 KEVLDVMTE-LAGEGMtMVCVTH 199
Cdd:PRK13539 164 ALFAELIRAhLAQGGI-VIAATH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-217 |
1.71e-22 |
|
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: 89.43 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIvvdgieltddvkavekirrkvgm 86
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 vfqnfnlfphlTVLQNLTLApiwvrgmakseieeiammYLKrvripdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:cd03221 58 -----------TWGSTVKIG------------------YFE-------------QLSGGEKMRLALAKLLLENPNLLLLD 95
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGegmTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:cd03221 96 EPTNHLDLESIEALEEALKEYPG---TVILVSHDRYFLDQVATKIIELEDG 143
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-236 |
1.96e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 92.64 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKaveki 80
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQ----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNL---FPHLT---VLQNLTLAPIWVRgMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIAR 154
Cdd:PRK15056 77 KNLVAYVPQSEEVdwsFPVLVedvVMMGRYGHMGWLR-RAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 155 ALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVfMAEGSIIESGSPAEFFENPKS 234
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTV-MVKGTVLASGPTETTFTAENL 234
|
..
gi 2504588632 235 ER 236
Cdd:PRK15056 235 EL 236
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
22-219 |
1.61e-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: 92.80 E-value: 1.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKavEKIRRKVGMVFQNFNLFPHlTVLQ 101
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDR--ETFGKHIGYLPQDVELFPG-TVAE 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTlapiwvRGMAKSEIEEIammyLKRVRIPDqAH----KFP-----------GQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:TIGR01842 411 NIA------RFGENADPEKI----IEAAKLAG-VHelilRLPdgydtvigpggATLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGfARQVADSIVFMAEGSI 219
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRI 531
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-217 |
3.21e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 92.25 E-value: 3.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQ-TGHIvvdgieLTDDVKAVEKIRRKVGMVFQNFNLFPHLTV 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALaGRIQGNNfTGTI------LANNRKPTKQILKRTGFVTQDDILYPHLTV 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNL----------TLAPIWVRGMAKSEIEEIAMMYLKRVRIpdqAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:PLN03211 158 RETLvfcsllrlpkSLTKQEKILVAESVISELGLTKCENTII---GNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2504588632 170 SALDPEMVKEVLDVMTELAGEGMTMVCVTHE-MGFARQVADSIVFMAEG 217
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-232 |
6.20e-21 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 91.31 E-value: 6.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMVFQNFNLFPHlTVL 100
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTK--LQLDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLA-PiwvrGMAKSEIEEIAMM---YLKRVRIPDQAHKFPGQ----LSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:PRK10789 407 NNIALGrP----DATQQEIEHVARLasvHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAV 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 173 DPEMVKEVLDVMTELaGEGMTMVCVTHEMGfARQVADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:PRK10789 483 DGRTEHQILHNLRQW-GEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-222 |
1.06e-20 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 90.23 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQT--GHIVVDGIELT-DDVKAVEKirr 82
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILFDGEVCRfKDIRDSEA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 kVGMVF--QNFNLFPHLTVLQNLTLA-PIWVRGMAK-SEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCM 158
Cdd:NF040905 78 -LGIVIihQELALIPYLSIAENIFLGnERAKRGVIDwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 159 RPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIES 222
Cdd:NF040905 157 DVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIET 220
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
16-229 |
1.63e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 87.76 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 16 YNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIRRKVGMVFQNfnlfP 95
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLALRQQVATVFQD----P 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 96 HLTVLQNLTLAPIW--VRGMAKSEiEEIAMMYLKRVRIPDqAHKFPGQ----LSGGQQQRVAIARALCMRPEIMLFDEPT 169
Cdd:PRK13638 87 EQQIFYTDIDSDIAfsLRNLGVPE-AEITRRVDEALTLVD-AQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 170 SALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFF 229
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-227 |
2.54e-20 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 86.43 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQtGHIVVDGIELtDDVKAVEKIRRKvGMVFQNFNLFPHLTVLQ 101
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ-GEILLNGRPL-SDWSAAELARHR-AYLSQQQSPPFAMPVFQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTLApiwVRGMAKSEIEEIAMMYL-KRVRIPDQAHKFPGQLSGGQQQRVAIArALCMR--PEI------MLFDEPTSAL 172
Cdd:COG4138 89 YLALH---QPAGASSEAVEQLLAQLaEALGLEDKLSRPLTQLSGGEWQRVRLA-AVLLQvwPTInpegqlLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 173 DPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-225 |
2.54e-20 |
|
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: 85.54 E-value: 2.54e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltdDVKAV--EKIRRKVGMVFQNFNLFPHlT 98
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGI----DISTIplEDLRSSLTIIPQDPTLFSG-T 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLapiwvrgMAKSEIEEIammyLKRVRIPDQAHkfpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVK 178
Cdd:cd03369 98 IRSNLDP-------FDEYSDEEI----YGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2504588632 179 EVLDVMTELAgEGMTMVCVTHEMgfaRQVA--DSIVFMAEGSIIESGSP 225
Cdd:cd03369 163 LIQKTIREEF-TNSTILTIAHRL---RTIIdyDKILVMDAGEVKEYDHP 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-221 |
4.25e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 88.69 E-value: 4.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 23 RDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT-----DDVKA----VEKIRRKVGmvfqnfnL 93
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISprsplDAVKKgmayITESRRDNG-------F 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 FPHLTVLQNLTLAPIWVRGMAK------SEIEEIAMMYLKRVRIPDQAHKFP---GQLSGGQQQRVAIARALCMRPEIML 164
Cdd:PRK09700 353 FPNFSIAQNMAISRSLKDGGYKgamglfHEVDEQRTAENQRELLALKCHSVNqniTELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIE 221
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
21-199 |
6.72e-20 |
|
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: 84.33 E-value: 6.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGielTDDVKAVEKIRRKVGMVFQNFNLFPHLTVL 100
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNG---TPLAEQRDEPHENILYLGHLPGLKPELSAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLT-LAPIwvRGMAKSEIEEIammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKE 179
Cdd:TIGR01189 92 ENLHfWAAI--HGGAQRTIEDA----LAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVAL 165
|
170 180
....*....|....*....|
gi 2504588632 180 VLDVMTELAGEGMTMVCVTH 199
Cdd:TIGR01189 166 LAGLLRAHLARGGIVLLTTH 185
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
5-201 |
1.57e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.89 E-value: 1.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdVKAVEKIRRKV 84
Cdd:PRK11288 3 PYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRF-ASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTLAPIWVRG--MAKSEIEEIAMMYLKRVRI---PDQAHKFpgqLSGGQQQRVAIARALCMR 159
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPHKGgiVNRRLLNYEAREQLEHLGVdidPDTPLKY---LSIGQRQMVEIAKALARN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2504588632 160 PEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEM 201
Cdd:PRK11288 159 ARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRM 200
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
22-225 |
3.45e-19 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 83.19 E-value: 3.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQ--TGHIVVDGIELTDdVKAVEKIRRKVGMVFQNFNLFPHLTV 99
Cdd:COG0396 16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEvtSGSILLDGEDILE-LSPDERARAGIFLAFQYPVEIPGVSV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLAPIWVRGMAKSEIEEIAMM--YLKRVRIPDqahKF------PGqLSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:COG0396 95 SNFLRTALNARRGEELSAREFLKLLkeKMKELGLDE---DFldryvnEG-FSGGEKKRNEILQMLLLEPKLAILDETDSG 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 172 LDPEMVKEVLDVMTELAGEGMTMVCVTHemgFAR----QVADSIVFMAEGSIIESGSP 225
Cdd:COG0396 171 LDIDALRIVAEGVNKLRSPDRGILIITH---YQRildyIKPDFVHVLVDGRIVKSGGK 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-228 |
4.67e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 85.49 E-value: 4.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT--DDVKAve 78
Cdd:PRK15439 6 TTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArlTPAKA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 kirRKVG--MVFQNFNLFPHLTVLQNLTLapiwvrGMAKSEIEEIAM-MYLKRVRIPDQAHKFPGQLSGGQQQRVAIARA 155
Cdd:PRK15439 84 ---HQLGiyLVPQEPLLFPNLSVKENILF------GLPKRQASMQKMkQLLAALGCQLDLDSSAGSLEVADRQIVEILRG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 156 LCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:PRK15439 155 LMRDSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
2-219 |
7.78e-19 |
|
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: 84.88 E-value: 7.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 2 TENAIIELRKVGKWY-NSYHALR--DVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQTGHIVVDGIELtdDVKAV 77
Cdd:TIGR02633 253 IGDVILEARNLTCWDvINPHRKRvdDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPV--DIRNP 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 78 EK-IRRKVGMVFQN---FNLFPHLTVLQNLTLAPI---WVRGMAKSEIEEIAMMY-LKRVRIPDQAHKFP-GQLSGGQQQ 148
Cdd:TIGR02633 331 AQaIRAGIAMVPEDrkrHGIVPILGVGKNITLSVLksfCFKMRIDAAAELQIIGSaIQRLKVKTASPFLPiGRLSGGNQQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 149 RVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
25-199 |
9.86e-19 |
|
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: 81.39 E-value: 9.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 25 VSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGielTDDVKAVEKIRRKVGMVFQNFNLFPHLTVLQNLT 104
Cdd:cd03231 19 LSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLDFQRDSIARGLLYLGHAPGIKTTLSVLENLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 105 LapiWVRGMAKSEIEEIammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVM 184
Cdd:cd03231 96 F---WHADHSDEQVEEA----LARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAM 168
|
170
....*....|....*
gi 2504588632 185 TELAGEGMTMVCVTH 199
Cdd:cd03231 169 AGHCARGGMVVLTTH 183
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-232 |
3.43e-18 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 81.88 E-value: 3.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCInrLEAH-QTGHIVVD-----GIELTddvKAVEKIRRKV-----GMVF 88
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAI--CGITkDNWHVTADrfrwnGIDLL---KLSPRERRKIigreiAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 89 QNFN--LFPHLTVLQNLTLA--------PIWVRGMAKSEIeeiAMMYLKRVRIPDqaHK-----FPGQLSGGQQQRVAIA 153
Cdd:COG4170 96 QEPSscLDPSAKIGDQLIEAipswtfkgKWWQRFKWRKKR---AIELLHRVGIKD--HKdimnsYPHELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 154 RALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAG-EGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-199 |
4.08e-18 |
|
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: 78.73 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVvdgieltddvkavekirrkvgmvfqnfnlfphltvlq 101
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG------------------------------------- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 nltlapiwvrgmaKSEIEEIAMM----YLKRVRIPDQ-AHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEM 176
Cdd:cd03223 60 -------------MPEGEDLLFLpqrpYLPLGTLREQlIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
|
170 180
....*....|....*....|...
gi 2504588632 177 VKEVLDVMTElagEGMTMVCVTH 199
Cdd:cd03223 127 EDRLYQLLKE---LGITVISVGH 146
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
39-231 |
6.18e-18 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 82.75 E-value: 6.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 39 GPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekiRRKVGMVFQNFNLFPHLTVLQN-LTLAPIWVRGMAKSE 117
Cdd:TIGR01257 963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAV---RQSLGMCPQHNILFHHLTVAEHiLFYAQLKGRSWEEAQ 1039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 118 IEEIAMmyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAgEGMTMVCV 197
Cdd:TIGR01257 1040 LEMEAM--LEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYR-SGRTIIMS 1116
|
170 180 190
....*....|....*....|....*....|....
gi 2504588632 198 THEMGFARQVADSIVFMAEGSIIESGSPAeFFEN 231
Cdd:TIGR01257 1117 THHMDEADLLGDRIAIISQGRLYCSGTPL-FLKN 1149
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
21-227 |
1.09e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 81.71 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRL------EAHQTGHIVVDG-IEltddvkavekIRRKVGMVFQNFNL 93
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLlpasegEAWLFGQPVDAGdIA----------TRRRVGYMSQAFSL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 94 FPHLTVLQNLTL-APIWvrGMAKSEIEE-IAMMyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:NF033858 351 YGELTVRQNLELhARLF--HLPAAEIAArVAEM-LERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSG 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 172 LDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFArQVADSIVFMAEGSIIESGSPAE 227
Cdd:NF033858 428 VDPVARDMFWRLLIELSREdGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAA 483
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
22-247 |
1.14e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.83 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTD-DVKAvekIRRKVGMVFQNFNLFPHLTVL 100
Cdd:PRK10575 27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESwSSKA---FARKVAYLPQQLPAAEGMTVR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLA--PiWVRGMAK------SEIEE-IAMMYLKRVripdqAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:PRK10575 104 ELVAIGryP-WHGALGRfgaadrEKVEEaISLVGLKPL-----AHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 172 LDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTRQFLGQILEH 247
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPH 254
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-223 |
1.20e-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: 78.91 E-value: 1.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 16 YNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIeltDDVKAVEKIRRKVGMVF-QNFNLF 94
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL---VPWKRRKKFLRRIGVVFgQKTQLW 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 95 PHLTVLQNLTL-APIW--VRGMAKSEIEEIAMMyLKRVRIPDQAHKfpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSA 171
Cdd:cd03267 108 WDLPVIDSFYLlAAIYdlPPARFKKRLDELSEL-LDLEELLDTPVR---QLSLGQRMRAEIAAALLHEPEILFLDEPTIG 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 172 LDPEMVKEVLDVMTELAGEGMTMVCVT-HEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03267 184 LDVVAQENIRNFLKEYNRERGTTVLLTsHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-199 |
1.25e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQ--TGHIVVDGIELTDDVKAVEKIRRKvgmvfQNFNlfphl 97
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTpvAGCVDVPDNQFGREASLIDAIGRK-----GDFK----- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNLTLApiwvrGMAKseieeiAMMYLKRVRipdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMV 177
Cdd:COG2401 114 DAVELLNAV-----GLSD------AVLWLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|...
gi 2504588632 178 KEVLDVMTELAGE-GMTMVCVTH 199
Cdd:COG2401 173 KRVARNLQKLARRaGITLVVATH 195
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
22-200 |
2.00e-17 |
|
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: 77.67 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEA-HQTGHIVVDGIELTDDvkavekIRRKVGMVFQNFNLFPHLTV 99
Cdd:cd03232 23 LNNISGYVKPGTLTALMGESGAGKTTLLDVLaGRKTAgVITGEILINGRPLDKN------FQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLTLAPiWVRGmakseieeiammylkrvripdqahkfpgqLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKE 179
Cdd:cd03232 97 REALRFSA-LLRG-----------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|.
gi 2504588632 180 VLDVMTELAGEGMTMVCVTHE 200
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIHQ 167
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-227 |
4.62e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 79.69 E-value: 4.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKvGMVF-----QNFNLFP 95
Cdd:COG3845 273 ALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITG--LSPRERRRL-GVAYipedrLGRGLVP 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 96 HLTVLQNLTL-----APIWVRG-MAKSEIEEIAMMYLKR--VRIPDQAHKFpGQLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:COG3845 350 DMSVAENLILgryrrPPFSRGGfLDRKAIRAFAEELIEEfdVRTPGPDTPA-RSLSGGNQQKVILARELSRDPKLLIAAQ 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 168 PTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:COG3845 429 PTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAE 488
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
5-220 |
5.33e-17 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 79.66 E-value: 5.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 5 AIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT-DDVKAVEKirRK 83
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQE--AG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNLTLAPIWVRGMAK---SEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRP 160
Cdd:PRK10762 81 IGIIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFES 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 161 EIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSII 220
Cdd:PRK10762 161 KVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFI 220
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
20-237 |
6.23e-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: 6.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLeAHQT-GHIVVDGIeltDDVKAVEKIRRKVGMVF-QNFNLFPHL 97
Cdd:COG4586 36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGI-LVPTsGEVRVLGY---VPFKRRKEFARRIGVVFgQRSQLWWDL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNLTL-APIWvrGMAKSEIEE-IAMM--------YLKR-VRipdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:COG4586 112 PAIDSFRLlKAIY--RIPDAEYKKrLDELvelldlgeLLDTpVR----------QLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 167 EPTSALDPEMVKEVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERT 237
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-231 |
1.40e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 78.86 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRC-INRLEAHQTGHIVvdgieltddvkavekIRRKVGMVFQNFNLFpHLTVL 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVV---------------IRGSVAYVPQVSWIF-NATVR 696
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLTLApiwvrgmAKSEIEEiammYLKRVRIPDQAHK---FPGQ-----------LSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:PLN03232 697 ENILFG-------SDFESER----YWRAIDVTALQHDldlLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFD 765
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVaDSIVFMAEGSIIESGSPAEFFEN 231
Cdd:PLN03232 766 DPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSKS 829
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
6-173 |
1.71e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 76.31 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvkavekiRRKVG 85
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG-------------KLRIG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPH--LTVLQNLTLAPiwvrGMAKSEIeeiaMMYLKRVRiPDQAHKFPGQ-LSGGQQQRVAIARALCMRPEI 162
Cdd:PRK09544 71 YVPQKLYLDTTlpLTVNRFLRLRP----GTKKEDI----LPALKRVQ-AGHLIDAPMQkLSGGETQRVLLARALLNRPQL 141
|
170
....*....|.
gi 2504588632 163 MLFDEPTSALD 173
Cdd:PRK09544 142 LVLDEPTQGVD 152
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-211 |
2.08e-16 |
|
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: 78.05 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNS-YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRcinrleahqtghiVVDGIELTDDVKAVEKIRRKV 84
Cdd:TIGR03719 4 IYTMNRVSKVVPPkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLR-------------IMAGVDKDFNGEARPQPGIKV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 85 GMVFQNFNLFPHLTVLQNLTLAPIWVRGMAKsEIEEIAMMYL-----------------------------KRVRIPDQA 135
Cdd:TIGR03719 71 GYLPQEPQLDPTKTVRENVEEGVAEIKDALD-RFNEISAKYAepdadfdklaaeqaelqeiidaadawdldSQLEIAMDA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 136 HKFP------GQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGegmTMVCVTHEMGFARQVAD 209
Cdd:TIGR03719 150 LRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYPG---TVVAVTHDRYFLDNVAG 226
|
..
gi 2504588632 210 SI 211
Cdd:TIGR03719 227 WI 228
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-219 |
3.61e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 3.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 24 DVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQTGHIVVDGIELtdDVKA-VEKIRRKVGMVFQN---FNLFPHLT 98
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPV--KIRNpQQAIAQGIAMVPEDrkrDGIVPVMG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLAPI--WVRGMAKSEIEEIAMM--YLKRVRI----PDQAhkfPGQLSGGQQQRVAIARALCMRPEIMLFDEPTS 170
Cdd:PRK13549 358 VGKNITLAALdrFTGGSRIDDAAELKTIleSIQRLKVktasPELA---IARLSGGNQQKAVLAKCLLLNPKILILDEPTR 434
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2504588632 171 ALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:PRK13549 435 GIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-227 |
4.61e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.97 E-value: 4.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 25 VSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQtGHIVVDGIELtDDVKAVEKIRRKVGMVFQNFNLFpHLTVLQNLT 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPGS-GSIQFAGQPL-EAWSAAELARHRAYLSQQQTPPF-AMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 105 L--APIWVRGMAKSEIEEIAmmylKRVRIPDQAHKFPGQLSGGQQQRVAIArALCMR--PEI------MLFDEPTSALDP 174
Cdd:PRK03695 92 LhqPDKTRTEAVASALNEVA----EALGLDDKLGRSVNQLSGGEWQRVRLA-AVVLQvwPDInpagqlLLLDEPMNSLDV 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 175 EMVKeVLD-VMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAE 227
Cdd:PRK03695 167 AQQA-ALDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
22-219 |
5.12e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.58 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELT-----DDVKA----VEKIRRKVGMVFQnfn 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtrspqDGLANgivyISEDRKRDGLVLG--- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 93 lfphLTVLQNLTLAPI------WVRGMAKSEIEEIA-MMYLKRVRIP--DQAhkfPGQLSGGQQQRVAIARALCMRPEIM 163
Cdd:PRK10762 345 ----MSVKENMSLTALryfsraGGSLKHADEQQAVSdFIRLFNIKTPsmEQA---IGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2504588632 164 LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-230 |
5.99e-16 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 76.91 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI----NRLEAHQT--GHIV-------VDGIELTDDV---KAVEKIRRKvg 85
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALlaemDKVEGHVHmkGSVAyvpqqawIQNDSLRENIlfgKALNEKYYQ-- 731
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNFNLFPHLTVLQnltlapiwvrGMAKSEIEEIAMmylkrvripdqahkfpgQLSGGQQQRVAIARALCMRPEIMLF 165
Cdd:TIGR00957 732 QVLEACALLPDLEILP----------SGDRTEIGEKGV-----------------NLSGGQKQRVSLARAVYSNADIYLF 784
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 166 DEPTSALDPEMVKEVLDVMTELAG--EGMTMVCVTHEMGFARQVaDSIVFMAEGSIIESGSPAEFFE 230
Cdd:TIGR00957 785 DDPLSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
22-223 |
7.52e-16 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 73.45 E-value: 7.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQ--TGHIVVDGIELTddvKAVEKIRRKVGMVFQNFNLFPHLT 98
Cdd:cd03233 23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALaNRTEGNVsvEGDIHYNGIPYK---EFAEKYPGEIIYVSEEDVHFPTLT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLApiwvrgmAKSeieeiammylkrvripdQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVK 178
Cdd:cd03233 100 VRETLDFA-------LRC-----------------KGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2504588632 179 EVLDVMTELAGE-GMT-MVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:cd03233 156 EILKCIRTMADVlKTTtFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-234 |
1.45e-15 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 75.97 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTddVKAVEKIRRKVGMVFQNFNLFPHlTVLQ 101
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG--AYGLRELRRQFSMIPQDPVLFDG-TVRQ 1402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NL------TLAPIW-------VRGMAKSEIEEIammylkRVRIPDQAHKFpgqlSGGQQQRVAIARALCMRPE-IMLFDE 167
Cdd:PTZ00243 1403 NVdpfleaSSAEVWaalelvgLRERVASESEGI------DSRVLEGGSNY----SVGQRQLMCMARALLKKGSgFILMDE 1472
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 168 PTSALDPEMVKEV-LDVMTelAGEGMTMVCVTHEMGFARQVaDSIVFMAEGSIIESGSPAEFFENPKS 234
Cdd:PTZ00243 1473 ATANIDPALDRQIqATVMS--AFSAYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSPRELVMNRQS 1537
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-230 |
2.35e-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: 75.37 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMVFQNFNLFP-----H 96
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAK--IGLHDLRFKITIIPQDPVLFSgslrmN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 LTVLQNLTLAPIWvrgMAKseieEIAMMYLKRVRIPD----QAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:TIGR00957 1380 LDPFSQYSDEEVW---WAL----ELAHLKTFVSALPDkldhECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAV 1452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 173 DPEmVKEVLDVMTELAGEGMTMVCVTHE----MGFARqvadsIVFMAEGSIIESGSPAEFFE 230
Cdd:TIGR00957 1453 DLE-TDNLIQSTIRTQFEDCTVLTIAHRlntiMDYTR-----VIVLDKGEVAEFGAPSNLLQ 1508
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-221 |
3.23e-15 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 74.24 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVgkwynSYH------ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkAVEKI 80
Cdd:PRK10522 323 LELRNV-----TFAyqdngfSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAE--QPEDY 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 RRKVGMVFQNFNLFPHLTVLQNLT----LAPIWVR--GMA-KSEIEEIAMMYLKrvripdqahkfpgqLSGGQQQRVAIA 153
Cdd:PRK10522 396 RKLFSAVFTDFHLFDQLLGPEGKPanpaLVEKWLErlKMAhKLELEDGRISNLK--------------LSKGQKKRLALL 461
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 154 RALCMRPEIMLFDEPTSALDP----EMVKEVLDVMTELageGMTMVCVTHEMGFARQvADSIVFMAEGSIIE 221
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPhfrrEFYQVLLPLLQEM---GKTIFAISHDDHYFIH-ADRLLEMRNGQLSE 529
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-232 |
8.34e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.53 E-value: 8.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNsyhALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCIN-------RLEAHQtghIVVDGIELtddVKA 76
Cdd:PRK15093 8 NLTIEFKTSDGWVK---AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICgvtkdnwRVTADR---MRFDDIDL---LRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 77 VEKIRRK-----VGMVFQNFN--LFPHLTVLQNLTLA-PIWV-RGMAKSEI---EEIAMMYLKRVRIPDQA---HKFPGQ 141
Cdd:PRK15093 79 SPRERRKlvghnVSMIFQEPQscLDPSERVGRQLMQNiPGWTyKGRWWQRFgwrKRRAIELLHRVGIKDHKdamRSFPYE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 142 LSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTEL-AGEGMTMVCVTHEMGFARQVADSIVFMAEGSII 220
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
250
....*....|..
gi 2504588632 221 ESGSPAEFFENP 232
Cdd:PRK15093 239 ETAPSKELVTTP 250
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-240 |
1.05e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 71.40 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCinrLEAHQTGHIVVDGIELTDDVK----------AVEKIRRKVGMVFQNF 91
Cdd:PRK13547 17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKA---LAGDLTGGGAPRGARVTGDVTlngeplaaidAPRLARLRAVLPQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 92 NLFPhLTVLQNLTLA--PIWVRGMAKS-EIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCM---------R 159
Cdd:PRK13547 94 PAFA-FSAREIVLLGryPHARRAGALThRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaqP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 160 PEIMLFDEPTSALDPEMVKEVLDVMTELAGE-GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENPKSERTR 238
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLTPAHIARCY 252
|
..
gi 2504588632 239 QF 240
Cdd:PRK13547 253 GF 254
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
20-223 |
1.12e-14 |
|
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: 69.66 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTmircinrleahqtghIVVDGIEltddvkavEKIRRKVGMVFQNFnlFPHLTV 99
Cdd:cd03238 9 HNLQNLDVSIPLNVLVVVTGVSGSGKST---------------LVNEGLY--------ASGKARLISFLPKF--SRNKLI 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 ----LQNLTlapiwvrgmakseieEIAMMYLKrvriPDQAhkfPGQLSGGQQQRVAIARALCMRPE--IMLFDEPTSALD 173
Cdd:cd03238 64 fidqLQFLI---------------DVGLGYLT----LGQK---LSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLH 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2504588632 174 PEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESG 223
Cdd:cd03238 122 QQDINQLLEVIKGLIDLGNTVILIEHNLDVLSS-ADWIIDFGPGSGKSGG 170
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-220 |
3.59e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 71.30 E-value: 3.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 9 LRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELtDDVKAVEKIRRKVGMVF 88
Cdd:PRK10982 1 MSNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEI-DFKSSKEALENGISMVH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 89 QNFNLFPHLTVLQNLTLAPIWVRGMAKSEieeiAMMYLKRVRIPDQ------AHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK10982 80 QELNLVLQRSVMDNMWLGRYPTKGMFVDQ----DKMYRDTKAIFDEldididPRAKVATLSVSQMQMIEIAKAFSYNAKI 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 163 MLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSII 220
Cdd:PRK10982 156 VIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-231 |
4.44e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.31 E-value: 4.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRC-INRLEAHQTGHIVvdgieltddvkavekIRRKVGMVFQNFNLFpHLT 98
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAmLGELPPRSDASVV---------------IRGTVAYVPQVSWIF-NAT 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLApiwvrgmakSEIEeiAMMYLKRVRIPDQAHKF---PG-----------QLSGGQQQRVAIARALCMRPEIML 164
Cdd:PLN03130 695 VRDNILFG---------SPFD--PERYERAIDVTALQHDLdllPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYI 763
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVaDSIVFMAEGSIIESGSPAEFFEN 231
Cdd:PLN03130 764 FDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN 829
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
7-221 |
6.31e-14 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 70.60 E-value: 6.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGkwYnSYHALRD--------VSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvkAVE 78
Cdd:COG4615 328 LELRGVT--Y-RYPGEDGdegftlgpIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD--NRE 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKVGMVFQNFNLFPHLTvlqnltlapiwvrGMAKSEIEEIAMMYLKRVRIpdqAHK--FPG------QLSGGQQQRV 150
Cdd:COG4615 403 AYRQLFSAVFSDFHLFDRLL-------------GLDGEADPARARELLERLEL---DHKvsVEDgrfsttDLSQGQRKRL 466
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 151 A-IARALCMRPeIMLFDEPTSALDPEMVK----EVLdvmTELAGEGMTMVCVTH-EMGFarQVADSIVFMAEGSIIE 221
Cdd:COG4615 467 AlLVALLEDRP-ILVFDEWAADQDPEFRRvfytELL---PELKARGKTVIAISHdDRYF--DLADRVLKMDYGKLVE 537
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
25-219 |
2.63e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 25 VSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDvKAVEKIRRkvGMVF-----QNFNLFPHLTV 99
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIR-SPRDAIRA--GIMLcpedrKAEGIIPVHSV 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQNLT-------------LAPIWVRGMAKSEIEEIammylkRVRIPDqAHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:PRK11288 349 ADNINisarrhhlragclINNRWEAENADRFIRSL------NIKTPS-REQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHE----MGfarqVADSIVFMAEGSI 219
Cdd:PRK11288 422 EPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlpevLG----VADRIVVMREGRI 474
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-218 |
3.32e-13 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 68.89 E-value: 3.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWY--NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvkavEKIRRK 83
Cdd:TIGR01257 1937 ILRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAG----------KSILTN 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNLTLAP------IWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALC 157
Cdd:TIGR01257 2007 ISDVHQNMGYCPQFDAIDDLLTGRehlylyARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALI 2086
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGS 218
Cdd:TIGR01257 2087 GCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGA 2147
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-238 |
5.48e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.08 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMVFQNFNLFPHlTVLQ 101
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAK--FGLTDLRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NL------TLAPIWvRGMAKSEIEEIammyLKRVRIPDQAHKFPG--QLSGGQQQRVAIARALCMRPEIMLFDEPTSALD 173
Cdd:PLN03232 1329 NIdpfsehNDADLW-EALERAHIKDV----IDRNPFGLDAEVSEGgeNFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2504588632 174 PEMVKEVLDVMTElAGEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFENPKSERTR 238
Cdd:PLN03232 1404 VRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFFR 1466
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-174 |
6.72e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 68.01 E-value: 6.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLeAHQTGHIVVDGIELtdDVKAVEKIRRKVGMVFQNFNLFPHlTVLQ 101
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSW--NSVTLQTWRKAFGVIPQKVFIFSG-TFRK 1310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTLAPIWvrgmAKSEIEEIAmmylKRVRIPDQAHKFPGQL-----------SGGQQQRVAIARALCMRPEIMLFDEPTS 170
Cdd:TIGR01271 1311 NLDPYEQW----SDEEIWKVA----EEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPSA 1382
|
....
gi 2504588632 171 ALDP 174
Cdd:TIGR01271 1383 HLDP 1386
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-230 |
1.28e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.88 E-value: 1.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIvvdgiELTDDVKavekirrk 83
Cdd:TIGR03719 320 DKVIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-----EIGETVK-------- 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNF-NLFPHLTVlqnltlapiWvrgmakseiEEIA----MMYLKRVRIPDQAH------------KFPGQLSGGQ 146
Cdd:TIGR03719 387 LAYVDQSRdALDPNKTV---------W---------EEISggldIIKLGKREIPSRAYvgrfnfkgsdqqKKVGQLSGGE 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 147 QQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGegmTMVCVTHEMGFARQVADSIvfMAegsiIESGSPA 226
Cdd:TIGR03719 449 RNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNFAG---CAVVISHDRWFLDRIATHI--LA----FEGDSHV 519
|
....
gi 2504588632 227 EFFE 230
Cdd:TIGR03719 520 EWFE 523
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
22-230 |
1.34e-12 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 66.67 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekIRRKVGMVFQN-----FNLFPH 96
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV--LRQGVAMVQQDpvvlaDTFLAN 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 LTVLQNLTLAPIWvrgmakSEIEEIAMMYLKRvRIPDQAHKFPGQ----LSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:PRK10790 435 VTLGRDISEEQVW------QALETVQLAELAR-SLPDGLYTPLGEqgnnLSVGQKQLLALARVLVQTPQILILDEATANI 507
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 173 DPEMVKEVLDVMTELAgEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFE 230
Cdd:PRK10790 508 DSGTEQAIQQALAAVR-EHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLA 563
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-228 |
1.65e-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: 65.12 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 28 SIGKGEKVVVCGPSGSGKSTMIRCInrleahqTGHIVVDGIELTDDVKAV----EKIRRKVGMVFQNFnLFphlTVLQNL 103
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKML-------AGVLKPDEGDIEIELDTVsykpQYIKADYEGTVRDL-LS---SITKDF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 104 TLAPIWvrgmaKSEIeeiaMMYLKRVRIPDQahKFPgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPE---MVKEV 180
Cdd:cd03237 90 YTHPYF-----KTEI----AKPLQIEQILDR--EVP-ELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEqrlMASKV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2504588632 181 LDVMTELAGEgmTMVCVTHEMGFARQVADS-IVFmaegsiieSGSPAEF 228
Cdd:cd03237 158 IRRFAENNEK--TAFVVEHDIIMIDYLADRlIVF--------EGEPSVN 196
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
21-217 |
1.91e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 66.29 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 21 ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELtDDVKAVEKIRRKVGMVFQ---NFNLFPHL 97
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKI-NNHNANEAINHGFALVTEerrSTGIYAYL 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNLTLAPI--WVRGMA-------KSEIEEI--AMmylkRVRIPDQaHKFPGQLSGGQQQRVAIARALCMRPEIMLFD 166
Cdd:PRK10982 342 DIGFNSLISNIrnYKNKVGlldnsrmKSDTQWVidSM----RVKTPGH-RTQIGSLSGGNQQKVIIGRWLLTQPEILMLD 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEG 217
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
22-229 |
4.83e-12 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 63.77 E-value: 4.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvKAVEKIRRKVGMVFQN---------FN 92
Cdd:cd03288 37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISK--LPLHTLRSRLSIILQDpilfsgsirFN 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 93 LFPHLTVlqnlTLAPIWvrgmaksEIEEIAMMYLKRVRIP---DQAHKFPGQ-LSGGQQQRVAIARALCMRPEIMLFDEP 168
Cdd:cd03288 115 LDPECKC----TDDRLW-------EALEIAQLKNMVKSLPgglDAVVTEGGEnFSVGQRQLFCLARAFVRKSSILIMDEA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 169 TSALDpeMVKE-VLD--VMTELAGEgmTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFF 229
Cdd:cd03288 184 TASID--MATEnILQkvVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLL 242
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-227 |
7.24e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 7.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDdvkavEKIRRKVG 85
Cdd:NF033858 1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD-----ARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 -----MVfQNF--NLFPHLTVLQNL----TLapiwvRGMAKSEieeiammylKRVRIPD--QA---HKFP----GQLSGG 145
Cdd:NF033858 76 priayMP-QGLgkNLYPTLSVFENLdffgRL-----FGQDAAE---------RRRRIDEllRAtglAPFAdrpaGKLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 146 QQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE--GMTMVCVTHEMGFARQVaDSIVFMAEGSIIESG 223
Cdd:NF033858 141 MKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVLATG 219
|
....
gi 2504588632 224 SPAE 227
Cdd:NF033858 220 TPAE 223
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
111-228 |
8.14e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 63.99 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 111 RGMAKSEIEEIammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGE 190
Cdd:NF000106 118 RKDARARADEL----LERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD 193
|
90 100 110
....*....|....*....|....*....|....*...
gi 2504588632 191 GMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEF 228
Cdd:NF000106 194 GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
20-225 |
8.29e-12 |
|
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: 63.40 E-value: 8.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMI---------RCINRLEAHQTGHIVVDGIELTDDV---------------- 74
Cdd:cd03271 9 NNLKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalaRRLHLKKEQPGNHDRIEGLEHIDKVividqspigrtprsnp 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 75 ----KAVEKIRRkvgmVF------QNFNlfphltvlqNLTLApiwVRGMAKSeIEEIAMMYLKRVR-----IPDQAHKFP 139
Cdd:cd03271 89 atytGVFDEIRE----LFcevckgKRYN---------RETLE---VRYKGKS-IADVLDMTVEEALeffenIPKIARKLQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 140 ------------GQ----LSGGQQQRVAIARALCMR---PEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHE 200
Cdd:cd03271 152 tlcdvglgyiklGQpattLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
250 260 270
....*....|....*....|....*....|.
gi 2504588632 201 MGFARqVADSIVFM------AEGSIIESGSP 225
Cdd:cd03271 232 LDVIK-CADWIIDLgpeggdGGGQVVASGTP 261
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-244 |
8.74e-12 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 64.74 E-value: 8.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRlEAHQ-----TGHIVVDGIELTDDVKaveKIRRKVGMVFQNFNLFPH 96
Cdd:TIGR00956 77 LKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS-NTDGfhigvEGVITYDGITPEEIKK---HYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 LTVLQNLTLAP----IWVRGM-------AKSEIEEIAMMY-LKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIML 164
Cdd:TIGR00956 153 LTVGETLDFAArcktPQNRPDgvsreeyAKHIADVYMATYgLSHTRNTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 165 FDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVThemgfARQVA-------DSIVFMAEGSIIESGS---PAEFFEN--- 231
Cdd:TIGR00956 233 WDNATRGLDSATALEFIRALKTSANILDTTPLVA-----IYQCSqdayelfDKVIVLYEGYQIYFGPadkAKQYFEKmgf 307
|
250
....*....|....*
gi 2504588632 232 --PKSERTRQFLGQI 244
Cdd:TIGR00956 308 kcPDRQTTADFLTSL 322
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-208 |
1.71e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 63.21 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 6 IIELRKVGKWYNS-YHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVV-DGIeltddvkavekirrK 83
Cdd:PRK11819 6 IYTMNRVSKVVPPkKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPGI--------------K 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNFNLFPHLTVLQNLT--LAPIWVrgmAKSEIEEIAMMY----------LKR----------------------- 128
Cdd:PRK11819 72 VGYLPQEPQLDPEKTVRENVEegVAEVKA---ALDRFNEIYAAYaepdadfdalAAEqgelqeiidaadawdldsqleia 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 129 ---VRIPDQAHKFpGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGegmTMVCVTHEMGFAR 205
Cdd:PRK11819 149 mdaLRCPPWDAKV-TKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFLHDYPG---TVVAVTHDRYFLD 224
|
...
gi 2504588632 206 QVA 208
Cdd:PRK11819 225 NVA 227
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
22-232 |
1.71e-11 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 63.64 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDgieltddvkavekirRKVGMVfqnfnlfPHLTVLQ 101
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE---------------RSIAYV-------PQQAWIM 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTlapiwVRGMAKSEIEEIAMMYLKRVRI----PDQAHKFPG----------QLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:PTZ00243 734 NAT-----VRGNILFFDEEDAARLADAVRVsqleADLAQLGGGleteigekgvNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2504588632 168 PTSALDPE----MVKEVLdvMTELAGEgmTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFENP 232
Cdd:PTZ00243 809 PLSALDAHvgerVVEECF--LGALAGK--TRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSADFMRTS 872
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
23-226 |
2.18e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 23 RDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKaveKIRRKVGMVF-----QNFNLFPHL 97
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST---AQRLARGLVYlpedrQSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQN---LT--LAPIWVRGMAKSEIEEiamMYLKRVRI----PDQAHKfpgQLSGGQQQRVAIARALCMRPEIMLFDEP 168
Cdd:PRK15439 357 PLAWNvcaLThnRRGFWIKPARENAVLE---RYRRALNIkfnhAEQAAR---TLSGGNQQKVLIAKCLEASPQLLIVDEP 430
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 169 TSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIieSGSPA 226
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI--SGALT 486
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
22-174 |
3.57e-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: 61.79 E-value: 3.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLeAHQTGHIVVDGIELtdDVKAVEKIRRKVGMVFQNFNLFPHlTVLQ 101
Cdd:cd03289 20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRL-LNTEGDIQIDGVSW--NSVPLQKWRKAFGVIPQKVFIFSG-TFRK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTLAPIWvrgmAKSEIEEIAmmylKRVRIPDQAHKFPGQL-----------SGGQQQRVAIARALCMRPEIMLFDEPTS 170
Cdd:cd03289 96 NLDPYGKW----SDEEIWKVA----EEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSA 167
|
....
gi 2504588632 171 ALDP 174
Cdd:cd03289 168 HLDP 171
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
29-199 |
4.61e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.63 E-value: 4.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 29 IGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAvekirRKVGMVFQNFNLFPHLTVLQNLTlapi 108
Cdd:PRK13543 34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRS-----RFMAYLGHLPGLKADLSTLENLH---- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 109 WVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMT-EL 187
Cdd:PRK13543 105 FLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISaHL 184
|
170
....*....|..
gi 2504588632 188 AGEGMTMVcVTH 199
Cdd:PRK13543 185 RGGGAALV-TTH 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-213 |
6.69e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.97 E-value: 6.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 23 RDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIR----RKVGM------------ 86
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEHTNDMTNEQDYQgdeeQNVGMknvnefsltkeg 1264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 -------VFQN----------------------FNLFPHLTVLQNLTLAPIWVRGMAKSEIEEIAMMyLKRVRIPDQAHK 137
Cdd:PTZ00265 1265 gsgedstVFKNsgkilldgvdicdynlkdlrnlFSIVSQEPMLFNMSIYENIKFGKEDATREDVKRA-CKFAAIDEFIES 1343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 138 FPGQ-----------LSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEG-MTMVCVTHEMGFAR 205
Cdd:PTZ00265 1344 LPNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRIASIK 1423
|
....*...
gi 2504588632 206 QVADSIVF 213
Cdd:PTZ00265 1424 RSDKIVVF 1431
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
18-212 |
9.03e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.50 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 18 SYHALRD-VSLSIGKGEKVVVCGPSGSGKSTMIRCIN-------------------RLEA----HQTGHI---VVDGI-E 69
Cdd:PRK11147 14 SDAPLLDnAELHIEDNERVCLVGRNGAGKSTLMKILNgevllddgriiyeqdlivaRLQQdpprNVEGTVydfVAEGIeE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 70 LTDDVKAVEKIRRKVGMVFQNFNLfPHLTVLQN-LTLAPIWvrgMAKSEIEEIammyLKRVRIPdqAHKFPGQLSGGQQQ 148
Cdd:PRK11147 94 QAEYLKRYHDISHLVETDPSEKNL-NELAKLQEqLDHHNLW---QLENRINEV----LAQLGLD--PDAALSSLSGGWLR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 149 RVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGegmTMVCVTHEMGFARQVADSIV 212
Cdd:PRK11147 164 KAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG---SIIFISHDRSFIRNMATRIV 224
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
23-204 |
9.26e-11 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 59.43 E-value: 9.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 23 RDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELtddvkavekirRKVGMVFqNFNLF-------- 94
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI-----------RRQRDEY-HQDLLylghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 95 -PHLTVLQNLTlapiWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALD 173
Cdd:PRK13538 86 kTELTALENLR----FYQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180 190
....*....|....*....|....*....|..
gi 2504588632 174 PEMVKEVLDVMTE-LAGEGMTMVCVTHEMGFA 204
Cdd:PRK13538 162 KQGVARLEALLAQhAEQGGMVILTTHQDLPVA 193
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
23-205 |
1.06e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 61.20 E-value: 1.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 23 RDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKaVEKIRRKVGMVFQNFNLFPH------ 96
Cdd:PTZ00265 402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDIN-LKWWRSKIGVVSQDPLLFSNsiknni 480
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 ---LTVLQNLTLAP-----------------------------IWVRGMAKSEIEEIAMMY-----------LKRVRIPD 133
Cdd:PTZ00265 481 kysLYSLKDLEALSnyynedgndsqenknkrnscrakcagdlnDMSNTTDSNELIEMRKNYqtikdsevvdvSKKVLIHD 560
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 134 QAHKFP-----------GQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAG-EGMTMVCVTHEM 201
Cdd:PTZ00265 561 FVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIAHRL 640
|
....
gi 2504588632 202 GFAR 205
Cdd:PTZ00265 641 STIR 644
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-224 |
1.54e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 59.66 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 1 MTENAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQ--TGHIVVDGIELTdDVKAVE 78
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKilEGDILFKGESIL-DLEPEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 79 KIRRKVGMVFQNFNLFPHLTVLQNLTLAPIWVR-GMAKSEIEEIAMMYL--KRVRIPDQAHKFPGQ-----LSGGQQQRV 150
Cdd:CHL00131 81 RAHLGIFLAFQYPIEIPGVSNADFLRLAYNSKRkFQGLPELDPLEFLEIinEKLKLVGMDPSFLSRnvnegFSGGEKKRN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 151 AIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHemgFARQ----VADSIVFMAEGSIIESGS 224
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH---YQRLldyiKPDYVHVMQNGKIIKTGD 235
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
39-216 |
3.90e-10 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 59.74 E-value: 3.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 39 GPSGSGKSTMIRCinrLEAHQTGHIVVDGIELTDDVKAVEKIRRKVGMVFQNFNLFPHLTVLQNLTLAPiWVRGMAKSEI 118
Cdd:TIGR00956 796 GASGAGKTTLLNV---LAERVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTSTVRESLRFSA-YLRQPKSVSK 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 119 EEiAMMYLKRV-------RIPDQAHKFPGQ-LSGGQQQRVAIARALCMRPEIMLF-DEPTSALDPEMVKEVLDVMTELAG 189
Cdd:TIGR00956 872 SE-KMEYVEEVikllemeSYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLLLFlDEPTSGLDSQTAWSICKLMRKLAD 950
|
170 180
....*....|....*....|....*..
gi 2504588632 190 EGMTMVCVTHEmgfarqvaDSIVFMAE 216
Cdd:TIGR00956 951 HGQAILCTIHQ--------PSAILFEE 969
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
15-218 |
4.56e-10 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 57.73 E-value: 4.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 15 WYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCInrLEAHQT--GHIVVDGIELTDDVKAVEKIRRK--VGMVFQN 90
Cdd:cd03290 10 WGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAI--LGEMQTleGKVHWSNKNESEPSFEATRSRNRysVAYAAQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 91 FNLFpHLTVLQNLTLAPIWVRGMAKSEIEEIAMMY-LKRVRIPDQAH--KFPGQLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:cd03290 88 PWLL-NATVEENITFGSPFNKQRYKAVTDACSLQPdIDLLPFGDQTEigERGINLSGGQRQRICVARALYQNTNIVFLDD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 168 PTSALDPEMVKEVLD--VMTELAGEGMTMVCVTHEMGFARQvADSIVFMAEGS 218
Cdd:cd03290 167 PFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPH-ADWIIAMKDGS 218
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
8-200 |
6.96e-10 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 59.09 E-value: 6.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 8 ELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIrciNRLEAHQTGHIVVDGIELTDDVKAVEKIRRKVGMV 87
Cdd:PLN03140 882 EMKEQGVTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLM---DVLAGRKTGGYIEGDIRISGFPKKQETFARISGYC 958
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 88 FQNFNLFPHLTVLQNLTLAPiWVRgMAKSEIEEIAMMYLKRV-------RIPDQAHKFPG--QLSGGQQQRVAIARALCM 158
Cdd:PLN03140 959 EQNDIHSPQVTVRESLIYSA-FLR-LPKEVSKEEKMMFVDEVmelveldNLKDAIVGLPGvtGLSTEQRKRLTIAVELVA 1036
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2504588632 159 RPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHE 200
Cdd:PLN03140 1037 NPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQ 1078
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
19-241 |
7.94e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.36 E-value: 7.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 19 YH-ALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvkavekirrKVGMVFQNFNLFPHL 97
Cdd:PRK13545 36 YHyALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG---------------SAALIAISSGLNGQL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 98 TVLQNLTLAPIwVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMV 177
Cdd:PRK13545 101 TGIENIELKGL-MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFT 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 178 KEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESGSPAEFFENpkserTRQFL 241
Cdd:PRK13545 180 KKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH-----YDEFL 238
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-227 |
9.16e-10 |
|
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: 58.49 E-value: 9.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI------NRLE-AHQT--GHIVVDGIELTDDV---------------- 74
Cdd:TIGR00630 622 NNLKNITVSIPLGLFTCITGVSGSGKSTLINDTlypalaNRLNgAKTVpgRYTSIEGLEHLDKVihidqspigrtprsnp 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 75 ----KAVEKIR---------RKVGMVFQNF----------------------NLFPHLTVLQNL---------TLApiwV 110
Cdd:TIGR00630 702 atytGVFDEIRelfaetpeaKVRGYTPGRFsfnvkggrceacqgdgvikiemHFLPDVYVPCEVckgkrynreTLE---V 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 111 RGMAKSeIEEIAMMYLKRVR-----IPDQAHKFP------------GQ----LSGGQQQRVAIARALCMR---PEIMLFD 166
Cdd:TIGR00630 779 KYKGKN-IADVLDMTVEEAYeffeaVPSISRKLQtlcdvglgyirlGQpattLSGGEAQRIKLAKELSKRstgRTLYILD 857
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 167 EPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQvADSIVFM------AEGSIIESGSPAE 227
Cdd:TIGR00630 858 EPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKT-ADYIIDLgpeggdGGGTVVASGTPEE 923
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
22-220 |
1.23e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGkstmircinRLE-----------AHQTGHIVVDGIELtdDVKAVEKI---------- 80
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAG---------RTElamsvfgrsygRNISGTVFKDGKEV--DVSTVSDAidaglayvte 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 81 -RRKVGMVFQNfnlfphlTVLQNLTLAPIwvRGMAK----SEIEEI--AMMYLKRVRIpdqahKFP------GQLSGGQQ 147
Cdd:NF040905 345 dRKGYGLNLID-------DIKRNITLANL--GKVSRrgviDENEEIkvAEEYRKKMNI-----KTPsvfqkvGNLSGGNQ 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 148 QRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSII 220
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-203 |
1.23e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 57.72 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINrlEAHQTGHivvdgielTDDV----------KA 76
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLIT--GDHPQGY--------SNDLtlfgrrrgsgET 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 77 VEKIRRKVGMVFQNFnlfpHL-----TVLQNLTLA----PIWVRGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQ-LSGGQ 146
Cdd:PRK10938 331 IWDIKKHIGYVSSSL----HLdyrvsTSVRNVILSgffdSIGIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHsLSWGQ 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 147 QQRVAIARALCMRPEIMLFDEPTSALDP---EMVKEVLDVMTelaGEGMTMV------------CVTHEMGF 203
Cdd:PRK10938 407 QRLALIVRALVKHPTLLILDEPLQGLDPlnrQLVRRFVDVLI---SEGETQLlfvshhaedapaCITHRLEF 475
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
22-219 |
2.08e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 57.27 E-value: 2.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRC-INRLEAhQTGHIVVdGIELtdDVKAVEKIRRkvgmvfqnfNLFPHLTVL 100
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQA-DSGRIHC-GTKL--EVAYFDQHRA---------ELDPEKTVM 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 101 QNLtlapiwvrGMAKSEIE-----EIAMMYL-------KRVRIPDQAhkfpgqLSGGQQQRVAIARaLCMRP-EIMLFDE 167
Cdd:PRK11147 402 DNL--------AEGKQEVMvngrpRHVLGYLqdflfhpKRAMTPVKA------LSGGERNRLLLAR-LFLKPsNLLILDE 466
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 168 PTSALDPEMVkEVLDVMteLAGEGMTMVCVTHEMGFA-RQVADSIVFMAEGSI 219
Cdd:PRK11147 467 PTNDLDVETL-ELLEEL--LDSYQGTVLLVSHDRQFVdNTVTECWIFEGNGKI 516
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
140-241 |
2.52e-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: 57.10 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 140 GQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDpemVKE---VLDVMTELAGEGMTMVCVTHEMGFARQVADSIVfmae 216
Cdd:COG1245 211 SELSGGELQRVAIAAALLRDADFYFFDEPSSYLD---IYQrlnVARLIRELAEEGKYVLVVEHDLAILDYLADYVH---- 283
|
90 100
....*....|....*....|....*....
gi 2504588632 217 gsiIESGSPAEF--FENPKSERT--RQFL 241
Cdd:COG1245 284 ---ILYGEPGVYgvVSKPKSVRVgiNQYL 309
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-234 |
2.52e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 57.44 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIE-----LTDdvkavekIRRKVGMVFQNFNLFPH 96
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDiskfgLMD-------LRKVLGIIPQAPVLFSG 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 lTVLQNL------TLAPIWvrgmakseiEEIAMMYLKRV--RIPD--QAHKFPG--QLSGGQQQRVAIARALCMRPEIML 164
Cdd:PLN03130 1328 -TVRFNLdpfnehNDADLW---------ESLERAHLKDVirRNSLglDAEVSEAgeNFSVGQRQLLSLARALLRRSKILV 1397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 165 FDEPTSALDpemVKEVLDVMTELAGE--GMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEFFENPKS 234
Cdd:PLN03130 1398 LDEATAAVD---VRTDALIQKTIREEfkSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEGS 1465
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
20-223 |
2.64e-09 |
|
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: 55.73 E-value: 2.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMI----------RCINRLEA---HQTGHIVvdgielTDDVKAVEKIRRKVGM 86
Cdd:cd03270 9 HNLKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrRYVESLSAyarQFLGQMD------KPDVDSIEGLSPAIAI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 87 VFQNFNLFPHLTV-----LQNLtLAPIWVRGMAKSEIE---EIAMMYLKRVRIPdqahkfpGQLSGGQQQRVAIARALCM 158
Cdd:cd03270 83 DQKTTSRNPRSTVgtvteIYDY-LRLLFARVGIRERLGflvDVGLGYLTLSRSA-------PTLSGGEAQRIRLATQIGS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 159 RPE--IMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESG 223
Cdd:cd03270 155 GLTgvLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRA-ADHVIDIGPGAGVHGG 220
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
20-199 |
6.52e-09 |
|
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: 53.52 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKIrrkvgmvfqnfnlFPHLTV 99
Cdd:cd03227 9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGCIVAAVSA-------------ELIFTR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 100 LQnltlapiwvrgmakseieeiammylkrvripdqahkfpgqLSGGQQQRVAIARAL----CMRPEIMLFDEPTSALDPE 175
Cdd:cd03227 76 LQ----------------------------------------LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPR 115
|
170 180
....*....|....*....|....
gi 2504588632 176 MVKEVLDVMTELAGEGMTMVCVTH 199
Cdd:cd03227 116 DGQALAEAILEHLVKGAQVIVITH 139
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
132-238 |
7.07e-09 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 55.64 E-value: 7.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 132 PDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDpemVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSI 211
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD---LHAVLWLETYLLKWPKTFIVVSHAREFLNTVVTDI 411
|
90 100
....*....|....*....|....*..
gi 2504588632 212 VFMAEGSIIESGSPAEFFENPKSERTR 238
Cdd:PLN03073 412 LHLHGQKLVTYKGDYDTFERTREEQLK 438
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-223 |
7.31e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 54.82 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 17 NSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvkavekirrKVGMVFQNFNLFPH 96
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG---------------EVSVIAISAGLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 97 LTVLQNLTLAPIWVrGMAKSEIEEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEM 176
Cdd:PRK13546 100 LTGIENIEFKMLCM-GFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2504588632 177 VKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMAEGSIIESG 223
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYG 225
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
16-200 |
1.06e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 16 YNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVEKirrKVGMVFQNFNLFP 95
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQK---QLCFVGHRSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 96 HLTVLQNLTLAPIWVRGmaKSEIEEIammylkrVRIPDQAH--KFP-GQLSGGQQQRVAIARALCMRPEIMLFDEPTSAL 172
Cdd:PRK13540 88 YLTLRENCLYDIHFSPG--AVGITEL-------CRLFSLEHliDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*...
gi 2504588632 173 DPEMVKEVLDVMTELAGEGMTMVCVTHE 200
Cdd:PRK13540 159 DELSLLTIITKIQEHRAKGGAVLLTSHQ 186
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-213 |
1.19e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.81 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 29 IGKGEKVVVCGPSGSGKSTMIRCInrleahqTGHIVVDGIELTDDVKAVEK---IRRKVGMvfqnfnlfphlTVLQNL-T 104
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLL-------AGVLKPDEGEVDPELKISYKpqyIKPDYDG-----------TVEDLLrS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 105 LAPIWVRGMAKSEIeeiammyLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPE---MVKEVL 181
Cdd:PRK13409 424 ITDDLGSSYYKSEI-------IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAI 496
|
170 180 190
....*....|....*....|....*....|...
gi 2504588632 182 DVMTElaGEGMTMVCVTHEMGFARQVADS-IVF 213
Cdd:PRK13409 497 RRIAE--EREATALVVDHDIYMIDYISDRlMVF 527
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
31-213 |
1.51e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 52.38 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 31 KGEKVVVCGPSGSGKSTMIRCI-NRLEAHQTGHIVVDGieltddvkavekirrkvgmvfqnfnlfphltvlqnltlapiw 109
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDG------------------------------------------ 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 110 vrgmakseieEIAMMYLKRVRIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAG 189
Cdd:smart00382 39 ----------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLL 108
|
170 180 190
....*....|....*....|....*....|
gi 2504588632 190 EGM------TMVCVTHEMGFARQVADSIVF 213
Cdd:smart00382 109 LLLkseknlTVILTTNDEKDLGPALLRRRF 138
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-228 |
1.59e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.51 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 7 IELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRC-INRLEaHQTGHivvdgieltddVKAVEKIrrKVG 85
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGT-----------VKWSENA--NIG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 86 MVFQNfnlfpHLTVLQN-LTLAPiWVRGMAKSEIEEIAMM-YLKRVRIP-DQAHKFPGQLSGGQQQRVAIARALCMRPEI 162
Cdd:PRK15064 386 YYAQD-----HAYDFENdLTLFD-WMSQWRQEGDDEQAVRgTLGRLLFSqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNV 459
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 163 MLFDEPTSALDPEMVkEVLDVMTELAgEGmTMVCVTHEMGFARQVADSIVFMAEGSIIE-SGSPAEF 228
Cdd:PRK15064 460 LVMDEPTNHMDMESI-ESLNMALEKY-EG-TLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEEY 523
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-219 |
1.79e-08 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 54.41 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHI-VVDGIeltddvkavekirr 82
Cdd:PRK10636 310 NPLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIgLAKGI-------------- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 83 KVGMVFQN---FnLFPHLTVLQNLT-LAPiwvrgmakSEIEEIAMMYLKRVRIP-DQAHKFPGQLSGGQQQRVAIARALC 157
Cdd:PRK10636 376 KLGYFAQHqleF-LRADESPLQHLArLAP--------QELEQKLRDYLGGFGFQgDKVTEETRRFSGGEKARLVLALIVW 446
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2504588632 158 MRPEIMLFDEPTSALDPEMVKEVLDVMTELAGegmTMVCVTHEMGFARQVADSIVFMAEGSI 219
Cdd:PRK10636 447 QRPNLLLLDEPTNHLDLDMRQALTEALIDFEG---ALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
141-237 |
2.33e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.04 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 141 QLSGGQQQRVAIARALCMRPEIMLFDEPTSALDpemVKE---VLDVMTELAgEGMTMVCVTHEMGFARQVADSIVfmaeg 217
Cdd:PRK13409 212 ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD---IRQrlnVARLIRELA-EGKYVLVVEHDLAVLDYLADNVH----- 282
|
90 100
....*....|....*....|..
gi 2504588632 218 siIESGSPAEF--FENPKSERT 237
Cdd:PRK13409 283 --IAYGEPGAYgvVSKPKGVRV 302
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
22-218 |
2.63e-08 |
|
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: 53.32 E-value: 2.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQtGHIVVDG-IELTDDVKAVEKIRRKVGMVFQ-NFNLFPHLT 98
Cdd:cd03291 53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLIlGELEPSE-GKIKHSGrISFSSQFSWIMPGTIKENIIFGvSYDEYRYKS 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLApiwvrgmakseiEEIAmmylkrvRIPDQAHKFPGQ----LSGGQQQRVAIARALCMRPEIMLFDEPTSALDP 174
Cdd:cd03291 132 VVKACQLE------------EDIT-------KFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2504588632 175 EMVKEVLD--VMTELAGEgmTMVCVTHEMGFARQvADSIVFMAEGS 218
Cdd:cd03291 193 FTEKEIFEscVCKLMANK--TRILVTSKMEHLKK-ADKILILHEGS 235
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
141-236 |
2.84e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.14 E-value: 2.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 141 QLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQVADSIVFMaegsii 220
Cdd:cd03236 139 QLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCL------ 212
|
90
....*....|....*...
gi 2504588632 221 eSGSPAEF--FENPKSER 236
Cdd:cd03236 213 -YGEPGAYgvVTLPKSVR 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
110-236 |
4.51e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.42 E-value: 4.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 110 VRGMAKSEIEEIAMMYLKRVRIPDQAHKFpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAG 189
Cdd:cd03222 42 VKILAGQLIPNGDNDEWDGITPVYKPQYI--DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2504588632 190 EGM-TMVCVTHEMGFARQVADSI-VFMAEGSIIESGSPaeffenPKSER 236
Cdd:cd03222 120 EGKkTALVVEHDLAVLDYLSDRIhVFEGEPGVYGIASQ------PKGTR 162
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
24-199 |
6.54e-08 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 52.83 E-value: 6.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 24 DVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVDGieltddvkavekiRRKVGMVFQNfnlfPHLTV--LQ 101
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPA-------------KGKLFYVPQR----PYMTLgtLR 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 102 NLTLAPIWV-----RGMAKSEIEEIammyLKRVRIPDQAHKFPG---------QLSGGQQQRVAIARALCMRPEIMLFDE 167
Cdd:TIGR00954 533 DQIIYPDSSedmkrRGLSDKDLEQI----LDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDE 608
|
170 180 190
....*....|....*....|....*....|...
gi 2504588632 168 PTSALDPEMVkevlDVMTELAGE-GMTMVCVTH 199
Cdd:TIGR00954 609 CTSAVSVDVE----GYMYRLCREfGITLFSVSH 637
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
140-246 |
7.99e-08 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 52.77 E-value: 7.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 140 GQ----LSGGQQQRVAIARALCMRPE---IMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQvADSIV 212
Cdd:PRK00349 825 GQpattLSGGEAQRVKLAKELSKRSTgktLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHNLDVIKT-ADWII 903
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2504588632 213 FMA-E-----GSIIESGSPAEFFENPKSeRTRQFLGQILE 246
Cdd:PRK00349 904 DLGpEggdggGEIVATGTPEEVAKVEAS-YTGRYLKPVLE 942
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-213 |
1.49e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 51.71 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 28 SIGKGEKVVVCGPSGSGKSTMIRCInrleahqTGHIVVDGIELTDDVKAVEK---IRRKVGMvfqnfnlfphlTVLQNL- 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKIL-------AGVLKPDEGEVDEDLKISYKpqyISPDYDG-----------TVEEFLr 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 104 -TLAPIWVRGMAKSEIEE---IAMMYLKRVRipdqahkfpgQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPE---M 176
Cdd:COG1245 424 sANTDDFGSSYYKTEIIKplgLEKLLDKNVK----------DLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlA 493
|
170 180 190
....*....|....*....|....*....|....*...
gi 2504588632 177 VKEVLDVMTElaGEGMTMVCVTHEMGFARQVADSI-VF 213
Cdd:COG1245 494 VAKAIRRFAE--NRGKTAMVVDHDIYLIDYISDRLmVF 529
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
139-212 |
1.81e-07 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 49.91 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 139 PGQLSGGQQQ------RVAIARALCMRPEIMLFDEPTSALDPEMVKEVL-DVMTELAGEG-MTMVCVTHEMGFaRQVADS 210
Cdd:cd03240 113 RGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEERKSQKnFQLIVITHDEEL-VDAADH 191
|
..
gi 2504588632 211 IV 212
Cdd:cd03240 192 IY 193
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-243 |
2.17e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 51.37 E-value: 2.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 142 LSGGQQQRVAIARALcmRPEIM----LFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHE---MGFARQVAD----S 210
Cdd:PRK00635 477 LSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDeqmISLADRIIDigpgA 554
|
90 100 110
....*....|....*....|....*....|...
gi 2504588632 211 IVFmaEGSIIESGSPAEFFENPKSeRTRQFLGQ 243
Cdd:PRK00635 555 GIF--GGEVLFNGSPREFLAKSDS-LTAKYLRQ 584
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-242 |
3.01e-07 |
|
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: 51.06 E-value: 3.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGEKVVVCGPSGSGKSTMIRCI-NRLEAHQtGHIVVDG-IELTDDVKAVEKIRRKVGMVFQ-NFNLFPHLT 98
Cdd:TIGR01271 442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEPSE-GKIKHSGrISFSPQTSWIMPGTIKDNIIFGlSYDEYRYTS 520
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 99 VLQNLTLApiwvrgmakseiEEIAMMylkrvriPDQAHKFPGQ----LSGGQQQRVAIARALCMRPEIMLFDEPTSALDP 174
Cdd:TIGR01271 521 VIKACQLE------------EDIALF-------PEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 175 EMVKEVLDVMTELAGEGMTMVCVTHEMGFARQvADSIVFMAEGSIIESGSPAEfFENPKSERTRQFLG 242
Cdd:TIGR01271 582 VTEKEIFESCLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSE-LQAKRPDFSSLLLG 647
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-230 |
5.13e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.12 E-value: 5.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 4 NAIIELRKVGKWYNSYHALRDVSLSIGKGEKVVVCGPSGSGKSTMIRCINRLEAHQTGHIVVdGieltDDVKavekirrk 83
Cdd:PRK11819 322 DKVIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-G----ETVK-------- 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 84 VGMVFQNF-NLFPHLTVlqnltlapiWvrgmakseiEEIA----MMYLKRVRIP-------------DQaHKFPGQLSGG 145
Cdd:PRK11819 389 LAYVDQSRdALDPNKTV---------W---------EEISggldIIKVGNREIPsrayvgrfnfkggDQ-QKKVGVLSGG 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 146 QQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGegmTMVCVTHEMGFARQVADSIvfMA-EGSiiesgS 224
Cdd:PRK11819 450 ERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRALEEALLEFPG---CAVVISHDRWFLDRIATHI--LAfEGD-----S 519
|
....*.
gi 2504588632 225 PAEFFE 230
Cdd:PRK11819 520 QVEWFE 525
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
20-246 |
1.36e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.06 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTMIR-----CINRL-EAHQTGHIVVDG------IELTDD-------------V 74
Cdd:PRK00635 609 HNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtlvpAVEEFiEQGFCSNLSIQWgaisrlVHITRDlpgrsqrsipltyI 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 75 KAVEKIR---------RKVGMVFQNFNL------------FPHLTVLQNLTLAP-------------IWVRGMAKSeIEE 120
Cdd:PRK00635 689 KAFDDLRelfaeqprsKRLGLTKSHFSFntplgacaecqgLGSITTTDNRTSIPcpsclgkrflpqvLEVRYKGKN-IAD 767
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 121 IAMM--------YLKRVRIPDQAHKF------------P-GQLSGGQQQRVAIARALCM---RPEIMLFDEPTSALDPEM 176
Cdd:PRK00635 768 ILEMtayeaekfFLDEPSIHEKIHALcslgldylplgrPlSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHD 847
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2504588632 177 VKEVLDVMTELAGEGMTMVCVTHEMGFARqVADSIVFMAE------GSIIESGSPAEFF--ENPKSERTRQFLGQILE 246
Cdd:PRK00635 848 IKALIYVLQSLTHQGHTVVIIEHNMHVVK-VADYVLELGPeggnlgGYLLASCSPEELIhlHTPTAKALRPYLSSPQE 924
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
140-246 |
3.90e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.33 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 140 GQ----LSGGQQQRVAIARALCMRPE---IMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARqVADSIV 212
Cdd:COG0178 821 GQpattLSGGEAQRVKLASELSKRSTgktLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHNLDVIK-TADWII 899
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2504588632 213 FM------AEGSIIESGSPAEFFENPKSErTRQFLGQILE 246
Cdd:COG0178 900 DLgpeggdGGGEIVAEGTPEEVAKVKASY-TGRYLKEYLE 938
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-175 |
5.12e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 5.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 39 GPSGSGKSTMIRCINRLEAHQTGHIVVDGIELTDDVKAVekirrkVGMVFQNFNLFPHLTVLQNLTLapiWVRGMAKSEI 118
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY------CTYIGHNLGLKLEMTVFENLKF---WSEIYNSAET 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 2504588632 119 EEIAMMYLKrvrIPDQAHKFPGQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPE 175
Cdd:PRK13541 104 LYAAIHYFK---LHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
141-223 |
8.21e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.16 E-value: 8.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 141 QLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMG----FARQVAdsivFMAE 216
Cdd:PRK10938 135 YLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDeipdFVQFAG----VLAD 210
|
....*..
gi 2504588632 217 GSIIESG 223
Cdd:PRK10938 211 CTLAETG 217
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
115-235 |
1.01e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 115 KSEIEEIAMMY--LKRVRIPDQA--HKFPGQLSGGQQQR---------VAIARALCMRPE---IMLFDEPTSALDPEMVK 178
Cdd:PRK00635 1660 QTPIEEVAETFpfLKKIQKPLQAliDNGLGYLPLGQNLSslslsekiaIKIAKFLYLPPKhptLFLLDEIATSLDNQQKS 1739
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 179 EVLDVMTELAGEGMTMVCVTHEMGFARQvADSIVFMAEGS------IIESGSPAEFFENPKSE 235
Cdd:PRK00635 1740 ALLVQLRTLVSLGHSVIYIDHDPALLKQ-ADYLIEMGPGSgktggkILFSGPPKDISASKDSL 1801
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
139-199 |
1.94e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 44.69 E-value: 1.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 139 PGQLSGGQQQ---RVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTH 199
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PilT |
COG2805 |
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular ... |
35-64 |
3.74e-05 |
|
Type IV pilus assembly protein PilT, pilus retraction ATPase [Cell motility, Extracellular structures];
Pssm-ID: 442056 Cd Length: 342 Bit Score: 43.93 E-value: 3.74e-05
10 20 30
....*....|....*....|....*....|....
gi 2504588632 35 VVVCGPSGSGKST----MIRCINRleaHQTGHIV 64
Cdd:COG2805 128 VLVTGPTGSGKSTtlaaMIDYINE---TRAKHII 158
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
20-47 |
6.36e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 6.36e-05
10 20
....*....|....*....|....*...
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKST 47
Cdd:COG0178 14 HNLKNIDVDIPRNKLVVITGLSGSGKSS 41
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
143-239 |
6.76e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 6.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 143 SGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGegmTMVCVTHEMGFARQVADSIVFMAEGSIIES 222
Cdd:PRK10636 151 SGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG---TLILISHDRDFLDPIVDKIIHIEQQSLFEY 227
|
90
....*....|....*..
gi 2504588632 223 GSPAEFFENPKSERTRQ 239
Cdd:PRK10636 228 TGNYSSFEVQRATRLAQ 244
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
22-242 |
8.09e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.07 E-value: 8.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 22 LRDVSLSIGKGeKVVVCGPSGSGKSTMIRCINRL-------------------EAHQTGHIVV-----------DGIELT 71
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLlgpsssrkfdeedfylgddPDLPEIEIELtfgsllsrllrLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 72 DD---VKAVEKIRRKVGMVFQNFN-----LFPHLTVLQNLTLAPiwvrgmAKSEIEEIAMMYlkRVRIPDqAHKFP-GQL 142
Cdd:COG3593 93 DKeelEEALEELNEELKEALKALNellseYLKELLDGLDLELEL------SLDELEDLLKSL--SLRIED-GKELPlDRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 143 SGGQQQRVAIARALCM-------RPEIMLFDEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARQV-ADSIVFM 214
Cdd:COG3593 164 GSGFQRLILLALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVpLENIRRL 243
|
250 260
....*....|....*....|....*...
gi 2504588632 215 AEGSIIESGSPAEFFENPKSERTRQFLG 242
Cdd:COG3593 244 RRDSGGTTSTKLIDLDDEDLRKLLRYLG 271
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
142-195 |
8.89e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 43.31 E-value: 8.89e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2504588632 142 LSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTELAGeGMTMV 195
Cdd:PLN03073 628 LSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVLFQG-GVLMV 680
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
140-243 |
1.23e-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: 43.08 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 140 GQLSGGQQQRVAIARALCMRPEIMLF--DEPTSALDPEMVKEVLDVMTELAGEGMTMVCVTHEMGFARqVADSIVFMAEG 217
Cdd:TIGR00630 487 GTLSGGEAQRIRLATQIGSGLTGVLYvlDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIR-AADYVIDIGPG 565
|
90 100 110
....*....|....*....|....*....|..
gi 2504588632 218 S------IIESGSPAEFFENPKSeRTRQFLGQ 243
Cdd:TIGR00630 566 AgehggeVVASGTPEEILANPDS-LTGQYLSG 596
|
|
| PilT |
cd01131 |
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein ... |
35-69 |
4.99e-04 |
|
Pilus retraction ATPase PilT; Pilus retraction ATPase PilT is a nucleotide-binding protein responsible for the retraction of type IV pili, likely by pili disassembly. This retraction provides the force required for travel of bacteria in low water environments by a mechanism known as twitching motility.
Pssm-ID: 410875 [Multi-domain] Cd Length: 223 Bit Score: 40.21 E-value: 4.99e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2504588632 35 VVVCGPSGSGKST----MIRCINRleaHQTGHIVV--DGIE 69
Cdd:cd01131 24 VLVTGPTGSGKSTtlaaMIDYINE---TRSKHIITieDPIE 61
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
108-210 |
7.95e-04 |
|
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: 40.42 E-value: 7.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 108 IWVRGMAKSEIEEIAMMYLKRVRI----PDQAHKFPGQLSGGQQQ------RVAIARALCMRPEIMLFDEPTSALDPEMV 177
Cdd:TIGR00606 1162 IEIRSDADENVSASDKRRNYNYRVvmlkGDTALDMRGRCSAGQKVlasliiRLALAETFCLNCGIIALDEPTTNLDRENI 1241
|
90 100 110
....*....|....*....|....*....|....*...
gi 2504588632 178 KEVLDVMTEL-----AGEGMTMVCVTHEMGFARQVADS 210
Cdd:TIGR00606 1242 ESLAHALVEIiksrsQQRNFQLLVITHDEDFVELLGRS 1279
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
129-207 |
8.06e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 40.26 E-value: 8.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 129 VRIPDQAHKFP-GQLSGGQQQRVAIARALCMRPEIMLFDEPTSALDPEMVKEVLDVMTElagEGMTMVCVTHEMGFARQV 207
Cdd:PRK15064 142 VGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNE---RNSTMIIISHDRHFLNSV 218
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
20-48 |
1.59e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.61 E-value: 1.59e-03
10 20
....*....|....*....|....*....
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKSTM 48
Cdd:TIGR00630 10 HNLKNIDVEIPRDKLVVITGLSGSGKSSL 38
|
|
| SbcC_Walker_B |
pfam13558 |
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ... |
140-186 |
2.05e-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: 36.44 E-value: 2.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 140 GQLSGGQQQR---VAIARALCM----------RPEIMLFDEPTSALDPEMVKEVLDVMTE 186
Cdd:pfam13558 31 GGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
|
|
| Srp102 |
COG2229 |
Signal recognition particle receptor subunit beta, a GTPase [Intracellular trafficking, ... |
34-52 |
3.81e-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: 37.11 E-value: 3.81e-03
|
| ATPase_2 |
pfam01637 |
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ... |
8-106 |
4.53e-03 |
|
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.
Pssm-ID: 376582 [Multi-domain] Cd Length: 222 Bit Score: 37.30 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2504588632 8 ELRKVGKWYNSyhalrdvslsiGKGEKVVVCGPSGSGKSTMIR-CINRLEAHQTGHIVVD-----GIELTDDVKAVEKIR 81
Cdd:pfam01637 7 ELKELEEWAER-----------GPNLIYVIYGPEGCGKTALLReSIENLLDLGYYVIYYDplrryFISKLDRFEEVRRLA 75
|
90 100
....*....|....*....|....*
gi 2504588632 82 RKVGMVFQNFNLFPHLTVLQNLTLA 106
Cdd:pfam01637 76 EALGIAVPKAELEESKLAFLAIELL 100
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
19-83 |
4.93e-03 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 37.09 E-value: 4.93e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2504588632 19 YHALRDVSLSIGKGeKVVVCGPSGSGKSTMIRCI--------NRLEAHQTGHIVVDGIELTDDVKAVEKIRRK 83
Cdd:pfam13476 6 FRSFRDQTIDFSKG-LTLITGPNGSGKTTILDAIklalygktSRLKRKSGGGFVKGDIRIGLEGKGKAYVEIT 77
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
20-47 |
5.12e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 5.12e-03
10 20
....*....|....*....|....*...
gi 2504588632 20 HALRDVSLSIGKGEKVVVCGPSGSGKST 47
Cdd:PRK00349 14 HNLKNIDLDIPRDKLVVFTGLSGSGKSS 41
|
|
| YjeQ_EngC |
cd01854 |
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; ... |
31-63 |
8.82e-03 |
|
Ribosomal interacting GTPase YjeQ/EngC, a circularly permuted subfamily of the Ras GTPases; YjeQ (YloQ in Bacillus subtilis) is a ribosomal small subunit-dependent GTPase; hence also known as RsgA. YjeQ is a late-stage ribosomal biogenesis factor involved in the 30S subunit maturation, and it represents a protein family whose members are broadly conserved in bacteria and have been shown to be essential to the growth of E. coli and B. subtilis. Proteins of the YjeQ family contain all sequence motifs typical of the vast class of P-loop-containing GTPases, but show a circular permutation, with a G4-G1-G3 pattern of motifs as opposed to the regular G1-G3-G4 pattern seen in most GTPases. All YjeQ family proteins display a unique domain architecture, which includes an N-terminal OB-fold RNA-binding domain, the central permuted GTPase domain, and a zinc knuckle-like C-terminal cysteine domain.
Pssm-ID: 206747 [Multi-domain] Cd Length: 211 Bit Score: 36.22 E-value: 8.82e-03
10 20 30
....*....|....*....|....*....|....*.
gi 2504588632 31 KGEKVVVCGPSGSGKSTMircINRL--EAHQ-TGHI 63
Cdd:cd01854 84 KGKTSVLVGQSGVGKSTL---LNALlpELVLaTGEI 116
|
|
| COG4639 |
COG4639 |
Predicted kinase [General function prediction only]; |
35-85 |
9.92e-03 |
|
Predicted kinase [General function prediction only];
Pssm-ID: 443677 [Multi-domain] Cd Length: 145 Bit Score: 35.58 E-value: 9.92e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2504588632 35 VVVCGPSGSGKSTMIRcinrleAHQTGHIVVDgielTDDvkavekIRRKVG 85
Cdd:COG4639 5 VVLIGLPGSGKSTFAR------RLFAPTEVVS----SDD------IRALLG 39
|
|
| |
