|
Name |
Accession |
Description |
Interval |
E-value |
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-241 |
0e+00 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 505.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRK-LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVYLGHEFR 240
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGEDFR 239
|
.
gi 764533248 241 L 241
Cdd:COG1137 240 L 240
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-241 |
2.40e-165 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 455.97 E-value: 2.40e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGY 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 163 EPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVYLGHEFRL 241
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQFRL 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-236 |
6.37e-156 |
|
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: 431.97 E-value: 6.37e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYL 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRKDlDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVYLG 236
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-241 |
8.51e-132 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 371.53 E-value: 8.51e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVYLGHEFR 240
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFR 240
|
.
gi 764533248 241 L 241
Cdd:PRK10895 241 L 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-238 |
1.73e-78 |
|
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: 236.86 E-value: 1.73e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIM-------------AILETRKDLDRAGRHREL-ESLLQEFHISHIRDSLGMSLSGGERRRV 146
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLvaaharlgrgllaALLRLPRARREEREARERaEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLK-NKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEIL 225
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRdERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
250
....*....|...
gi 764533248 226 ANQLVKEVYLGHE 238
Cdd:COG0411 242 ADPRVIEAYLGEE 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-235 |
3.04e-75 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 227.64 E-value: 3.04e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARagIGYL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRkDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLvKEVYL 235
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL-EDVFL 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-230 |
4.45e-72 |
|
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: 219.62 E-value: 4.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYL 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIM--AILETRKDLDRAGRHREL-------ESLLQEFHISHIRDSLGMSLSGGERRRVEIARALAT 154
Cdd:cd03219 81 FQIPRLFPELTVLENVMvaAQARTGSGLLLARARREEreareraEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLV 230
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
1.57e-71 |
|
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: 218.31 E-value: 1.57e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKdlDRAGRHRELESL------LQEFhishiRDSLGMSLSGGERRRVEIARALAT 154
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARR--DRAEVRADLERVyelfprLKER-----RRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVY 234
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAY 233
|
..
gi 764533248 235 LG 236
Cdd:COG0410 234 LG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-227 |
2.01e-69 |
|
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: 212.29 E-value: 2.01e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYL 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRKdldRAGRHRELESLLQEFHISH-IRDSLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARR---RAKRKARLERVYELFPRLKeRRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 163 EPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-227 |
8.76e-68 |
|
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: 208.94 E-value: 8.76e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMhgRARAGIGYL 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRKDLDRAGRHReLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEELKKR-IEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-232 |
3.37e-60 |
|
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: 189.42 E-value: 3.37e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRA--RAG 79
Cdd:COG1127 4 PMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:COG1127 84 IGMLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEIL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 160 LLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA--NQLVKE 232
Cdd:COG1127 164 LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAsdDPWVRQ 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-215 |
4.86e-60 |
|
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: 186.83 E-value: 4.86e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMhgRARAGIGYL 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE--EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMailetrkdldragrhrelesllqefhishirdslgmsLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03230 79 PEEPSLYENLTVRENLK-------------------------------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-228 |
4.78e-58 |
|
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: 183.69 E-value: 4.78e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSY-KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGY 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLR-ELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQ--EASIFRKlSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG1122 80 VFQnpDDQLFAP-TVEEDVAFGPENLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-241 |
1.11e-57 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 184.93 E-value: 1.11e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDqqdvtHQPMHGRARAGIGY 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWD-----GEPLDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMAiLETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVY-LARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 163 EPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEIlanqlvKEVYLGHEFRL 241
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI------RRQFGRNTLRL 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
2.38e-56 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 179.90 E-value: 2.38e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVthqpmhGRARAGI 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFR--KLSVADNI-MAILETRKDLDRAGR--HRELESLLQEFHISHIRD-SLGmSLSGGERRRVEIARALAT 154
Cdd:COG1121 78 GYVPQRAEVDWdfPITVRDVVlMGRYGRRGLFRRPSRadREAVDEALERVGLEDLADrPIG-ELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGqLIAEGTAEEILANQLVKEVY 234
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAY 235
|
....*..
gi 764533248 235 lGHEFRL 241
Cdd:COG1121 236 -GGPVAL 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-240 |
5.36e-55 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 176.77 E-value: 5.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIGY 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMA---------ILETRKDLDRAgrhrelESLLQEFHISHIRDSLGMSLSGGERRRVEIARALA 153
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALgryphlglfGRPSAEDREAV------EEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKE 232
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEE 233
|
....*...
gi 764533248 233 VYlGHEFR 240
Cdd:COG1120 234 VY-GVEAR 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-232 |
7.76e-54 |
|
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: 173.07 E-value: 7.76e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTH--QPMHGRARAGIGYLP 84
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 85 QEASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 165 FAGVDPISVGDIKQIIHHLKN-KGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA--NQLVKE 232
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLVRQ 234
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
1.88e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 170.66 E-value: 1.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 161 LDEPFAGVDP---ISV-GDIKQIIHHLknkGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:COG3842 159 LDEPLSALDAklrEEMrEELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-219 |
4.86e-51 |
|
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: 165.39 E-value: 4.86e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGIGYL 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 164 PFAGVDPIS----VGDIKQIIHHLknkGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03259 157 PLSALDAKLreelREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-224 |
1.89e-50 |
|
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: 163.83 E-value: 1.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQ--VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgrARAGIG 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADN--IMAILetrKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:cd03263 79 YCPQFDALFDELTVREHlrFYARL---KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 160 LLDEPFAGVDPISVGDIKQIIHHLKnKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
4-227 |
3.40e-50 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 167.25 E-value: 3.40e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDV-THQPMHGRaraGIGY 82
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRP-PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 163 EPFAGVDPISVGDI-KQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG1118 159 EPFGALDAKVRKELrRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-219 |
4.80e-50 |
|
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: 162.45 E-value: 4.80e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDqqdvtHQPMHGRARAGIGYL 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFD-----GKPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETrKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-224 |
3.00e-49 |
|
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: 161.15 E-value: 3.00e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYL 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRKdldraGRHREL-ESLLQEFHISH-IRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALP-----RRSRKIpDEIYELFPVLKeMLGRRGGDLSGGQQQQLAIARALVTRPKLLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHLKN-KGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:TIGR03410 156 DEPTEGIQPSIIKDIGRVIRRLRAeGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-227 |
3.68e-49 |
|
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: 168.54 E-value: 3.68e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSR-----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRA- 76
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRe 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 -RAGIGYLPQ--EASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHIS-HIRDSLGMSLSGGERRRVEIARAL 152
Cdd:COG1123 340 lRRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARAL 419
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 153 ATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG1123 420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-219 |
4.80e-49 |
|
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: 160.08 E-value: 4.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmhgRARAGIGYL 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI---EALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMailetRKDLDRAGRHRELESLLQEFHISHIRD------SLGMslsggeRRRVEIARALATAPK 157
Cdd:cd03268 78 IEAPGFYPNLTARENLR-----LLARLLGIRKKRIDEVLDVVGLKDSAKkkvkgfSLGM------KQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 158 FILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-214 |
1.10e-48 |
|
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: 159.17 E-value: 1.10e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 8 HLAKSY--KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARaGIGYLPQ 85
Cdd:cd03225 4 NLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR-KVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 86 --EASIFrKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03225 83 npDDQFF-GPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQ 214
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-219 |
2.60e-48 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 158.08 E-value: 2.60e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 5 KAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThqpmhgRARAGIGYLP 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE------KERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 85 QEASIFRK--LSVADNIMAILETR----KDLDRAGRHRELEsLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:cd03235 75 QRRSIDRDfpISVRDVVLMGLYGHkglfRRLSKADKAKVDE-ALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNdGQLIAEG 219
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-199 |
6.81e-47 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 156.02 E-value: 6.81e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQ----VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThqpmhgRA 76
Cdd:COG1116 5 APALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT------GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 RAGIGYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAP 156
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRE 199
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDE 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-224 |
3.58e-46 |
|
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: 152.91 E-value: 3.58e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 6 AQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmhGRARAGIGYLPQ 85
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 86 EASIFRKLSVADNiMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:cd03265 81 DLSVDDELTGWEN-LYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 166 AGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-219 |
1.25e-45 |
|
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: 151.75 E-value: 1.25e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSY----KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMhgRARA 78
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA--EARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GIGYLPQEASIFRKLSVADNImAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-224 |
1.54e-45 |
|
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: 154.08 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 11 KSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARagIGYLPQEASIF 90
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRS--IGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 RKLSVADNIMAILETRkDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDP 170
Cdd:TIGR01188 79 EDLTGRENLEMMGRLY-GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 764533248 171 ISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-219 |
2.53e-45 |
|
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: 149.51 E-value: 2.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 5 KAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIGYLP 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 85 QeasifrklsvadnimailetrkdldragrhrelesLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd03214 80 Q-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 165 FAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-218 |
7.47e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 149.81 E-value: 7.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKS----RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpMHGRAR 77
Cdd:COG1136 3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISS--LSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AG-----IGYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARAL 152
Cdd:COG1136 81 ARlrrrhIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 153 ATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNvRETLDICETAYIVNDGQLIAE 218
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-214 |
1.19e-44 |
|
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: 147.72 E-value: 1.19e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVT-HQPMHGRARAGIGY 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTdLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMailetrkdldragrhrelesllqefhishirdslgMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIA-----------------------------------LGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 764533248 163 EPFAGVDPISVGDIKQIIHHLK-NKGIGVLITDHNVRETLDICETAYIVNDGQ 214
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQaQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-166 |
1.42e-44 |
|
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: 146.64 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGYLPQEASIFRKLSVADN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 99 IMAILETrKDLDRAGRHRELESLLQEFHISHIRDSL----GMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:pfam00005 80 LRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-195 |
2.73e-44 |
|
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: 147.63 E-value: 2.73e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARagIG 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNIMAILETRKdldRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYG---LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....*
gi 764533248 162 DEPFAGVDPISVGDIKQII-HHLKNKGIgVLITDH 195
Cdd:COG4133 156 DEPFTALDAAGVALLAELIaAHLARGGA-VLLTTH 189
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-199 |
5.49e-44 |
|
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: 147.23 E-value: 5.49e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQ----VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThqpmhgRARAG 79
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQG-VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 764533248 160 LLDEPFAGVDPISVGDIKQIIHHL--KNKGIGVLITdHNVRE 199
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIwrETGKTVLLVT-HDIDE 194
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
8.22e-44 |
|
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: 147.64 E-value: 8.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKS----RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAg 79
Cdd:COG1124 2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQ--EASIFRKLSVADnimAILETRKDLDRAGRHRELESLLQEFHI-SHIRDSLGMSLSGGERRRVEIARALATAP 156
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDR---ILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-214 |
1.76e-43 |
|
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: 143.92 E-value: 1.76e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 5 KAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGYLP 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 85 QeasifrklsvadnimailetrkdldragrhrelesllqefhishirdslgmsLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 764533248 165 FAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQ 214
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-224 |
2.15e-43 |
|
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: 146.33 E-value: 2.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAIlKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGI 80
Cdd:cd03296 1 MSI-EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKDLDR---AGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPK 157
Cdd:cd03296 77 GFVFQHYALFRHMTVFDNVAFGLRVKPRSERppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 158 FILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:cd03296 157 VLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
2-234 |
8.67e-43 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 145.20 E-value: 8.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKS-RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG--RARA 78
Cdd:COG3638 1 PMLELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GIGYLPQEASIFRKLSVADNIMAiletrkdlDRAGRHRELESLLQEFHISHIR------DSLGMS---------LSGGER 143
Cdd:COG3638 81 RIGMIFQQFNLVPRLSVLTNVLA--------GRLGRTSTWRSLLGLFPPEDREralealERVGLAdkayqradqLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 144 RRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAE 222
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
250
....*....|..
gi 764533248 223 EiLANQLVKEVY 234
Cdd:COG3638 233 E-LTDAVLREIY 243
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-234 |
1.02e-42 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 144.74 E-value: 1.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmhGRARAGIGYL 83
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAP--RAALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIM--AILEtrkDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:TIGR03864 80 FQQPTLDLDLSVRQNLRyhAALH---GLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVREtLDICETAYIVNDGQLIAEGTAEEILANQLVKEVY 234
Cdd:TIGR03864 157 DEPTVGLDPASRAAITAHVRALaRDQGLSVLWATHLVDE-IEASDRLVVLHRGRVLADGAAAELRGATGGADLE 229
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-215 |
9.65e-42 |
|
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: 141.47 E-value: 9.65e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKS----RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRA--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 RAGIGYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAP 156
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAG-VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNvRETLDICETAYIVNDGQL 215
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-219 |
9.66e-42 |
|
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: 141.18 E-value: 9.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGqIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARagIGYL 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVAD--NIMAILetrKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03264 78 PQEFGVYPNFTVREflDYIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 162 DEPFAGVDPisvgdiKQII---HHLKNKGIG--VLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03264 155 DEPTAGLDP------EERIrfrNLLSELGEDriVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-237 |
1.16e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 142.18 E-value: 1.16e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIG 81
Cdd:COG4674 9 PILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNIMAILETRKDLDRAGRHR-------ELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALAT 154
Cdd:COG4674 89 RKFQKPTVFEELTVFENLELALKGDRGVFASLFARltaeerdRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQ 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 155 APKFILLDEPFAGvdpISVGDIKQ---IIHHLKnKGIGVLITDHN---VRetlDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:COG4674 169 DPKLLLLDEPVAG---MTDAETERtaeLLKSLA-GKHSVVVVEHDmefVR---QIARKVTVLHQGSVLAEGSLDEVQADP 241
|
....*....
gi 764533248 229 LVKEVYLGH 237
Cdd:COG4674 242 RVIEVYLGR 250
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-238 |
1.18e-41 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 142.09 E-value: 1.18e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVvRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGIGYL 83
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRK-VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 164 PFAGVDPISVG----DIKQIIhhlKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEV--YLGH 237
Cdd:cd03299 156 PFSALDVRTKEklreELKKIR---KEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVaeFLGF 232
|
.
gi 764533248 238 E 238
Cdd:cd03299 233 N 233
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-234 |
1.26e-41 |
|
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: 141.94 E-value: 1.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKS-RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG--RARAGI 80
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAiletrkdlDRAGRHRELESLLQEFHISHIR------DSLGMS---------LSGGERRR 145
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLS--------GRLGRRSTWRSLFGLFPKEEKQralaalERVGLLdkayqradqLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 146 VEIARALATAPKFILLDEPFAGVDPISVgdiKQIIHHLK----NKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTA 221
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASS---RQVMDLLKrinrEEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
250
....*....|...
gi 764533248 222 EEiLANQLVKEVY 234
Cdd:cd03256 230 AE-LTDEVLDEIY 241
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-232 |
5.07e-41 |
|
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: 140.51 E-value: 5.07e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQ-VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGY 82
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMAI--LETRKDLDRAGRHRELESLLqEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVpkLLKWPKEKIRERADELLALV-GLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLK---NKGIgVLITdHNVRETLDICETAYIVNDGQLIAEGTAEEIL---ANQLVKE 232
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQqelGKTI-VFVT-HDIDEAFRLADRIAIMKNGEIVQVGTPDEILrspANDFVAE 234
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-224 |
3.79e-40 |
|
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: 137.70 E-value: 3.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKA-----DQGRVLIDQQDVTHQPMHGRA-R 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AGIGYLPQEASIFRKlSVADNIMAILETRKDLDRAGRHRELESLLQ------EFHishiRDSLGMSLSGGERRRVEIARA 151
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRkaalwdEVK----DRLHALGLSGGQQQRLCLARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 152 LATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKgIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:cd03260 156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-231 |
5.65e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 143.62 E-value: 5.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQ-PMHGRaRAG 79
Cdd:COG1129 2 EPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsPRDAQ-AAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQEASIFRKLSVADNIMAILETRKD--LDRAGRHRELESLLQEFHIsHIR-DSLGMSLSGGERRRVEIARALATAP 156
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGglIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 157 KFILLDEPFAgvdPISVGDIKQ---IIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVK 231
Cdd:COG1129 160 RVLILDEPTA---SLTEREVERlfrIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVR 234
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
6.75e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 136.48 E-value: 6.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGYL 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP-EWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKlSVADNIMAILETRKdldRAGRHRELESLLQEFHISH-IRDSLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRE---RKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 764533248 163 EPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-219 |
1.91e-39 |
|
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: 136.10 E-value: 1.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSR----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTH--QPMHGRA 76
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 RAGIGYLPQEA--SIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEfHISHIRDSLGM---SLSGGERRRVEIARA 151
Cdd:cd03257 81 RKEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLV-GVGLPEEVLNRyphELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 152 LATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-227 |
3.35e-39 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 135.51 E-value: 3.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRA-RAGIG 81
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-227 |
3.53e-39 |
|
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: 141.58 E-value: 3.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKS--RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD---QGRVLIDQQDVTHQPMHGRA 76
Cdd:COG1123 3 PLLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 RAgIGYLPQEA-SIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATA 155
Cdd:COG1123 83 RR-IGMVFQDPmTQLNPVTVGDQIAEALENLG-LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 156 PKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-224 |
3.83e-39 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 138.68 E-value: 3.83e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 8 HLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpMHGRARAgIGYLPQEA 87
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRK-VGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 88 SIFRKLSVADNI---MAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK10851 84 ALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 165 FAGVDPISVGDIKQIIHHLKN--KGIGVLITdHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEelKFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-196 |
5.40e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 134.41 E-value: 5.40e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYK-SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpMHGRA----R 77
Cdd:COG2884 1 MIRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSR--LKRREipylR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AGIGYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPK 157
Cdd:COG2884 79 RRIGVVFQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 764533248 158 FILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHN 196
Cdd:COG2884 158 LLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD 196
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-228 |
6.91e-39 |
|
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: 141.44 E-value: 6.91e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSY--KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmHGRARAGIG 81
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD-EDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKlSVADNIM---------AILETrkdLDRAGRHRELESLLQEFHiSHIrDSLGMSLSGGERRRVEIARAL 152
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRlarpdatdeELWAA---LERVGLGDWLAALPDGLD-TWL-GEGGRRLSGGERRRLALARAL 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 153 ATAPKFILLDEPFAGVDPISVGDI-KQIIHHLKNKGIgVLITDHnvRETLDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:COG4987 487 LRDAPILLLDEPTEGLDAATEQALlADLLEALAGRTV-LLITHR--LAGLERMDRILVLEDGRIVEQGTHEELLAQN 560
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-170 |
7.37e-39 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 137.90 E-value: 7.37e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGI 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170
....*....|
gi 764533248 161 LDEPFAGVDP 170
Cdd:COG3839 157 LDEPLSNLDA 166
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-228 |
2.18e-38 |
|
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: 141.12 E-value: 2.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaRAGIGYLPQEASIFRKlS 94
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-RRQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNIMAILETRKD------LDRAGRHRELESLLQEFHiSHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:COG2274 565 IRENITLGDPDATDeeiieaARLAGLHDFIEALPMGYD-TVVGEG-GSNLSGGQRQRLAIARALLRNPRILILDEATSAL 642
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 169 DPISVgdiKQIIHHLKN--KGIGVLITDHNvRETLDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:COG2274 643 DAETE---AIILENLRRllKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-228 |
6.87e-38 |
|
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: 138.74 E-value: 6.87e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSY-KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaRAGIGY 82
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFrKLSVADNimaILETRKDLDRAgrhrELESLLQEFHISHIRDSL-----------GMSLSGGERRRVEIARA 151
Cdd:COG4988 416 VPQNPYLF-AGTIREN---LRLGRPDASDE----ELEAALEAAGLDEFVAALpdgldtplgegGRGLSGGQAQRLALARA 487
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 152 LATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITdHNVrETLDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:COG4988 488 LLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRL-ALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-214 |
8.49e-38 |
|
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: 129.81 E-value: 8.49e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSR--QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIG 81
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFrKLSVADNImailetrkdldragrhrelesllqefhishirdslgmsLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHLKNKGIGVLITdHNVrETLDICETAYIVNDGQ 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIA-HRL-STIRDADRIIVLDDGR 171
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-227 |
2.73e-37 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 133.69 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGR------VLIDQQDVTHQPMHGRAragIGYLPQEASIFRKLS 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRirlggeVLQDSARGIFLPPHRRR---IGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNIMAileTRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:COG4148 94 VRGNLLY---GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 175 DI----KQIIHHLknkGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG4148 171 EIlpylERLRDEL---DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
2.91e-37 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 130.77 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMA---ILETRKDLDRAGRHRELESLLQEFhishiRDSLGMSLSGGERRRVEIARALATAPK 157
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMggfFAERDQFQERIKWVYELFPRLHER-----RIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 158 FILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVYLG 236
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-227 |
1.19e-36 |
|
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: 128.85 E-value: 1.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSR----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGR--A 76
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 RAGIGYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAP 156
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-219 |
1.63e-36 |
|
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: 128.18 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 28 SGQIVGLLGPNGAGKTTCFYMIVGLVKADQG------RVLIDQQDVTHQPMHGRaraGIGYLPQEASIFRKLSVADNI-- 99
Cdd:cd03297 22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngTVLFDSRKKINLPPQQR---KIGLVFQQYALFPHLNVRENLaf 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 100 -MAILETRKDLDRAgrhrelESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS----VG 174
Cdd:cd03297 99 gLKRKRNREDRISV------DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrlqlLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 764533248 175 DIKQIihhLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03297 173 ELKQI---KKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-231 |
2.70e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 133.61 E-value: 2.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVT-HQPMHGRArAGIG 81
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIA-LGIG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNIMAILETRKD--LDRAGRHRELESLLQEFHIS-----HIRDslgmsLSGGERRRVEIARALAT 154
Cdd:COG3845 84 MVHQHFMLVPNLTVAENIVLGLEPTKGgrLDRKAARARIRELSERYGLDvdpdaKVED-----LSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVK 231
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAE 235
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
3.68e-36 |
|
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: 125.62 E-value: 3.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVT-HQPMHGRaRAGIGY 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDAR-RAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQeasifrklsvadnimailetrkdldragrhrelesllqefhishirdslgmsLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 163 EPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-236 |
6.22e-36 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.79 E-value: 6.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 23 SLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGIGYLPQEASIFRKLSVADNIMAI 102
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 103 LETRKDLDRAGRHReLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHH 182
Cdd:COG3840 96 LRPGLKLTAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 183 L-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEV--YLG 236
Cdd:COG3840 175 LcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALaaYLG 231
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
19-238 |
1.00e-35 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 127.03 E-value: 1.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQEASIFRKLSVADN 98
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 99 IM-------------AILET-------RKDLDRAGRHRELESLLQefhisHIRDSLGmSLSGGERRRVEIARALATAPKF 158
Cdd:PRK11300 101 LLvaqhqqlktglfsGLLKTpafrraeSEALDRAATWLERVGLLE-----HANRQAG-NLAYGQQRRLEIARCMVTQPEI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVYLGH 237
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAYLGE 254
|
.
gi 764533248 238 E 238
Cdd:PRK11300 255 A 255
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-234 |
1.72e-35 |
|
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: 124.95 E-value: 1.72e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGL--VKADQGRVLIDQQDVTHQPMHGRARAGIG 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADnimailetrkdldragrhrelesllqefhisHIRDsLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03217 81 LAFQYPPEIPGVKNAD-------------------------------FLRY-VNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNvRETLD--ICETAYIVNDGQLIAEGTAEeiLANQLVKEVY 234
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY-QRLLDyiKPDRVHVLYDGRIVKSGDKE--LALEIEKKGY 200
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
15-228 |
3.21e-35 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 126.42 E-value: 3.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVthqPMHGR-----ARAGIGYLPQEASI 89
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRsrlytVRKRMSMLFQSGAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 90 FRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVD 169
Cdd:PRK11831 96 FTDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 170 PISVGDIKQIIHHLkNKGIGV--LITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:PRK11831 176 PITMGVLVKLISEL-NSALGVtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-195 |
5.36e-35 |
|
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: 124.18 E-value: 5.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRA-RAGIGY 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|...
gi 764533248 163 EPFAGVDPISVGDIKQIIHHLKNKGIGVLITDH 195
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-224 |
7.97e-35 |
|
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: 124.27 E-value: 7.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGIGYL 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 164 PFAGVDpisvgdiKQIIHHL--------KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:cd03300 157 PLGALD-------LKLRKDMqlelkrlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-226 |
1.57e-34 |
|
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: 126.38 E-value: 1.57e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDqqDVTHQ--------PMHGRAragIGYLPQEASIFRK 92
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLN--GRTLFdsrkgiflPPEKRR---IGYVFQEARLFPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 LSVADNImaiLETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS 172
Cdd:TIGR02142 90 LSVRGNL---RYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 173 VgdiKQIIHHLKN----KGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:TIGR02142 167 K---YEILPYLERlhaeFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-169 |
4.05e-34 |
|
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: 121.59 E-value: 4.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGIGYL 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRK----DLDRagRHRELESLLQefhISHIRDSLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKvpkdEIDE--RVREVAELLQ---IEHLLDRKPKQLSGGQRQRVALGRAIVREPKVF 152
|
170
....*....|
gi 764533248 160 LLDEPFAGVD 169
Cdd:cd03301 153 LMDEPLSNLD 162
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-234 |
6.28e-34 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 122.10 E-value: 6.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGL--VKADQGRVLIDQQDVTHQPMHGRARAGIG 81
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YL---PQEasiFRKLSVADNIMAILETR--KDLDRAGRHRELESLLQEFHI--SHIRDSLGMSLSGGERRRVEIARALAT 154
Cdd:COG0396 81 LAfqyPVE---IPGVSVSNFLRTALNARrgEELSAREFLKLLKEKMKELGLdeDFLDRYVNEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVReTLDICE--TAYIVNDGQLIAEGTAEeiLANQLVKE 232
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQR-ILDYIKpdFVHVLVDGRIVKSGGKE--LALELEEE 234
|
..
gi 764533248 233 VY 234
Cdd:COG0396 235 GY 236
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
1.00e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 123.38 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIg 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 yLPQEASIFRKLSVADNIMAIleTRKDLDRAGRHRELESLLQEF-HISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13537 85 -VPQFDNLDPDFTVRENLLVF--GRYFGLSAAAARALVPPLLEFaKLENKADAKVGELSGGMKRRLTLARALVNDPDVLV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQL---VKEVY 234
Cdd:PRK13537 162 LDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEIY 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-227 |
1.87e-33 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 123.26 E-value: 1.87e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSYKSR----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG--RARAGI 80
Cdd:COG1135 5 ENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAARRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG1135 85 GMIFQHFNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 161 LDEPFAGVDPISVGDI----KQIihhlkNKGIG---VLITD--HNVREtldICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG1135 164 CDEATSALDPETTRSIldllKDI-----NRELGltiVLITHemDVVRR---ICDRVAVLENGRIVEQGPVLDVFAN 231
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-170 |
3.20e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.51 E-value: 3.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD---QGRVLIDQQDVTHQPMHGRaraGI 80
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR---RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMaiLETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLA--FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170
....*....|
gi 764533248 161 LDEPFAGVDP 170
Cdd:COG4136 157 LDEPFSKLDA 166
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-234 |
3.23e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.61 E-value: 3.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmhGRARAGI-GY 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWS--PWELARRrAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADnIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALA-------TA 155
Cdd:COG4559 80 LPQHSSLAFPFTVEE-VVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 156 PKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVY 234
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-201 |
1.04e-32 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 119.58 E-value: 1.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSY----KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqPMHGRa 76
Cdd:COG4525 1 MSMLTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 ragiGYLPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAP 156
Cdd:COG4525 79 ----GVVFQKDALLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETL 201
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEAL 199
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-241 |
1.07e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.48 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 11 KSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVthqPMHGR-ARAGIGYLPQEASI 89
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARlARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 90 FRKLSVADNIMAIletrkdldraGRH-----RELE----SLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13536 126 DLEFTVRENLLVF----------GRYfgmstREIEavipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLI 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQL---VKEVYLG- 236
Cdd:PRK13536 196 LDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIgcqVIEIYGGd 275
|
....*.
gi 764533248 237 -HEFRL 241
Cdd:PRK13536 276 pHELSS 281
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-234 |
1.59e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 118.65 E-value: 1.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 5 KAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmhGRARAgigylp 84
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP--SRELA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 85 qeasifRKLSV--ADNIMAILETRKDLDRAGR------------HRELESLLQEFHISHIRDSLGMSLSGGERRRVEIAR 150
Cdd:COG4604 75 ------KRLAIlrQENHINSRLTVRELVAFGRfpyskgrltaedREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 151 ALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHnvretlDI----CETAYIV--NDGQLIAEGTAEE 223
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH------DInfasCYADHIVamKDGRVVAQGTPEE 222
|
250
....*....|.
gi 764533248 224 ILANQLVKEVY 234
Cdd:COG4604 223 IITPEVLSDIY 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-224 |
1.64e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 123.20 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAksykSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGY 82
Cdd:COG1129 256 VLEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAY 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LP---QEASIFRKLSVADNI-MAILETRKD---LDRAGRHRELESLLQEFHI--SHIRDSLGmSLSGGERRRVEIARALA 153
Cdd:COG1129 332 VPedrKGEGLVLDLSIRENItLASLDRLSRgglLDRRRERALAEEYIKRLRIktPSPEQPVG-NLSGGNQQKVVLAKWLA 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 154 TAPKFILLDEPFAGVDpisVG---DIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:COG1129 411 TDPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
16-226 |
2.23e-32 |
|
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: 123.70 E-value: 2.23e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmhgRARAG--IGYLPQEASIFRKl 93
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELGrhIGYLPQDVELFDG- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNI--MAILETRKDLD---RAGRHRELESLLQEFHiSHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:COG4618 421 TIAENIarFGDADPEKVVAaakLAGVHEMILRLPDGYD-TRIGEG-GARLSGGQRQRIGLARALYGDPRLVVLDEPNSNL 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 169 DPISVGDIKQIIHHLKNKGIGVLITDHNVReTLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:COG4618 499 DDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVLA 555
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-238 |
5.12e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 117.57 E-value: 5.12e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIG 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNI----MAILETRKDLDRAgrhreLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALA---- 153
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVamgrAPHGLSRAEDDAL-----VAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwe 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 154 --TAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLV 230
Cdd:PRK13548 155 pdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETL 234
|
....*...
gi 764533248 231 KEVYlGHE 238
Cdd:PRK13548 235 RRVY-GAD 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-227 |
2.58e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 116.33 E-value: 2.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSY-KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQP---MHGRARA 78
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GIGYLPQEASIFRKlSVADNImAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK13639 81 GIVFQNPDDQLFAP-TVEEDV-AFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK13639 159 IVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSD 227
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-234 |
6.29e-31 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 114.73 E-value: 6.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIGY 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQ-----EASIFRKLsVADNIMAILETRKDLDRAGRHReLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPK 157
Cdd:PRK11231 81 LPQhhltpEGITVREL-VAYGRSPWLSLWGRLSAEDNAR-VNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 158 FILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVY 234
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF 235
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-198 |
6.49e-31 |
|
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: 113.91 E-value: 6.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 14 KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD---QGRVLIDQQDVTHQPMHGRaragIGYLPQEASIF 90
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC----VAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 RKLSVADNI--MAILETRKDLDRAGRHRELE-SLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:cd03234 94 PGLTVRETLtyTAILRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190
....*....|....*....|....*....|.
gi 764533248 168 VDPISVGDIKQIIHHLKNKGIGVLITDHNVR 198
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPR 204
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-227 |
8.00e-31 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 119.11 E-value: 8.00e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 12 SY-KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGYLPQEASIF 90
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLE-SLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 rKLSVADNI-MAILE-TRKDLDRAGR----HRELESLLQEFHiSHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:COG1132 427 -SGTIRENIrYGRPDaTDEEVEEAAKaaqaHEFIEALPDGYD-TVVGER-GVNLSGGQRQRIAIARALLKDPPILILDEA 503
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 165 FAGVDPISVgdiKQIIHHLKN--KGIGVLITDHNVReTLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG1132 504 TSALDTETE---ALIQEALERlmKGRTTIVIAHRLS-TIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-224 |
1.55e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.09 E-value: 1.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRAragIGY 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP---INM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 163 EPFAGVDP-------ISVGDIkqiihhLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK11607 175 EPMGALDKklrdrmqLEVVDI------LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-215 |
2.36e-30 |
|
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: 110.98 E-value: 2.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAksykSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIG 81
Cdd:cd03215 3 PVLEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLP---QEASIFRKLSVADNImailetrkdldragrhrelesllqefhishirdSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:cd03215 79 YVPedrKREGLVLDLSVAENI---------------------------------ALSSLLSGGNQQKVVLARWLARDPRV 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:cd03215 126 LILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
2.73e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 113.36 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYK-SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG-RARA 78
Cdd:PRK13652 1 MHLIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GIGYLPQEASIFRKLSVADniMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK13652 81 GLVFQNPDDQIFSPTVEQD--IAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI-LANQLVKEVYL 235
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARVHL 237
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-219 |
3.84e-30 |
|
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: 112.04 E-value: 3.84e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 13 YKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIgYLPQEASIFRK 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 LSVADNiMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS 172
Cdd:cd03267 110 LPVIDS-FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVA 188
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 764533248 173 VGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03267 189 QENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-216 |
4.35e-30 |
|
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: 111.19 E-value: 4.35e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 6 AQHLAKSY-KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVthqpmHGRARAG-IGYL 83
Cdd:cd03226 2 IENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-----KAKERRKsIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEAS--IFRKlSVADNImaiLETRKDLDRAGRhrELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03226 77 MQDVDyqLFTD-SVREEL---LLGLKELDAGNE--QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLI 216
Cdd:cd03226 151 DEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
6.34e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 112.39 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYK--SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAG 79
Cdd:PRK13632 6 VMIKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK-EIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQEA-SIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVEDDIAFGLENKK-VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLIT-DHNVRETLdICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNN 232
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-219 |
2.51e-29 |
|
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: 109.12 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMhgrARAGIGYLPQEASIFRKLSVADNIM 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 101 AILETRKDLDRAGRHReLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQII 180
Cdd:cd03298 93 LGLSPGLKLTAEDRQA-IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 764533248 181 HHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-236 |
6.37e-29 |
|
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: 109.85 E-value: 6.37e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQP--MHGRARAGIGYLPQ--EASIFr 91
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkKLKDLRKKVGLVFQfpEHQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 92 KLSVADNIM--------AILETRKDLDRAGRHREL-ESLLQE--FHishirdslgmsLSGGERRRVEIARALATAPKFIL 160
Cdd:TIGR04521 97 EETVYKDIAfgpknlglSEEEAEERVKEALELVGLdEEYLERspFE-----------LSGGQMRRVAIAGVLAMEPEVLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN-QLVKEVYLG 236
Cdd:TIGR04521 166 LDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDvDELEKIGLD 243
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-164 |
6.98e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.24 E-value: 6.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 6 AQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIdQQDVThqpmhgraragIGYLPQ 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 86 EASIFRKLSVADNIM------------------AILETRKDLDRAGR-------------HRELESLLQEFHISHIRDSL 134
Cdd:COG0488 69 EPPLDDDLTVLDTVLdgdaelraleaeleeleaKLAEPDEDLERLAElqeefealggweaEARAEEILSGLGFPEEDLDR 148
|
170 180 190
....*....|....*....|....*....|.
gi 764533248 135 GMS-LSGGERRRVEIARALATAPKFILLDEP 164
Cdd:COG0488 149 PVSeLSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-227 |
1.07e-28 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 108.59 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTT---CF---YMIVGLVKADqGRVLIDQQDVTHQ---PM 72
Cdd:COG1117 10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLnrmNDLIPGARVE-GEILLDGEDIYDPdvdVV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 73 HGRARagIGYLPQEASIFRKlSVADNIMAILETRKDLDRAGRHRELESLLQEFHI-SHIRDSL---GMSLSGGERRRVEI 148
Cdd:COG1117 89 ELRRR--VGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwDEVKDRLkksALGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 149 ARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKgIGVLITDHNVRETLDICE-TAYIvNDGQLIAEGTAEEILAN 227
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDyTAFF-YLGELVEFGPTEQIFTN 243
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-226 |
1.26e-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: 112.97 E-value: 1.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKS--RQVVR---DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLI----DQQDVTHQPMH 73
Cdd:TIGR03269 279 IIKVRNVSKRYISvdRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 74 GRARAG--IGYLPQEASIFRKLSVADNIM-AI-LETRKDLdraGRHRELESL----LQEFHISHIRDSLGMSLSGGERRR 145
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPHRTVLDNLTeAIgLELPDEL---ARMKAVITLkmvgFDEEKAEEILDKYPDELSEGERHR 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 146 VEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515
|
..
gi 764533248 225 LA 226
Cdd:TIGR03269 516 VE 517
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-164 |
2.25e-28 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 112.08 E-value: 2.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVlidqqdvthqpmhgraRAG--- 79
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------------KLGetv 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 -IGYLPQEASIFR-KLSVADNImailetrKDLDRAGRHRELESLLQEFHIS--HIRDSLGmSLSGGERRRVEIARALATA 155
Cdd:COG0488 379 kIGYFDQHQEELDpDKTVLDEL-------RDGAPGGTEQEVRGYLGRFLFSgdDAFKPVG-VLSGGEKARLALAKLLLSP 450
|
....*....
gi 764533248 156 PKFILLDEP 164
Cdd:COG0488 451 PNVLLLDEP 459
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
2.52e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 108.40 E-value: 2.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKS-RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQP---MHGRARA 78
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRkglMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GIGYLPQEASIFRKLSVADNIMAILETRKDLDRAgrHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK13636 85 GMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEV--RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 159 ILLDEPFAGVDPISVGDI-KQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANqlvKEVYLGH 237
Cdd:PRK13636 163 LVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE---KEMLRKV 239
|
....
gi 764533248 238 EFRL 241
Cdd:PRK13636 240 NLRL 243
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-226 |
2.81e-28 |
|
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: 112.06 E-value: 2.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTH--QPMHGRAragIGYLPQEASIFrKL 93
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwdRETFGKH---IGYLPQDVELF-PG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNIM---------AILETRKdldRAGRHRELESLLQEFHiSHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:TIGR01842 407 TVAENIArfgenadpeKIIEAAK---LAGVHELILRLPDGYD-TVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 165 FAGVDpiSVGDI--KQIIHHLKNKGIGVLITDHNVReTLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:TIGR01842 482 NSNLD--EEGEQalANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-227 |
3.15e-28 |
|
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: 108.99 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSR----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKA---DQGRVLIDQQDVTHqpMHGR 75
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK--LSEK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 76 AR-----AGIGYLPQE--ASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGM---SLSGGERRR 145
Cdd:COG0444 79 ELrkirgREIQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 146 VEIARALATAPKFILLDEPFAGVDpISVGdiKQIIHHLKN----KGIGVL-ITdHN---VREtldICETAYIVNDGQLIA 217
Cdd:COG0444 159 VMIARALALEPKLLIADEPTTALD-VTIQ--AQILNLLKDlqreLGLAILfIT-HDlgvVAE---IADRVAVMYAGRIVE 231
|
250
....*....|
gi 764533248 218 EGTAEEILAN 227
Cdd:COG0444 232 EGPVEELFEN 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-230 |
3.42e-28 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 111.25 E-value: 3.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIG 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNIMAileTRKDLDRAGR------HRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATA 155
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFL---GREFVNRFGRidwkkmYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 156 PKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLV 230
Cdd:PRK10762 160 SKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLI 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
16-219 |
4.47e-28 |
|
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: 106.13 E-value: 4.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaRAGIGYLPQEASIFrKLSV 95
Cdd:cd03245 17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLF-YGTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNI------------MAILETRKDLDRAGRH-RELESLLQEfhishirdsLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03245 95 RDNItlgapladderiLRAAELAGVTDFVNKHpNGLDLQIGE---------RGRGLSGGQRQAVALARALLNDPPILLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 163 EPFAGVDPISVgdiKQIIHHLKN--KGIGVLITDHNVReTLDICETAYIVNDGQLIAEG 219
Cdd:cd03245 166 EPTSAMDMNSE---ERLKERLRQllGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-223 |
6.31e-28 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 107.02 E-value: 6.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQ---GRVLIDQQDVTHQPMHGR---- 75
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLARdirk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 76 ARAGIGYLPQEASIFRKLSVADNIM--AILETR------KDLDRAGRHRELESLLQ--EFHISHIRDSlgmSLSGGERRR 145
Cdd:PRK09984 84 SRANTGYIFQQFNLVNRLSVLENVLigALGSTPfwrtcfSWFTREQKQRALQALTRvgMVHFAHQRVS---TLSGGQQQR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 146 VEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEE 223
Cdd:PRK09984 161 VAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ 239
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
15-215 |
9.07e-28 |
|
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: 104.22 E-value: 9.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMhGRARAGIGYLPQEASIFrKLS 94
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVGYLPQDDELF-SGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNImailetrkdldragrhrelesllqefhishirdslgmsLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:cd03246 92 IAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 764533248 175 DIKQIIHHLKNKGIGVLITDHNvRETLDICETAYIVNDGQL 215
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
15-193 |
9.78e-28 |
|
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: 110.45 E-value: 9.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaRAGIGYLPQEASIFRKlS 94
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNIM------AILETRKDLDRAGRHRELESLLQEFHIshIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:TIGR02857 412 IAENIRlarpdaSDAEIREALERAGLDEFVAALPQGLDT--PIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHL 489
|
170 180
....*....|....*....|....*
gi 764533248 169 DPISVGDIKQIIHHLKNKGIGVLIT 193
Cdd:TIGR02857 490 DAETEAEVLEALRALAQGRTVLLVT 514
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-196 |
2.10e-27 |
|
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: 104.41 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpMHGRA----RAGIGYLPQEASIFRKLSVA 96
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSD--LRGRAipylRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 97 DNIMAILETRKDLDRAGRHReLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDI 176
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKR-VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180
....*....|....*....|
gi 764533248 177 KQIIHHLKNKGIGVLITDHN 196
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHA 195
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-224 |
4.67e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 108.21 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTH-QPMHGRArAGIG 81
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQ-LGIY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNIMAILETrkdldRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:PRK15439 90 LVPQEPLLFPNLSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-227 |
7.68e-27 |
|
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: 104.26 E-value: 7.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmHGRARA----GIGYLPQEASIFRKLS 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS-RKELRElrrkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNIMAILETRkDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:cd03294 119 VLENVAFGLEVQ-GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRR 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 764533248 175 DIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:cd03294 198 EMQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-226 |
7.95e-27 |
|
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: 103.07 E-value: 7.95e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 12 SY-KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVtHQPMHGRARAGIGYLPQEASIF 90
Cdd:cd03254 11 SYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI-RDISRKSLRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 RKlSVADNI-MAILETRKD-----LDRAGRHRELESLLQEFHiSHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd03254 90 SG-TIMENIrLGRPNATDEevieaAKEAGAHDFIMKLPNGYD-TVLGEN-GGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 165 FAGVDPISVGDIKQIIHHLkNKGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGTAEEILA 226
Cdd:cd03254 167 TSNIDTETEKLIQEALEKL-MKGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-224 |
8.26e-27 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 106.18 E-value: 8.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRAragIGY 82
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---VNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELESL----LQEFHISHIRDslgmsLSGGERRRVEIARALATAPKF 158
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALrmvqLEEFAQRKPHQ-----LSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-195 |
1.15e-26 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 101.54 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 12 SYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVlidqqdvthqpmHGRARAGIGYLPQEASIFR 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 92 KL--SVADNI-MAILETRKDLDRAGR--HRELESLLQEFHISHIRD-SLGmSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:NF040873 69 SLplTVRDLVaMGRWARRGLWRRLTRddRAAVDDALERVGLADLAGrQLG-ELSGGQRQRALLAQGLAQEADLLLLDEPT 147
|
170 180 190
....*....|....*....|....*....|
gi 764533248 166 AGVDPISVGDIKQIIHHLKNKGIGVLITDH 195
Cdd:NF040873 148 TGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-227 |
1.63e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.91 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMI------------VGLVKADQGRVLIDQQDVT 68
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCInlleqpeagtirVGDITIDTARSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 69 HQpmhgrARAGIGYLPQEASIFRKLSVADNIM---AILETRKDLDRAGRHRELeslLQEFHISHIRDSLGMSLSGGERRR 145
Cdd:PRK11264 81 RQ-----LRQHVGFVFQNFNLFPHRTVLENIIegpVIVKGEPKEEATARAREL---LAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 146 VEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEIL 225
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
..
gi 764533248 226 AN 227
Cdd:PRK11264 233 AD 234
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-218 |
1.98e-26 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 102.96 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKS---------RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTH-QP 71
Cdd:TIGR02769 1 SLLEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 72 MHGRA-RAGIGYLPQEA--SIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHI-SHIRDSLGMSLSGGERRRVE 147
Cdd:TIGR02769 81 KQRRAfRRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-227 |
2.07e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.50 E-value: 2.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 5 KAQHLAKSY--KSRQV--VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG--RARA 78
Cdd:PRK11153 3 ELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GIGYLPQEasiFRKLS---VADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATA 155
Cdd:PRK11153 83 QIGMIFQH---FNLLSsrtVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 156 PKFILLDEPFAGVDPISVgdiKQIIHHLK--NKGIG---VLITdHN---VREtldICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK11153 159 PKVLLCDEATSALDPATT---RSILELLKdiNRELGltiVLIT-HEmdvVKR---ICDRVAVIDAGRLVEQGTVSEVFSH 231
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-222 |
2.21e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 102.40 E-value: 2.21e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAIlKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLI-DQQ-DVTHQPMHGRARA 78
Cdd:COG4161 1 MSI-QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIaGHQfDFSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 ---GIGYLPQEASIFRKLSVADNI----MAILETRKDLDRAgrhrELESLLQEFHISHIRDSLGMSLSGGERRRVEIARA 151
Cdd:COG4161 80 lrqKVGMVFQQYNLWPHLTVMENLieapCKVLGLSKEQARE----KAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 152 LATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAE 222
Cdd:COG4161 156 LMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-224 |
3.17e-26 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 105.88 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHL-AKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIG 81
Cdd:COG3845 257 VLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEasifRK-------LSVADNimAILETRKD--------LDRAGRHRELESLLQEFHI--SHIRDSLGmSLSGGERR 144
Cdd:COG3845 337 YIPED----RLgrglvpdMSVAEN--LILGRYRRppfsrggfLDRKAIRAFAEELIEEFDVrtPGPDTPAR-SLSGGNQQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 145 RVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-225 |
3.41e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 3.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVthqpmHGRARAGI 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDV-----EALSARAA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYL----PQEASIFRKLSVADNI-MAILETRKDLDRAGR--HRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALA 153
Cdd:PRK09536 76 SRRvasvPQDTSLSFEFDVRQVVeMGRTPHRSRFDTWTEtdRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 154 TAPKFILLDEPFAGVDpisvgdikqiIHH----------LKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEE 223
Cdd:PRK09536 156 QATPVLLLDEPTASLD----------INHqvrtlelvrrLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPAD 225
|
..
gi 764533248 224 IL 225
Cdd:PRK09536 226 VL 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-224 |
3.75e-26 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 104.03 E-value: 3.75e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGIGYLPQE 86
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 87 ASIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLG-VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 167 GVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-199 |
4.15e-26 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 102.17 E-value: 4.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTT---CFYMIVGLVKA--DQGRVLIDQQDVTHQ---PMHG 74
Cdd:PRK14243 10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPGfrVEGKVTFHGKNLYAPdvdPVEV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 75 RARagIGYLPQEASIFRKlSVADNIM---AILETRKDLDragrhrEL--ESLLQEFHISHIRDSL---GMSLSGGERRRV 146
Cdd:PRK14243 90 RRR--IGMVFQKPNPFPK-SIYDNIAygaRINGYKGDMD------ELveRSLRQAALWDEVKDKLkqsGLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 764533248 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITdHNVRE 199
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HNMQQ 212
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-197 |
4.32e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAIlKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLI--DQQDVTHQP--MHGRA 76
Cdd:PRK11124 1 MSI-QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIagNHFDFSKTPsdKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 -RAGIGYLPQEASIFRKLSVADNI----MAILEtrkdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARA 151
Cdd:PRK11124 80 lRRNVGMVFQQYNLWPHLTVQQNLieapCRVLG----LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 764533248 152 LATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNV 197
Cdd:PRK11124 156 LMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEV 201
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-234 |
7.29e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 100.93 E-value: 7.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTcfymIVGLVKADQ-----------GRVL--IDQQDV 67
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGDLpptygndvrlfGERRggEDVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 68 thqpmhgRARagIGYLPQE--ASIFRKLSVADnimAIL------------ETRKDLDRAgrhrelESLLQEFHISHIRDS 133
Cdd:COG1119 77 -------RKR--IGLVSPAlqLRFPRDETVLD---VVLsgffdsiglyrePTDEQRERA------RELLELLGLAHLADR 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 134 LGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL---KNKGIgVLITdHNVRETLDICETAYIV 210
Cdd:COG1119 139 PFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaaeGAPTL-VLVT-HHVEEIPPGITHVLLL 216
|
250 260
....*....|....*....|....
gi 764533248 211 NDGQLIAEGTAEEILANQLVKEVY 234
Cdd:COG1119 217 KDGRVVAAGPKEEVLTSENLSEAF 240
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-234 |
1.62e-25 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 100.03 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVG--LVKADQGRVLIDQQDVTHQPMHGRARAGIg 81
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDERARAGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YL----PQE-----ASIFrkLSVADNIMAILETRKDLDRAGRHRELESLLQ--EFHISHIRDSLGMSLSGGERRRVEIAR 150
Cdd:TIGR01978 80 FLafqyPEEipgvsNLEF--LRSALNARRSARGEEPLDLLDFEKLLKEKLAllDMDEEFLNRSVNEGFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 151 ALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVReTLD--ICETAYIVNDGQLIAEGTAEeiLANQ 228
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR-LLNyiKPDYVHVLLDGRIVKSGDVE--LAKE 234
|
....*.
gi 764533248 229 LVKEVY 234
Cdd:TIGR01978 235 LEAKGY 240
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-226 |
8.19e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 98.93 E-value: 8.19e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQdvthqPMHGRARAGIGY 82
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK-----PLDYSKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRklsvaDNIMAILETRKDLDRAGRHREL-----------ESLLQEFHISHIRDSLGMSLSGGERRRVEIARA 151
Cdd:PRK13638 76 RQQVATVFQ-----DPEQQIFYTDIDSDIAFSLRNLgvpeaeitrrvDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 152 LATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:PRK13638 151 LVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-226 |
8.50e-25 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 97.73 E-value: 8.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 23 SLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmhgRARAGIGYLPQEASIFRKLSVADNIMAI 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP---PSRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 103 LETRKDLDRAGRHReLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHH 182
Cdd:PRK10771 96 LNPGLKLNAAQREK-LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 764533248 183 L-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:PRK10771 175 VcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLS 219
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
3-198 |
8.60e-25 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 97.81 E-value: 8.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSR----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVthQPMHGRARA 78
Cdd:TIGR02211 1 LLKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSL--SKLSSNERA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GI-----GYLPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELEsLLQEFHISHIRDSLGMSLSGGERRRVEIARALA 153
Cdd:TIGR02211 79 KLrnkklGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYE-MLEKVGLEHRINHRPSELSGGERQRVAIARALV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 764533248 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVR 198
Cdd:TIGR02211 158 NQPSLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLE 203
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-201 |
1.27e-24 |
|
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: 96.47 E-value: 1.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 12 SYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVK--ADQGRVLIDQQDVTHQpmhgRARAGIGYLPQEASI 89
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTglGVSGEVLINGRPLDKR----SFRKIIGYVPQDDIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 90 FRKLSVADNIMailetrkdldragrhrelesllqefHISHIRdslgmSLSGGERRRVEIARALATAPKFILLDEPFAGVD 169
Cdd:cd03213 94 HPTLTVRETLM-------------------------FAAKLR-----GLSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
170 180 190
....*....|....*....|....*....|..
gi 764533248 170 PISVGDIKQIIHHLKNKGIGVLITDHNVRETL 201
Cdd:cd03213 144 SSSALQVMSLLRRLADTGRTIICSIHQPSSEI 175
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-226 |
1.53e-24 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 98.22 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYK---------SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAhgglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 72 MHGRA--RAGIGYLPQEA--SIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHIS-HIRDSLGMSLSGGERRRV 146
Cdd:PRK10419 81 RAQRKafRRDIQMVFQDSisAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEIL 225
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKL 240
|
.
gi 764533248 226 A 226
Cdd:PRK10419 241 T 241
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-236 |
1.57e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 97.81 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLV-------KADqGRVLIDQQDVtHQPMHGRARAGIGYLPQEAS 88
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskiKVD-GKVLYFGKDI-FQIDAIKLRKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 89 IFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHI-SHIRDSL---GMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 165 FAGVDPISVGDIKQIIHHLKNKgIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA---NQLVKEVYLG 236
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTspkNELTEKYVIG 254
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-230 |
1.84e-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: 101.05 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD--QGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIM---AILETRKDLDRAGRHRELESLLQEFHISHIRDSLG-MSLSGGERRRVEIARALATAP 156
Cdd:TIGR02633 81 VIIHQELTLVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLV 230
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII 234
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
2-232 |
2.84e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 97.15 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMI------------VGLVKADQGRVLIDQQDVTh 69
Cdd:PRK14239 4 PILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIYSPRTDTV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 70 qpmhgRARAGIGYLPQEASIFrKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHI-SHIRDSL---GMSLSGGERRR 145
Cdd:PRK14239 83 -----DLRKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLhdsALGLSGGQQQR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 146 VEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITdHNVRETLDICE-TAYIVnDGQLIAEGTAEEI 224
Cdd:PRK14239 157 VCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDrTGFFL-DGDLIEYNDTKQM 234
|
....*...
gi 764533248 225 LANQLVKE 232
Cdd:PRK14239 235 FMNPKHKE 242
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-226 |
3.02e-24 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 96.79 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDV-THQPMHGRARagIGYLPQEASIFRKl 93
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQ--VGVVLQENVLFNR- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNImAILETRKDLDR-------AGRHRELESLLQEFhiSHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:cd03252 91 SIRDNI-ALADPGMSMERvieaaklAGAHDFISELPEGY--DTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 167 GVDPISVGDIKQIIHHLkNKGIGVLITDHNVrETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:cd03252 168 ALDYESEHAIMRNMHDI-CAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLA 225
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-226 |
4.79e-24 |
|
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: 96.15 E-value: 4.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGrARAGIGYLPQEASIFRKlS 94
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNIM---------AILETRKdldRAGRHRELESLLQEFhiSHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:cd03253 91 IGYNIRygrpdatdeEVIEAAK---AAQIHDKIMRFPDGY--DTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDEAT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 166 AGVDPISVGDIKQIIHHLKNKGIGVLITdHNVRETLDiCETAYIVNDGQLIAEGTAEEILA 226
Cdd:cd03253 166 SALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVN-ADKIIVLKDGRIVERGTHEELLA 224
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-169 |
4.94e-24 |
|
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: 95.96 E-value: 4.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSR----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRAR 77
Cdd:COG4181 7 PIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 ---AGIGYLPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELeslLQEFHISHIRDSLGMSLSGGERRRVEIARALAT 154
Cdd:COG4181 87 lraRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARAL---LERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
|
170
....*....|....*
gi 764533248 155 APKFILLDEPFAGVD 169
Cdd:COG4181 164 EPAILFADEPTGNLD 178
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-201 |
7.23e-24 |
|
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: 95.61 E-value: 7.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThQPMHGRAragigYLPQEASIFRKLSVADN 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPDRM-----VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 99 I-MAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIK 177
Cdd:TIGR01184 75 IaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180
....*....|....*....|....*
gi 764533248 178 -QIIHHLKNKGIGVLITDHNVRETL 201
Cdd:TIGR01184 155 eELMQIWEEHRVTVLMVTHDVDEAL 179
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-241 |
9.71e-24 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 95.29 E-value: 9.71e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 22 VSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAdQGRVLIDQQDVTHQPMHG--RARAgigYLPQEAS------IFRKL 93
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAElaRHRA---YLSQQQSppfampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SvadnimaiLETRKDLDRAGRHRELESLLQEFHIShirDSLG---MSLSGGERRRVEIARALAT-------APKFILLDE 163
Cdd:COG4138 91 A--------LHQPAGASSEAVEQLLAQLAEALGLE---DKLSrplTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVYlGHEFRL 241
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF-GVKFRR 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
3-164 |
1.06e-23 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 97.11 E-value: 1.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSY--------KSRQVVR---DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqp 71
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 72 MHGRA----RAGIGYLPQE--ASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLqefhishirDSLGMS-------- 137
Cdd:COG4608 85 LSGRElrplRRRMQMVFQDpyASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELL---------ELVGLRpehadryp 155
|
170 180
....*....|....*....|....*....
gi 764533248 138 --LSGGERRRVEIARALATAPKFILLDEP 164
Cdd:COG4608 156 heFSGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-195 |
1.15e-23 |
|
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: 98.59 E-value: 1.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQ-VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVtHQPMHGRARAGIGY 82
Cdd:TIGR02868 335 LELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV-SSLDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKlSVADNIM------AILETRKDLDRAGRHRELESLLQEFHISHIRDslGMSLSGGERRRVEIARALATAP 156
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRlarpdaTDEELWAALERVGLADWLRALPDGLDTVLGEG--GARLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 764533248 157 KFILLDEPFAGVDPisvGDIKQIIHHLKNKGIG---VLITDH 195
Cdd:TIGR02868 491 PILLLDEPTEHLDA---ETADELLEDLLAALSGrtvVLITHH 529
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-227 |
1.50e-23 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 94.77 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRA-RAGIGYLPQ 85
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 86 EASIFRKLSVADNIM-AILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK09493 85 QFYLFPHLTALENVMfGPLRVRG-ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 165 FAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-214 |
1.66e-23 |
|
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: 92.13 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQqdvthqpmhgraRAGIGYL 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQeasifrklsvadnimailetrkdldragrhrelesllqefhishirdslgmsLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03221 69 EQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 764533248 164 PFAGVDPISvgdIKQIIHHLKNKGIGVLITDHNvRETLD-ICETAYIVNDGQ 214
Cdd:cd03221 97 PTNHLDLES---IEALEEALKEYPGTVILVSHD-RYFLDqVATKIIELEDGK 144
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-220 |
2.22e-23 |
|
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: 98.55 E-value: 2.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVthQPMHGRARAGIGYLPQEASIFRKLSV 95
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLTV 1020
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNIMAILETR-KDLDRAgrHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:TIGR01257 1021 AEHILFYAQLKgRSWEEA--QLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRR 1098
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 764533248 175 DIKQIIHHLKNkGIGVLITDHNVRETLDICETAYIVNDGQLIAEGT 220
Cdd:TIGR01257 1099 SIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-227 |
2.32e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.92 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQ---------------------VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVL 61
Cdd:COG4586 1 IIEVENLSKTYRVYEkepglkgalkglfrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 62 IDqqdvthqpmhgraragiGYLPQEASI-FRK---------------LSVADNimaiLETRK---DLDRAGRHRELESLL 122
Cdd:COG4586 81 VL-----------------GYVPFKRRKeFARrigvvfgqrsqlwwdLPAIDS----FRLLKaiyRIPDAEYKKRLDELV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 123 QEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETL 201
Cdd:COG4586 140 ELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIE 219
|
250 260
....*....|....*....|....*.
gi 764533248 202 DICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG4586 220 ALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-235 |
2.32e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 95.25 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKS--RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLV---KADQGRVLIDQQDVTHQPMHG-RA 76
Cdd:PRK13640 5 IVEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDiRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 RAGIGYLPQEASiFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAP 156
Cdd:PRK13640 85 KVGIVFQNPDNQ-FVGATVGDDVAFGLENRA-VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHLKN-KGIGVLITDHNVRETlDICETAYIVNDGQLIAEGTAEEILAN-QLVKEVY 234
Cdd:PRK13640 163 KIIILDESTSMLDPAGKEQILKLIRKLKKkNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKvEMLKEIG 241
|
.
gi 764533248 235 L 235
Cdd:PRK13640 242 L 242
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-230 |
2.68e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 97.69 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD--QGRVLIDQQDVTHQPMHGRARA 78
Cdd:PRK13549 3 EYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GIGYLPQEASIFRKLSVADNIMAILETRKD--LDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAP 156
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLV 230
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDII 236
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-195 |
4.00e-23 |
|
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: 92.81 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDV-THQPMHGRARAGIGY 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPqeaSIFRKLSVADNIMAILEtrkdlDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:TIGR01189 81 LP---GLKPELSALENLHFWAA-----IHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|....
gi 764533248 163 EPFAGVDPISVGDIKQIIH-HLKNKGIgVLITDH 195
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRaHLARGGI-VLLTTH 185
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-169 |
4.11e-23 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 94.00 E-value: 4.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThQPMHGRaragiGY 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE-GPGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELESL----LQEFHISHIrdslgMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLkkvgLEGAEKRYI-----WQLSGGQRQRVGIARALAANPQL 149
|
170
....*....|.
gi 764533248 159 ILLDEPFAGVD 169
Cdd:PRK11248 150 LLLDEPFGALD 160
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-231 |
4.41e-23 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 97.16 E-value: 4.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYL 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNI-MAILETRKD------------------LDRAGRHRELESLLQEFHISHirdslgmslsggeRR 144
Cdd:PRK09700 86 YQELSVIDELTVLENLyIGRHLTKKVcgvniidwremrvraammLLRVGLKVDLDEKVANLSISH-------------KQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 145 RVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
|
....*..
gi 764533248 225 LANQLVK 231
Cdd:PRK09700 233 SNDDIVR 239
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-224 |
8.98e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 8.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 20 RDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYLP---QEASIFRKLSVA 96
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 97 DNIMAILETRKD--LDRAGRHRELESLLQEFHI--SHIRDSLGmSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS 172
Cdd:PRK15439 360 WNVCALTHNRRGfwIKPARENAVLERYRRALNIkfNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 764533248 173 VGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
1.06e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 92.67 E-value: 1.06e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVK-----ADQGRVLIDQQDVTHQPM-HG 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDViEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 75 RARAGIGY-LPQ---EASIFRKLSVADNIMAILETRKDL-DRAGRHRELESLLQEfhishIRDSLGM---SLSGGERRRV 146
Cdd:PRK14247 81 RRRVQMVFqIPNpipNLSIFENVALGLKLNRLVKSKKELqERVRWALEKAQLWDE-----VKDRLDApagKLSGGQQQRL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITdHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFPQQAARISDYVAFLYKGQIVEWGPTREVFT 234
|
.
gi 764533248 227 N 227
Cdd:PRK14247 235 N 235
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-219 |
1.18e-22 |
|
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: 90.84 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSY--KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVthQPMHGRARAGIG 81
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPV--SDLEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRklsvadnimailetrkdldragrhrelesllqefhiSHIRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03247 79 VLNQRPYLFD------------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 162 DEPFAGVDPISVGDI-KQIIHHLKNKGIgVLITDHNVreTLDICETAYIVNDGQLIAEG 219
Cdd:cd03247 123 DEPTVGLDPITERQLlSLIFEVLKDKTL-IWITHHLT--GIEHMDKILFLENGKIIMQG 178
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-235 |
1.29e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 93.26 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKS-RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG-RARAGI 80
Cdd:PRK13647 4 IIEVEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFrKLSVADNImAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13647 84 VFQDPDDQVF-SSTVWDDV-AFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGtAEEILAN-QLVKEVYL 235
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDeDIVEQAGL 236
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-220 |
1.34e-22 |
|
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: 91.70 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 17 QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGYLPQEASIFrklsva 96
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-DLRSSLTIIPQDPTLF------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 97 dniMAILetRKDLDRAGRHRELEsllqefhishIRDSL-----GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPI 171
Cdd:cd03369 95 ---SGTI--RSNLDPFDEYSDEE----------IYGALrvsegGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 764533248 172 SVGDIKQIIHHLKNkGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGT 220
Cdd:cd03369 160 TDALIQKTIREEFT-NSTILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-231 |
2.10e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 2.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYK--SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGI 80
Cdd:PRK13635 5 IIRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW-DVRRQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEA-SIFRKLSVADNIMAILETRKdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:PRK13635 84 GMVFQNPdNQFVGATVQDDVAFGLENIG-VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 160 LLDEPFAGVDPISVGDIKQIIHHLKN-KGIGVLITDHnvretlDICETAY-----IVNDGQLIAEGTAEEI--LANQLVK 231
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITH------DLDEAAQadrviVMNKGEILEEGTPEEIfkSGHMLQE 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-202 |
2.57e-22 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 92.07 E-value: 2.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKS-----RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRAR 77
Cdd:COG1101 1 MLELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AgIGYLPQEASI--FRKLSVADNiMAILETRkdldraGRHRELESLLQEFHISHIRD---SLGM-----------SLSGG 141
Cdd:COG1101 81 Y-IGRVFQDPMMgtAPSMTIEEN-LALAYRR------GKRRGLRRGLTKKRRELFREllaTLGLglenrldtkvgLLSGG 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 142 ERRRVEIARALATAPKFILLDEPFAGVDPISVGDI----KQIIhhlKNKGIGVLITDHNVRETLD 202
Cdd:COG1101 153 QRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVleltEKIV---EENNLTTLMVTHNMEQALD 214
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-233 |
2.77e-22 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 94.87 E-value: 2.77e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGL--VKADQGRVL-------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 62 --------IDQQDV----THQPMHGRARAGIGYLPQEA-SIFRKLSVADNIMAILE-----TRKDLDRAGRhrelesLLQ 123
Cdd:TIGR03269 81 pcpvcggtLEPEEVdfwnLSDKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEeigyeGKEAVGRAVD------LIE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 124 EFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDI-KQIIHHLKNKGIGVLITDHNVRETLD 202
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhNALEEAVKASGISMVLTSHWPEVIED 234
|
250 260 270
....*....|....*....|....*....|...
gi 764533248 203 ICETAYIVNDGQLIAEGTAEEILAN--QLVKEV 233
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEVVAVfmEGVSEV 267
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-226 |
3.53e-22 |
|
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: 91.14 E-value: 3.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 14 KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGrARAGIGYLPQEASIFRKl 93
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNIM--AILETRKDLDRAGR----HRELESLLQEFHiSHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:cd03251 91 TVAENIAygRPGATREEVEEAARaanaHEFIMELPEGYD-TVIGER-GVKLSGGQRQRIAIARALLKDPPILILDEATSA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 168 VDPISVGDIKQIIHHLKnKGIGVLITDH---NVRETLDICetayIVNDGQLIAEGTAEEILA 226
Cdd:cd03251 169 LDTESERLVQAALERLM-KNRTTFVIAHrlsTIENADRIV----VLEDGKIVERGTHEELLA 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-169 |
3.55e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 3.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaraGI 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNiMAI---LETRKDLDRAGRHRELESLLQefhISHIRDSLGMSLSGGERRRVEIARALATAPK 157
Cdd:PRK11000 78 GMVFQSYALYPHLSVAEN-MSFglkLAGAKKEEINQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170
....*....|..
gi 764533248 158 FILLDEPFAGVD 169
Cdd:PRK11000 154 VFLLDEPLSNLD 165
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-227 |
3.83e-22 |
|
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: 91.06 E-value: 3.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 12 SYKSR---QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRaRAGIGYLPQEAS 88
Cdd:cd03249 9 RYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEPV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 89 IFrKLSVADNIM-----AILETRKDLDR-AGRHRELESLLQEFHiSHIRDSlGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03249 88 LF-DGTIAENIRygkpdATDEEVEEAAKkANIHDFIMSLPDGYD-TLVGER-GSQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 163 EPFAGVDPISVGDIKQIIHHLKnKGIGVLITDHNVrETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:cd03249 165 EATSALDAESEKLVQEALDRAM-KGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQ 227
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-227 |
4.43e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 92.07 E-value: 4.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAIlKAQHLAKSYKSR-----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGR 75
Cdd:PRK13651 1 MQI-KVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 76 ARAGIGYLPQEASIFRKLSVADNI------------MAILET--RKD---------------LDRAGRHRELESLLQEFh 126
Cdd:PRK13651 80 KEKVLEKLVIQKTRFKKIKKIKEIrrrvgvvfqfaeYQLFEQtiEKDiifgpvsmgvskeeaKKRAAKYIELVGLDESY- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 127 ishirdsLGMS---LSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDI 203
Cdd:PRK13651 159 -------LQRSpfeLSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEW 231
|
250 260
....*....|....*....|....
gi 764533248 204 CETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK13651 232 TKRTIFFKDGKIIKDGDTYDILSD 255
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
2-201 |
5.67e-22 |
|
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: 90.19 E-value: 5.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSY-------KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQ----DVT-- 68
Cdd:COG4778 3 TLLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAqa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 69 --HQPMHGRARAgIGYLPQeasiFrkLSV-----ADNIMA--ILETRKDLDRAgrHRELESLLQEFHI-SHIRDSLGMSL 138
Cdd:COG4778 83 spREILALRRRT-IGYVSQ----F--LRViprvsALDVVAepLLERGVDREEA--RARARELLARLNLpERLWDLPPATF 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 139 SGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVL-IT-DHNVRETL 201
Cdd:COG4778 154 SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFhDEEVREAV 218
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-227 |
6.68e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 90.87 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTcFYMIVGLVKADQGRVLIDQQ-DVTHQPMHGRaRAGIGY 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKST-FLKCLNRMNELESEVRVEGRvEFFNQNIYER-RVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEAS-IFRK-----LSVADNI---MAILETRKDLDRAGRhreLESLLQEF----HISHIRDSLGMSLSGGERRRVEIA 149
Cdd:PRK14258 86 LRRQVSmVHPKpnlfpMSVYDNVaygVKIVGWRPKLEIDDI---VESALKDAdlwdEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 150 RALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKG-IGVLITDHNVRETLDICE-TAYIVND----GQLIAEGTAEE 223
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDfTAFFKGNenriGQLVEFGLTKK 242
|
....
gi 764533248 224 ILAN 227
Cdd:PRK14258 243 IFNS 246
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-195 |
7.22e-22 |
|
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: 89.47 E-value: 7.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQpmHGRARAGIGYL 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ--RDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAIletRKDLDRAGrhreLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFW---HADHSDEQ----VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|...
gi 764533248 164 PFAGVDPISVGDIKQII-HHLKNKGIGVLITDH 195
Cdd:cd03231 152 PTTALDKAGVARFAEAMaGHCARGGMVVLTTHQ 184
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
19-222 |
1.15e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 90.33 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpmhGRARAGIGYLPQEASI---FRKLsV 95
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ----ALQKNLVAYVPQSEEVdwsFPVL-V 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNIM-------AILETRKDLDRAGRHRELESL-LQEFHISHIRDslgmsLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:PRK15056 98 EDVVMmgryghmGWLRRAKKRDRQIVTAALARVdMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 168 VDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNdGQLIAEGTAE 222
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTE 226
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-227 |
1.90e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.11 E-value: 1.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPM---HGRARAGIGYLPQEASIFRKlSVAD 97
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsDIRKKVGLVFQYPEYQLFEE-TIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 NImAI------LETRKDLDRAGRHRELESLLQEfhisHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPI 171
Cdd:PRK13637 104 DI-AFgpinlgLSEEEIENRVKRAMNIVGLDYE----DYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 172 SVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK13637 179 GRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-227 |
2.73e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 2.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 13 YKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQ-----GRVLIDQQDVTHQPMHG-RARAGIGYLPQE 86
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPiEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 87 ASIFRKLSVADNIM------AILETRKDLDRAGRHRELESLLQEFHISHIRDSLGmSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK14267 94 PNPFPHLTIYDNVAigvklnGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPS-NLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITdHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-231 |
2.91e-21 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 91.71 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 9 LAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQEAS 88
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 89 IFRKLSVADNIMAILETRKDL--DRAGRHRELESLLQEFHIS-HIRDSLGmSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYPTKGMfvDQDKMYRDTKAIFDELDIDiDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 166 AGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVK 231
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMDKIIA 228
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
2.96e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 2.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQ--VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGI 80
Cdd:PRK13648 7 IIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE-KLRKHI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQE------ASIFrKLSVADNIMAILETRKDLdragrHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALAT 154
Cdd:PRK13648 86 GIVFQNpdnqfvGSIV-KYDVAFGLENHAVPYDEM-----HRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 155 APKFILLDEPFAGVDPISVGDIKQIIHHLK-NKGIGVLITDHNVRETLdicETAYIV--NDGQLIAEGTAEEILANQ 228
Cdd:PRK13648 160 NPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAM---EADHVIvmNKGTVYKEGTPTEIFDHA 233
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
7-197 |
3.40e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 88.63 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQdvthqpmhgrarAGIGYLPQE 86
Cdd:PRK09544 8 ENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LRIGYVPQK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 87 ASIfrklsvaDNIMAILETRKDLDRAGRHR-ELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK09544 76 LYL-------DTTLPLTVNRFLRLRPGTKKeDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|...
gi 764533248 166 AGVDPISVGDIKQIIHHLKNK-GIGVLITDHNV 197
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
16-196 |
6.35e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 86.85 E-value: 6.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThqpmHGRARAGIGYLPQEASIFRKLSV 95
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID----DPDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNimaiLETRKDLdRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGD 175
Cdd:PRK13539 91 AEN----LEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|..
gi 764533248 176 IKQII-HHLKNKGIgVLITDHN 196
Cdd:PRK13539 166 FAELIrAHLAQGGI-VIAATHI 186
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-234 |
8.43e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 87.68 E-value: 8.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 22 VSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAdQGRVLIDQQDVTHQPMHGRARAGiGYLPQEAS------IFR--KL 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHR-AYLSQQQTppfampVFQylTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNimaileTRKDlDRAGRHRELESLLQefhishIRDSLGMS---LSGGERRRVEIA-------RALATAPKFILLDE 163
Cdd:PRK03695 93 HQPDK------TRTE-AVASALNEVAEALG------LDDKLGRSvnqLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVY 234
Cdd:PRK03695 160 PMNSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-226 |
9.60e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 87.44 E-value: 9.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 11 KSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIdqqdvthqpmHGRARA----GIGYLPQe 86
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV----------NGRVSAllelGAGFHPE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 87 asifrkLSVADNIM---AIL-ETRKDLDRagRHRELEsllqEFhiSHIRDSLGM---SLSGGERRRVEIARALATAPKFI 159
Cdd:COG1134 103 ------LTGRENIYlngRLLgLSRKEIDE--KFDEIV----EF--AELGDFIDQpvkTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 160 LLDEpfagVdpISVGDI------KQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:COG1134 169 LVDE----V--LAVGDAafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-228 |
1.17e-20 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.06 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDV-THQPMHGRArAGIGYLPQEasifRK----- 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLA-NGIVYISED----RKrdglv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 --LSVADNiMAILETRK------DLDRAGRHRELESLLQEFHI-SHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK10762 343 lgMSVKEN-MSLTALRYfsraggSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 164 PFAGVDpisVG---DIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEilANQ 228
Cdd:PRK10762 422 PTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQ--ATQ 484
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-229 |
1.65e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.39 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQG------RVLIDQQDVTHQPMHGRaraGIGYLPQEASIFRKLS 94
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFDAEKGICLPPEKR---RIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNI---MAiletRKDLDragrhrELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVD-P 170
Cdd:PRK11144 93 VRGNLrygMA----KSMVA------QFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlP 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 171 ISvgdiKQIIHHL----KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQL 229
Cdd:PRK11144 163 RK----RELLPYLerlaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSA 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-227 |
3.31e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.69 E-value: 3.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCF------------YMIVGLVKADqGRVLIDQQDVTHqp 71
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmndkvsgYRYSGDVLLG-GRSIFNYRDVLE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 72 mhgrARAGIGYLPQEASIFrKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHI-SHIRDSLGMS---LSGGERRRVE 147
Cdd:PRK14271 99 ----FRRRVGMLFQRPNPF-PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKgIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-228 |
3.68e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.21 E-value: 3.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQ-----VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIdqQDVTHQPMHGRAR 77
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AGIGYLPQEASIFRKL------------------SVADNIM--------AILETRKdldRAGRHRELESLLQEFhishiR 131
Cdd:PRK13631 99 LITNPYSKKIKNFKELrrrvsmvfqfpeyqlfkdTIEKDIMfgpvalgvKKSEAKK---LAKFYLNKMGLDDSY-----L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 132 DSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVN 211
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMD 250
|
250
....*....|....*..
gi 764533248 212 DGQLIAEGTAEEILANQ 228
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQ 267
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-227 |
4.41e-20 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 85.79 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVT--------------H 69
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 70 QPMHGRARAGIGYlpQEASIFRKLSVADNIMAILETRKDLDRA-GRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEI 148
Cdd:PRK10619 86 QLRLLRTRLTMVF--QHFNLWSHMTVLENVMEAPIQVLGLSKQeARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 149 ARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-236 |
5.08e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.78 E-value: 5.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDV---THQPMHGRARAGIGYLPQEASIFRKLSV 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNIMAILETRKDLDRAGRHRELESLLQeFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGD 175
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQ-VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 176 IKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEIL---ANQLVKEVYLG 236
Cdd:PRK10070 203 MQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpANDYVRTFFRG 267
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-228 |
5.65e-20 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 5.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSYKSR---QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVT---HQPMHGRaragI 80
Cdd:TIGR00958 482 QDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydHHYLHRQ----V 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKlSVADNIMAILeTRKDLDR-------AGRHRELESLLQEFHIShiRDSLGMSLSGGERRRVEIARALA 153
Cdd:TIGR00958 558 ALVGQEPVLFSG-SVRENIAYGL-TDTPDEEimaaakaANAHDFIMEFPNGYDTE--VGEKGSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 154 TAPKFILLDEPFAGVDpisvGDIKQIIHHLKN-KGIGVLITDHNvretLDICETA---YIVNDGQLIAEGTAEEILANQ 228
Cdd:TIGR00958 634 RKPRVLILDEATSALD----AECEQLLQESRSrASRTVLLIAHR----LSTVERAdqiLVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
2-171 |
5.74e-20 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 88.26 E-value: 5.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AIlKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARagIG 81
Cdd:NF033858 266 AI-EARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRR--VG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNIMaiLETRK-DLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:NF033858 343 YMSQAFSLYGELTVRQNLE--LHARLfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170
....*....|.
gi 764533248 161 LDEPFAGVDPI 171
Cdd:NF033858 421 LDEPTSGVDPV 431
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
17-228 |
5.84e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 87.96 E-value: 5.84e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 17 QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmHGRARAGIGYLPQEASIFRKlSVA 96
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAALRQAISVVSQRVHLFSA-TLR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 97 DNIMAILETRKD--LDRAGRHRELESLLQEfhishiRDSL-------GMSLSGGERRRVEIARA-LATAPkFILLDEPFA 166
Cdd:PRK11160 432 DNLLLAAPNASDeaLIEVLQQVGLEKLLED------DKGLnawlgegGRQLSGGEQRRLGIARAlLHDAP-LLLLDEPTE 504
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 167 GVDPISVGDIKQIIH-HLKNKGIgVLITdHNVR--ETLD-ICetayIVNDGQLIAEGTAEEILANQ 228
Cdd:PRK11160 505 GLDAETERQILELLAeHAQNKTV-LMIT-HRLTglEQFDrIC----VMDNGQIIEQGTHQELLAQQ 564
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
4-234 |
5.91e-20 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.81 E-value: 5.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIGYL 83
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILETRKDLDRAGRHRELESL---LQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK10253 87 AQNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVtkaMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVY 234
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-215 |
8.48e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 85.11 E-value: 8.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQdvthqPMHgRARAGIGYL 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLA-EAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMaiLETRKDLdragRHRELESLlqefhishirDSLGMS---------LSGGERRRVEIARALAT 154
Cdd:PRK11247 87 FQDARLLPWKKVIDNVG--LGLKGQW----RDAALQAL----------AAVGLAdranewpaaLSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 155 APKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-224 |
1.24e-19 |
|
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: 87.76 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYK--SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQG-------RVLIDQQDVtHQPMh 73
Cdd:TIGR01257 1937 ILRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGdatvagkSILTNISDV-HQNM- 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 74 graragiGYLPQeasifrklsvADNIMAILETRKDLDRAGRHR-----ELESL----LQEFHISHIRDSLGMSLSGGERR 144
Cdd:TIGR01257 2015 -------GYCPQ----------FDAIDDLLTGREHLYLYARLRgvpaeEIEKVanwsIQSLGLSLYADRLAGTYSGGNKR 2077
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 145 RVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:TIGR01257 2078 KLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-232 |
2.79e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 86.12 E-value: 2.79e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIM-AILETRKD-LDRAGRHRELESLLQEfhishirdsLGM---------SLSGGERRRVEIA 149
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYlGQLPHKGGiVNRRLLNYEAREQLEH---------LGVdidpdtplkYLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 150 RALATAPKFILLDEPfagVDPISVGDIKQ---IIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTA-EEIL 225
Cdd:PRK11288 153 KALARNARVIAFDEP---TSSLSAREIEQlfrVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDmAQVD 229
|
....*..
gi 764533248 226 ANQLVKE 232
Cdd:PRK11288 230 RDQLVQA 236
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-226 |
3.23e-19 |
|
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: 85.92 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGrARAGIGYLPQEASIFRKlS 94
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS-LRRQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNImaileTRKDLDRAGRHRELESL----LQEFhISHIRDSL-------GMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:TIGR02203 422 IANNI-----AYGRTEQADRAEIERALaaayAQDF-VDKLPLGLdtpigenGVLLSGGQRQRLAIARALLKDAPILILDE 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 164 PFAGVDPISVGDIKQIIHHLKnKGIGVLITDHNVrETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:TIGR02203 496 ATSALDNESERLVQAALERLM-QGRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
22-218 |
5.88e-19 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 84.96 E-value: 5.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 22 VSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQ---EASIFRKLSVADN 98
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 99 ImAILETRKDLdRAG--RHRELESLLQEFHISHI------RDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDp 170
Cdd:PRK11288 352 I-NISARRHHL-RAGclINNRWEAENADRFIRSLniktpsREQLIMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGID- 428
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 764533248 171 isVG---DIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:PRK11288 429 --VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
16-234 |
9.46e-19 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 9.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIGYLPQEASIFRKLSV 95
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VAYLPQQLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADnIMAI--LETRKDLDRAGR--HRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPI 171
Cdd:PRK10575 103 RE-LVAIgrYPWHGALGRFGAadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIA 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 172 SVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLVKEVY 234
Cdd:PRK10575 182 HQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
2-199 |
9.63e-19 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 81.68 E-value: 9.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIG 81
Cdd:PRK10247 6 PLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE-IYRQQVS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKlSVADNIMAILETRKDldrAGRHRELESLLQEFHI-SHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK10247 85 YCAQTPTLFGD-TVYDNLIFPWQIRNQ---QPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRE 199
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDE 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-181 |
1.01e-18 |
|
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: 81.75 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSR---QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThQPMHGRARAG 79
Cdd:cd03248 11 IVKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQEASIFRKlSVADNIMAILETRKDL------DRAGRHRELESLLQEFHIShiRDSLGMSLSGGERRRVEIARALA 153
Cdd:cd03248 90 VSLVGQEPVLFAR-SLQDNIAYGLQSCSFEcvkeaaQKAHAHSFISELASGYDTE--VGEKGSQLSGGQKQRVAIARALI 166
|
170 180
....*....|....*....|....*...
gi 764533248 154 TAPKFILLDEPFAGVDPISVGDIKQIIH 181
Cdd:cd03248 167 RNPQVLILDEATSALDAESEQQVQQALY 194
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-226 |
1.02e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.79 E-value: 1.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 13 YKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLI---DQQDVTHqpmhgRARAG--IGYLPQ-- 85
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlggDMADARH-----RRAVCprIAYMPQgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 86 EASIFRKLSVADNImailetrkD-------LDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:NF033858 86 GKNLYPTLSVFENL--------DffgrlfgQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 159 ILLDEPFAGVDPIS-------VGDIKQiihhlKNKGIGVLITdhnvretldiceTAYI-----------VNDGQLIAEGT 220
Cdd:NF033858 158 LILDEPTTGVDPLSrrqfwelIDRIRA-----ERPGMSVLVA------------TAYMeeaerfdwlvaMDAGRVLATGT 220
|
....*.
gi 764533248 221 AEEILA 226
Cdd:NF033858 221 PAELLA 226
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-195 |
1.03e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.00 E-value: 1.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQ-PMHGRARAGIGY 82
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPqeaSIFRKLSVADNIMAILETRKDLDRAGRHRELESL-LQEFhishiRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:PRK13538 82 QP---GIKTELTALENLRFYQRLHGPGDDEALWEALAQVgLAGF-----EDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 764533248 162 DEPFAGVDPISVGDIKQII-HHLKNKGIgVLITDH 195
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLaQHAEQGGM-VILTTH 187
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-195 |
1.11e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 84.33 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTT-----CFYMIVGLVKadQGRVLIDQQDVTHQPMHGRAragiGYLPQEASIF 90
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKGVKG--SGSVLLNGMPIDAKEMRAIS----AYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 RKLSVAD--NIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSL------GMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:TIGR00955 112 PTLTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|...
gi 764533248 163 EPFAGVDPISVGDIKQIIHHLKNKGIGVLITDH 195
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-226 |
1.14e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 82.52 E-value: 1.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 17 QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPM-----HGRARAGIGYLPQEASIFR 91
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 92 KlSVADNI--------MAILETRkdlDRAGRhrelesLLQEFHIShiRDSLGMS---LSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13646 101 D-TVEREIifgpknfkMNLDEVK---NYAHR------LLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 161 LDEPFAGVDPISVGDIKQIIHHLK---NKGIgVLITdHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:PRK13646 169 LDEPTAGLDPQSKRQVMRLLKSLQtdeNKTI-ILVS-HDMNEVARYADEVIVMKEGSIVSQTSPKELFK 235
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-163 |
1.41e-18 |
|
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: 84.10 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGrARAGIGYLPQEASIFRKlSV 95
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS-LRAAIGIVPQDTVLFND-TI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNImailetrkdldRAGR----HRELESLLQEFHISHIRDSL-----------GMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG5265 449 AYNI-----------AYGRpdasEEEVEAAARAAQIHDFIESLpdgydtrvgerGLKLSGGEKQRVAIARTLLKNPPILI 517
|
...
gi 764533248 161 LDE 163
Cdd:COG5265 518 FDE 520
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-225 |
1.50e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG-----RARAGIGYLPQEASIFRKLSV 95
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvRKKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNIMAILE---TRKDLDR-AGRHRELESLLQEFHishirDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPI 171
Cdd:PRK13643 104 KDVAFGPQNfgiPKEKAEKiAAEKLEMVGLADEFW-----EKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 764533248 172 SVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEIL 225
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-193 |
2.47e-18 |
|
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: 83.45 E-value: 2.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSY-KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLidqqdvthqPMHGrarAGIGYLPQ 85
Cdd:TIGR03719 8 NRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR---------PQPG---IKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 86 EASIFRKLSVADNIM-AILETRKDLDR------------------AGRHRELESLLQ-----------EFHISHIR---- 131
Cdd:TIGR03719 76 EPQLDPTKTVRENVEeGVAEIKDALDRfneisakyaepdadfdklAAEQAELQEIIDaadawdldsqlEIAMDALRcppw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 132 DSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQiihHLKN-KGIGVLIT 193
Cdd:TIGR03719 156 DADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEyPGTVVAVT 215
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-182 |
3.79e-18 |
|
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: 79.85 E-value: 3.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 18 VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGYLPQEASIFRKlSVad 97
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-DLRSRISIIPQDPVLFSG-TI-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 nimailetRKDLDRAGRH--RELESLLQEFHISHIRDSL-----------GMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd03244 95 --------RSNLDPFGEYsdEELWQALERVGLKEFVESLpggldtvveegGENLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170
....*....|....*...
gi 764533248 165 FAGVDPISVGDIKQIIHH 182
Cdd:cd03244 167 TASVDPETDALIQKTIRE 184
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
19-236 |
3.89e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQEASI-FRKLSVAD 97
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 NI--------MAILETRKDLDRAgrhreleslLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVD 169
Cdd:PRK13644 98 DLafgpenlcLPPIEIRKRVDRA---------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 170 PISVGDIKQIIHHLKNKGIGVLITDHNVREtLDICETAYIVNDGQLIAEGTAEEILANQLVKevYLG 236
Cdd:PRK13644 169 PDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
16-226 |
5.73e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 82.28 E-value: 5.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVK-ADQGRVLIDQQDVTHQPMHGRARAGIGYLPQEasifRK-- 92
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPED----RKrd 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 -----LSVADNI-MAILET---RKDLDRAGRHRELESLLQEFHI--SHIRDSLGmSLSGGERRRVEIARALATAPKFILL 161
Cdd:PRK13549 351 givpvMGVGKNItLAALDRftgGSRIDDAAELKTILESIQRLKVktASPELAIA-RLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 162 DEPFAGVDpisVG---DIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIA-----EGTAEEILA 226
Cdd:PRK13549 430 DEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGdlinhNLTQEQVME 499
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-197 |
6.56e-18 |
|
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: 79.76 E-value: 6.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESG-----QIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThqpmhgraragigYLPQEASIFRKLSV 95
Cdd:cd03237 12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKPQYIKADYEGTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNIMAIletrkdLDRAGRHRELES-LLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDP---- 170
Cdd:cd03237 79 RDLLSSI------TKDFYTHPYFKTeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrl 152
|
170 180
....*....|....*....|....*..
gi 764533248 171 ISVGDIKQIIHHLKNkgiGVLITDHNV 197
Cdd:cd03237 153 MASKVIRRFAENNEK---TAFVVEHDI 176
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-236 |
8.27e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 80.17 E-value: 8.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG-----RARAGIGYLPQEASIFRKLSV 95
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 AD------NIMAILEtrkdldragrhrELESLLQE-FHISHIRDSL----GMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK13649 105 KDvafgpqNFGVSQE------------EAEALAREkLALVGISESLfeknPFELSGGQMRRVAIAGILAMEPKILVLDEP 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 165 FAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN-QLVKEVYLG 236
Cdd:PRK13649 173 TAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvDFLEEKQLG 245
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-229 |
8.28e-18 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 81.79 E-value: 8.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSY---KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVK-ADQGRVLIDQQDVTHQPMHGRARA 78
Cdd:TIGR02633 257 ILEARNLTCWDvinPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIRA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 GIGYLPQEAS---IFRKLSVADNI-MAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGM----SLSGGERRRVEIAR 150
Cdd:TIGR02633 337 GIAMVPEDRKrhgIVPILGVGKNItLSVLKSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAVLAK 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 151 ALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIA-----EGTAEEIL 225
Cdd:TIGR02633 417 MLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGdfvnhALTQEQVL 496
|
....
gi 764533248 226 ANQL 229
Cdd:TIGR02633 497 AAAL 500
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-227 |
9.10e-18 |
|
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: 81.65 E-value: 9.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQ-----------VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAdQGRVLIDQQDVTH-- 69
Cdd:COG4172 275 LLEARDLKVWFPIKRglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGls 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 70 ----QPMhgRARAGIgylpqeasIFR--------KLSVADNI---MAILETrkDLDRAGRHRELESLLQEFHIShiRDSL 134
Cdd:COG4172 354 rralRPL--RRRMQV--------VFQdpfgslspRMTVGQIIaegLRVHGP--GLSAAERRARVAEALEEVGLD--PAAR 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 135 G---MSLSGGERRRVEIARALATAPKFILLDEPFAGVDpISVGdiKQIIHHLKN----KGIG-VLITdHN---VREtldI 203
Cdd:COG4172 420 HrypHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQ--AQILDLLRDlqreHGLAyLFIS-HDlavVRA---L 492
|
250 260
....*....|....*....|....
gi 764533248 204 CETAYIVNDGQLIAEGTAEEILAN 227
Cdd:COG4172 493 AHRVMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-235 |
1.38e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 79.49 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG-----RARAGIGYLPQEASIFRKlSV 95
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklRKKVSLVFQFPEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGD 175
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 176 IKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQ-LVKEVYL 235
Cdd:PRK13641 184 MMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKeWLKKHYL 244
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
10-235 |
1.54e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 10 AKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQE--- 86
Cdd:PRK13633 17 NEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpdn 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 87 ---ASIFRKlSVA---DNI-MAILETRKDLDRAgrhreLESL-LQEF--HISHIrdslgmsLSGGERRRVEIARALATAP 156
Cdd:PRK13633 97 qivATIVEE-DVAfgpENLgIPPEEIRERVDES-----LKKVgMYEYrrHAPHL-------LSGGQKQRVAIAGILAMRP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGTAEEILAN-QLVKEVY 234
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEvEMMKKIG 242
|
.
gi 764533248 235 L 235
Cdd:PRK13633 243 L 243
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-232 |
1.87e-17 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 80.98 E-value: 1.87e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 14 KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQ---EASIF 90
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 RKLSVADNI--------------MAILETRKDLDRAGRHRELESLlqefHISHIRDSLGmSLSGGERRRVEIARALATAP 156
Cdd:PRK09700 354 PNFSIAQNMaisrslkdggykgaMGLFHEVDEQRTAENQRELLAL----KCHSVNQNIT-ELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQL------IAEGTAEEILANQLV 230
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLtqiltnRDDMSEEEIMAWALP 508
|
..
gi 764533248 231 KE 232
Cdd:PRK09700 509 QE 510
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-164 |
1.90e-17 |
|
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: 80.75 E-value: 1.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQqdvTHQpmhgraragIGY 82
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE---TVK---------LAY 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQ-------EASIFRKLSVADNIMaILETRKDLDRA--GRHrelesllqEFHISHIRDSLGMsLSGGERRRVEIARALA 153
Cdd:TIGR03719 390 VDQsrdaldpNKTVWEEISGGLDII-KLGKREIPSRAyvGRF--------NFKGSDQQKKVGQ-LSGGERNRVHLAKTLK 459
|
170
....*....|.
gi 764533248 154 TAPKFILLDEP 164
Cdd:TIGR03719 460 SGGNVLLLDEP 470
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-196 |
1.93e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 1.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQ----VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRA- 76
Cdd:PRK10535 3 ALLELKDIRRSYPSGEeqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 --RAGIGYLPQEASIFRKLSVADN-----IMAILETRKDLDRAgrhrelESLLQEFHISHIRDSLGMSLSGGERRRVEIA 149
Cdd:PRK10535 83 lrREHFGFIFQRYHLLSHLTAAQNvevpaVYAGLERKQRLLRA------QELLQRLGLEDRVEYQPSQLSGGQQQRVSIA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 764533248 150 RALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHN 196
Cdd:PRK10535 157 RALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-226 |
3.21e-17 |
|
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: 80.17 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYK-SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRARAGIGY 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH-TLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFRKlSVADNIM-------AILETRKDLDRAGRHRELESLLQEFHISHIRDslGMSLSGGERRRVEIARALATA 155
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLlgakenvSQDEIWAACEIAEIKDDIENMPLGYQTELSEE--GSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 156 PKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDiceTAYIVNDGQLIAEGTAEEILA 226
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQSD---KIIVLDHGKIIEQGSHDELLD 697
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-226 |
3.40e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 78.60 E-value: 3.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRD---VSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAg 79
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQEA-SIFRKLSVADNIMAILETrKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK13642 83 IGMVFQNPdNQFVGATVEDDVAFGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDiCETAYIVNDGQLIAEGTAEEILA 226
Cdd:PRK13642 162 IILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-227 |
3.42e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.52 E-value: 3.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQ-------PMhgRARAGIGYLPQEAS 88
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkklkPL--RKKVGIVFQFPEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 89 IFRKlSVADNI----MAILETRKD-LDRAGRHRELESLLQEfhishIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK13634 98 LFEE-TVEKDIcfgpMNFGVSEEDaKQKAREMIELVGLPEE-----LLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 164 PFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK13634 172 PTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-226 |
5.16e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.54 E-value: 5.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 11 KSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD--QGRVLIDQQDVTHQPMHGraragIGYLPQEAS 88
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR-----TGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 89 IFRKLSVADNIM--AILETRKDLDRAGRHRELESLLQEFHISH-----IRDSLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:PLN03211 151 LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHN-VRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSDAMA 296
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-173 |
5.59e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.66 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGI-- 80
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERrr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 ------GYLPQEA--SIFRKLSVADNI----MAILEtrkdldragRH-----RELESLLQEFHISHIR-DSLGMSLSGGE 142
Cdd:PRK11701 86 llrtewGFVHQHPrdGLRMQVSAGGNIgerlMAVGA---------RHygdirATAGDWLERVEIDAARiDDLPTTFSGGM 156
|
170 180 190
....*....|....*....|....*....|.
gi 764533248 143 RRRVEIARALATAPKFILLDEPFAGVDpISV 173
Cdd:PRK11701 157 QQRLQIARNLVTHPRLVFMDEPTGGLD-VSV 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
3-198 |
6.42e-17 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.78 E-value: 6.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYK----SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpMHGRARA 78
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK--LSSAAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 79 G-----IGYLPQEASIFRKLSVADNI-MAILETRKDLDRAG-RHRELESLLQEFHISHIRDSlgmSLSGGERRRVEIARA 151
Cdd:PRK11629 83 ElrnqkLGFIYQFHHLLPDFTALENVaMPLLIGKKKPAEINsRALEMLAAVGLEHRANHRPS---ELSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 764533248 152 LATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVR 198
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
18-215 |
2.36e-16 |
|
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: 76.05 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 18 VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADqGRVLIDQQDVTHQPMHgRARAGIGYLPQEASIFRKlsvad 97
Cdd:cd03289 19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQ-KWRKAFGVIPQKVFIFSG----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 nimailETRKDLDRAGRHRE-----------LESLLQEF--HISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd03289 92 ------TFRKNLDPYGKWSDeeiwkvaeevgLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 764533248 165 FAGVDPISVGDIKQIIHHlKNKGIGVLITDHNVRETLDiCETAYIVNDGQL 215
Cdd:cd03289 166 SAHLDPITYQVIRKTLKQ-AFADCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
3-234 |
2.46e-16 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 75.45 E-value: 2.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVG--LVKADQGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKdldRAGRHRELESLlqEFH--ISHIRDSLGMS-----------LSGGERRRVE 147
Cdd:CHL00131 87 FLAFQYPIEIPGVSNADFLRLAYNSKR---KFQGLPELDPL--EFLeiINEKLKLVGMDpsflsrnvnegFSGGEKKRNE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVReTLDICETAY--IVNDGQLIAEGTAEeiL 225
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQR-LLDYIKPDYvhVMQNGKIIKTGDAE--L 238
|
....*....
gi 764533248 226 ANQLVKEVY 234
Cdd:CHL00131 239 AKELEKKGY 247
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-219 |
2.90e-16 |
|
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: 74.88 E-value: 2.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 10 AKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIdqqdvthqpmHGRARA----GIGYLPQ 85
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV----------RGRVSSllglGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 86 easifrkLSVADNI---MAILETRKDLDRAGRHRELE-SLLQEFHISHIRdslgmSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03220 99 -------LTGRENIylnGRLLGLSRKEIDEKIDEIIEfSELGDFIDLPVK-----TYSSGMKARLAFAIATALEPDILLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 162 DEPFAgvdpisVGDI------KQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03220 167 DEVLA------VGDAafqekcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
15-163 |
2.99e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 77.31 E-value: 2.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIGYLPQEASIFRKlS 94
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRN-IAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 95 VADNI------MAILETRKDLDRAGRHRELESLLQEFHiSHIRDSlGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK13657 425 IEDNIrvgrpdATDEEMRAAAERAQAHDFIERKPDGYD-TVVGER-GRQLSGGERQRLAIARALLKDPPILILDE 497
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-195 |
3.78e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 74.22 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 13 YKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThqpmhgRARAGigYLPQEASIFRK 92
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK------KDLCT--YQKQLCFVGHR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 LSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS 172
Cdd:PRK13540 83 SGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|...
gi 764533248 173 VGDIKQIIHHLKNKGIGVLITDH 195
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-169 |
7.79e-16 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 75.26 E-value: 7.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSR-QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpMHGRARaG 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADR-D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQEASIFRKLSVADNI--------MAILETRKDLDRAGRHRELESLLqefhishirDSLGMSLSGGERRRVEIARA 151
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMayglkirgMPKAEIEERVAEAARILELEPLL---------DRKPRELSGGQRQRVAMGRA 148
|
170
....*....|....*...
gi 764533248 152 LATAPKFILLDEPFAGVD 169
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLD 166
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
2-203 |
9.91e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 73.34 E-value: 9.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPmhgRARAgIG 81
Cdd:PRK13543 10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD---RSRF-MA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKLSVADNIMAILETRkdldraGRH--RELESLLQEFHISHIRDSLGMSLSGGERRRVEIARA-LATAPKF 158
Cdd:PRK13543 86 YLGHLPGLKADLSTLENLHFLCGLH------GRRakQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLW 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 764533248 159 iLLDEPFAGVDPISVGDIKQIIH-HLKNKGiGVLITDHNVRETLDI 203
Cdd:PRK13543 160 -LLDEPYANLDLEGITLVNRMISaHLRGGG-AALVTTHGAYAAPPV 203
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-228 |
1.38e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 74.27 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 17 QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMH----GRARAGIGYLPQ--EASIF 90
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikevKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 RKLSVADNIMAILETRKDLDRAgrHRELESLLQefHISHIRDSLGMS---LSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:PRK13645 105 QETIEKDIAFGPVNLGENKQEA--YKKVPELLK--LVQLPEDYVKRSpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 168 VDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQ 242
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
11-214 |
1.70e-15 |
|
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: 72.50 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 11 KSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLidqqdvthqpMHGRaragIGYLPQEASIF 90
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS----------VPGS----IAYVSQEPWIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 RkLSVADNIMAILETRKDldragRHRE------LESLLQEFH---ISHIRDSlGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03250 79 N-GTIRENILFGKPFDEE-----RYEKvikacaLEPDLEILPdgdLTEIGEK-GINLSGGQKQRISLARAVYSDADIYLL 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 162 DEPFAGVDPiSVGD--IKQ-IIHHLKNKGIGVLITdHNVrETLDICETAYIVNDGQ 214
Cdd:cd03250 152 DDPLSAVDA-HVGRhiFENcILGLLLNNKTRILVT-HQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-230 |
1.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQ---VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgRAR 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVW-DIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AGIGYLPQEA-SIFRKLSVADNIMAILETrKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAP 156
Cdd:PRK13650 81 HKIGMVFQNPdNQFVGATVEDDVAFGLEN-KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 157 KFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVREtLDICETAYIVNDGQLIAEGTAEEILA--NQLV 230
Cdd:PRK13650 160 KIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFSrgNDLL 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-164 |
2.44e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 74.77 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLI---------DQQdvthqpmh 73
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvDQS-------- 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 74 graRAGigyLPQEASIFRKLSVADNIMAIletrkdldraGRhRELESllqefhishiRDSLGM-------------SLSG 140
Cdd:PRK11819 396 ---RDA---LDPNKTVWEEISGGLDIIKV----------GN-REIPS----------RAYVGRfnfkggdqqkkvgVLSG 448
|
170 180
....*....|....*....|....
gi 764533248 141 GERRRVEIARALATAPKFILLDEP 164
Cdd:PRK11819 449 GERNRLHLAKTLKQGGNVLLLDEP 472
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-234 |
2.71e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.94 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD--------QGRVLIDQQDVTH--QPM 72
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAidAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 73 HGRARAgigYLPQEASIFRKLSVADniMAILETRKDLDRAG--RHRELESLLQEFHISHIRDSLG---MSLSGGERRRVE 147
Cdd:PRK13547 81 LARLRA---VLPQAAQPAFAFSARE--IVLLGRYPHARRAGalTHRDGEIAWQALALAGATALVGrdvTTLSGGELARVQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 148 IARALA---------TAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIA 217
Cdd:PRK13547 156 FARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250
....*....|....*..
gi 764533248 218 EGTAEEILANQLVKEVY 234
Cdd:PRK13547 236 HGAPADVLTPAHIARCY 252
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-223 |
2.89e-15 |
|
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: 74.44 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 9 LAKSYKsrqvvrDVSLSIESGQI-----VGLLGPNGAGKTTCFYMIVGLVKADQGRVlidQQDVThqpmhgraragIGYL 83
Cdd:COG1245 347 LTKSYG------GFSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK-----------ISYK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAILEtrkdlDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:COG1245 407 PQYISPDYDGTVEEFLRSANT-----DDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 764533248 164 PFAGVD---PISVGdiKQIIHHLKNKGIGVLITDHNVrETLDICETAYIVNDGQLIAEGTAEE 223
Cdd:COG1245 482 PSAHLDveqRLAVA--KAIRRFAENRGKTAMVVDHDI-YLIDYISDRLMVFEGEPGVHGHASG 541
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
14-228 |
4.77e-15 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 73.90 E-value: 4.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 14 KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMhGRARAGIGYLPQEASIFRKl 93
Cdd:PRK11176 354 KEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL-ASLRNQVALVSQNVHLFND- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNIMAILE---TRKDLDRAGRhrelESLLQEFhISHIRDSL-------GMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK11176 432 TIANNIAYARTeqySREQIEEAAR----MAYAMDF-INKMDNGLdtvigenGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 164 PFAGVDPISVGDIKQIIHHL-KNKgiGVLITDHNVrETLDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:PRK11176 507 ATSALDTESERAIQAALDELqKNR--TSLVIAHRL-STIEKADEILVVEDGEIVERGTHAELLAQN 569
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
5.43e-15 |
|
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: 73.57 E-value: 5.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKS----RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGL----VKADQGRVLIDQQDVTHQP- 71
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDLLGLSe 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 72 -----MHGRAragIGYLPQE--ASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGM---SLSGG 141
Cdd:COG4172 84 relrrIRGNR---IAMIFQEpmTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 142 ERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVL-ITdHN---VREtldICETAYIVNDGQLI 216
Cdd:COG4172 161 QRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLlIT-HDlgvVRR---FADRVAVMRQGEIV 236
|
250
....*....|.
gi 764533248 217 AEGTAEEILAN 227
Cdd:COG4172 237 EQGPTAELFAA 247
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-197 |
8.73e-15 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 72.92 E-value: 8.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 9 LAKSYKsrqvvrDVSLSIESGQI-----VGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQdvthqpmhgraragIGYL 83
Cdd:PRK13409 346 LTKKLG------DFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK--------------ISYK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQEASIFRKLSVADNIMAIletrkdLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK13409 406 PQYIKPDYDGTVEDLLRSI------TDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 479
|
170 180 190
....*....|....*....|....*....|....*..
gi 764533248 164 PFAGVD---PISVGdiKQIIHHLKNKGIGVLITDHNV 197
Cdd:PRK13409 480 PSAHLDveqRLAVA--KAIRRIAEEREATALVVDHDI 514
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
3-169 |
1.06e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 70.58 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQ----VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRA-- 76
Cdd:PRK10584 6 IVEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAkl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 RA-GIGYLPQEASIFRKLSVADNIMAILETRKDLDRAGRHRELEsLLQEFHISHIRDSLGMSLSGGERRRVEIARALATA 155
Cdd:PRK10584 86 RAkHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKA-LLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164
|
170
....*....|....
gi 764533248 156 PKFILLDEPFAGVD 169
Cdd:PRK10584 165 PDVLFADEPTGNLD 178
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-228 |
1.41e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 72.70 E-value: 1.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 18 VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAgIGYLPQEASIFRKlsvad 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG----- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 nimailETRKDLDRAGRHRELEsLLQEFHISHIRDSL--------------GMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PLN03232 1325 ------TVRFNIDPFSEHNDAD-LWEALERAHIKDVIdrnpfgldaevsegGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 164 PFAGVDPISVGDIKQIIHHlKNKGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
16-205 |
1.79e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 1.79e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVlidqqdvthQPMHGrarAGIGYLPQEASIFRKLSV 95
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA---------RPAPG---IKVGYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNIM-AILETRKDLDR------------------AGRHRELESLLQ-------EFHISHIRDSLGM--------SLSGG 141
Cdd:PRK11819 88 RENVEeGVAEVKAALDRfneiyaayaepdadfdalAAEQGELQEIIDaadawdlDSQLEIAMDALRCppwdakvtKLSGG 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 142 ERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQiihHLKN-KGIGVLITdHNvRETLD-----ICE 205
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQ---FLHDyPGTVVAVT-HD-RYFLDnvagwILE 232
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-224 |
2.25e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 71.29 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVkADQGRV----LIDQQDVTHQPMH--GRARAgigylPQEASIFRK 92
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNLPEKelNKLRA-----EQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 --------LSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGM---SLSGGERRRVEIARALATAPKFILL 161
Cdd:PRK09473 106 pmtslnpyMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 162 DEPFAGVDPISVGDIKQIIHHLK---NKGIgVLITdHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKrefNTAI-IMIT-HDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-228 |
5.69e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.64 E-value: 5.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLA-KSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAdQGRVLIDQQDVTHQPMhGRARAGIGY 82
Cdd:PRK11174 350 IEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDP-ESWRKHLSW 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQEASIFrKLSVADNImaiLETRKDLDRAgrhrELESLLQEFHISHIRDSL-----------GMSLSGGERRRVEIARA 151
Cdd:PRK11174 428 VGQNPQLP-HGTLRDNV---LLGNPDASDE----QLQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 152 LATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITdHNVrETLDICETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQL-EDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-202 |
5.93e-14 |
|
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: 70.71 E-value: 5.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSYKS--RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADqGRVLIDQ---QDVTHQpmhgRARAGIG 81
Cdd:TIGR01271 1221 QGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGvswNSVTLQ----TWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASIFRKlsvadnimailETRKDLDRAGRHRE-----------LESLLQEF--HISHIRDSLGMSLSGGERRRVEI 148
Cdd:TIGR01271 1296 VIPQKVFIFSG-----------TFRKNLDPYEQWSDeeiwkvaeevgLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCL 1364
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 764533248 149 ARALATAPKFILLDEPFAGVDPISVGDIKQIIHHlKNKGIGVLITDHNVRETLD 202
Cdd:TIGR01271 1365 ARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQ-SFSNCTVILSEHRVEALLE 1417
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-223 |
1.50e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 69.43 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTcFYMIV-----GlvKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQEasif 90
Cdd:NF040905 273 RKVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMSVfgrsyG--RNISGTVFKDGKEVDVSTVSDAIDAGLAYVTED---- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 91 RK---LSVADNI-----MAILetrKDLDRAG---RHREL---ESLLQEFHI-SHIRDSLGMSLSGGERRRVEIARALATA 155
Cdd:NF040905 346 RKgygLNLIDDIkrnitLANL---GKVSRRGvidENEEIkvaEEYRKKMNIkTPSVFQKVGNLSGGNQQKVVLSKWLFTD 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 156 PKFILLDEPFAGVDpisVG---DIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEE 223
Cdd:NF040905 423 PDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGELPREE 490
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-197 |
2.58e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSY-KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpMHGRA----R 77
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITR--LKNREvpflR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AGIGYLPQEASIFRKLSVADNIMAIL----ETRKDLdragrHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALA 153
Cdd:PRK10908 79 RQIGMIFQDHHLLMDRTVYDNVAIPLiiagASGDDI-----RRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVV 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 764533248 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNV 197
Cdd:PRK10908 154 NKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-224 |
2.90e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 2.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTcfymivGLVKADqgrvlIDQQDVTHQP-------MHGRA 76
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAH-----V*GPDAGRRPwrf*twcANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 -RAGIG-YLPQEASIFRKLSVADNIMAIlETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALAT 154
Cdd:NF000106 83 lRRTIG*HRPVR*GRRESFSGRENLYMI-GR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
102-230 |
3.03e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.50 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 102 ILETRKDLDRAgrhrelESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIH 181
Cdd:PRK10938 106 IQDEVKDPARC------EQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLA 179
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 764533248 182 HLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILANQLV 230
Cdd:PRK10938 180 SLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALV 228
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
16-202 |
3.08e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 68.30 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQivGLL--GPNGAGKTTCFYMIVGLVKADQGRVlidqqdvtHQPMHGRaragIGYLPQEAsifrKL 93
Cdd:COG4178 376 RPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGAR----VLFLPQRP----YL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNIMAIL--ETRKDLDRAgrhrELESLLQEFHISHIRDSL------GMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:COG4178 438 PLGTLREALLypATAEAFSDA----ELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEAT 513
|
170 180 190
....*....|....*....|....*....|....*...
gi 764533248 166 AGVDPISVGDI-KQIIHHLknKGIGVLITDHnvRETLD 202
Cdd:COG4178 514 SALDEENEAALyQLLREEL--PGTTVISVGH--RSTLA 547
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-226 |
3.44e-13 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 68.19 E-value: 3.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKS----RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGL-----VKADQGRVLIDQQDVTHQP 71
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 72 mHGRARAGIGylPQEASIFRKLSVADNIMAILETRK----DLDRAGRHR----ELESLLQEFHISHIRDSLG---MSLSG 140
Cdd:PRK15134 83 -EQTLRGVRG--NKIAMIFQEPMVSLNPLHTLEKQLyevlSLHRGMRREaargEILNCLDRVGIRQAAKRLTdypHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 141 GERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQN 239
|
....*..
gi 764533248 220 TAEEILA 226
Cdd:PRK15134 240 RAATLFS 246
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-202 |
1.23e-12 |
|
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: 63.71 E-value: 1.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVlidqqdvtHQPmhgrARAGIGYLPQEASIFRkls 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMP----EGEDLLFLPQRPYLPL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 vadnimailetrkdldraGRHRELesllqefhishIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:cd03223 78 ------------------GTLREQ-----------LIYPWDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESED 128
|
170 180
....*....|....*....|....*...
gi 764533248 175 DIKQIihhLKNKGIGVLITDHnvRETLD 202
Cdd:cd03223 129 RLYQL---LKELGITVISVGH--RPSLW 151
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
3-229 |
1.24e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.58 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSR---------QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMH 73
Cdd:PRK15112 4 LLEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 74 GRARAgIGYLPQEASifRKLSVADNIMAILET----RKDLDRAGRHRELESLLQEFHI--SHIRDSLGMsLSGGERRRVE 147
Cdd:PRK15112 84 YRSQR-IRMIFQDPS--TSLNPRQRISQILDFplrlNTDLEPEQREKQIIETLRQVGLlpDHASYYPHM-LAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
...
gi 764533248 227 NQL 229
Cdd:PRK15112 240 SPL 242
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
15-169 |
1.47e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 66.73 E-value: 1.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLidqqdvthqpmhgrARAGIGYLPQEASIFRKlS 94
Cdd:PTZ00243 672 PKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQAWIMNA-T 736
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNIMAILETR-KDLDRAGRHRELESLLQ------EFHISHirdsLGMSLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:PTZ00243 737 VRGNILFFDEEDaARLADAVRVSQLEADLAqlggglETEIGE----KGVNLSGGQKARVSLARAVYANRDVYLLDDPLSA 812
|
..
gi 764533248 168 VD 169
Cdd:PTZ00243 813 LD 814
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-226 |
1.50e-12 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 66.89 E-value: 1.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 18 VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGrARAGIGYLPQEASIFRKlsvad 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLFSG----- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 nimailETRKDLDRAGRHRElESLLQEFHISHIRDSL--------------GMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:TIGR00957 1375 ------SLRMNLDPFSQYSD-EEVWWALELAHLKTFVsalpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 164 PFAGVDpISVGDIKQIIHHLKNKGIGVLITDHNVRETLDIceTAYIVNDGQLIAE-GTAEEILA 226
Cdd:TIGR00957 1448 ATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY--TRVIVLDKGEVAEfGAPSNLLQ 1508
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-225 |
2.36e-12 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 65.91 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLakSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGY 82
Cdd:PRK10982 250 ILEVRNL--TSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 83 LPQE---ASIFRKLSVADN-IMAILETRKDLDRAGRHRELESLLQEF----------HISHIRdslgmSLSGGERRRVEI 148
Cdd:PRK10982 328 VTEErrsTGIYAYLDIGFNsLISNIRNYKNKVGLLDNSRMKSDTQWVidsmrvktpgHRTQIG-----SLSGGNQQKVII 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 149 ARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQL-----IAEGTAEE 223
Cdd:PRK10982 403 GRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVagivdTKTTTQNE 482
|
..
gi 764533248 224 IL 225
Cdd:PRK10982 483 IL 484
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-201 |
2.66e-12 |
|
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: 65.93 E-value: 2.66e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 18 VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDqqdvthqpmhgrARAGIGYLPQEASIFRKlSVAD 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------AKGKLFYVPQRPYMTLG-TLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 NIMAILETRKDLDRAGRHRELESLLQEFHISHI-RDSLGMS--------LSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:TIGR00954 534 QIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHIlEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECTSAV 613
|
170 180 190
....*....|....*....|....*....|....
gi 764533248 169 DPisvgDIKQ-IIHHLKNKGIGVLITDHnvRETL 201
Cdd:TIGR00954 614 SV----DVEGyMYRLCREFGITLFSVSH--RKSL 641
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-227 |
2.77e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.77 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVG-LVKADQGRVLIdqqdvthqpmhgraRAGIGYLPQEASIFRKl 93
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVI--------------RGSVAYVPQVSWIFNA- 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNIMaiLETRKDLDRAGRHRELESLLQEFHISHIRD-----SLGMSLSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:PLN03232 694 TVRENIL--FGSDFESERYWRAIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 169 DPISVGDI--KQIIHHLKNKgIGVLITdhNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PLN03232 772 DAHVAHQVfdSCMKDELKGK-TRVLVT--NQLHFLPLMDRIILVSEGMIKEEGTFAELSKS 829
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-227 |
6.36e-12 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 64.16 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQ----VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGL------VKADqgRVLIDQQDVTHQ 70
Cdd:COG4170 1 MPLLDIRNLTIEIDTPQgrvkAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhVTAD--RFRWNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 71 PMHGRaRAGIG------------YLPQEASIFRKLSvaDNIMAILETRKDLDRAG-RHRELESLLQEFHI---SHIRDSL 134
Cdd:COG4170 79 SPRER-RKIIGreiamifqepssCLDPSAKIGDQLI--EAIPSWTFKGKWWQRFKwRKKRAIELLHRVGIkdhKDIMNSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 135 GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDG 213
Cdd:COG4170 156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCG 235
|
250
....*....|....
gi 764533248 214 QLIAEGTAEEILAN 227
Cdd:COG4170 236 QTVESGPTEQILKS 249
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-195 |
6.92e-12 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 62.67 E-value: 6.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThqpmhgraragigyLPQEASIFRKLSV 95
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--------------FGREASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 ADNIMAILETrkdLDRAGrHRELESLLQEFHishirdslgmSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGD 175
Cdd:COG2401 109 KGDFKDAVEL---LNAVG-LSDAVLWLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174
|
170 180
....*....|....*....|.
gi 764533248 176 IKQIIHHL-KNKGIGVLITDH 195
Cdd:COG2401 175 VARNLQKLaRRAGITLVVATH 195
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-226 |
7.03e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 7.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 17 QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAdQGRVLIDQQdvthqPMHG---------RARAGIGYLPQEA 87
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDGQ-----PLHNlnrrqllpvRHRIQVVFQDPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 88 SIFRKLSVADNIMAILET-RKDLDRAGRHRELESLLQEFHIS-HIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 166 AGVDPISVGDIKQIIHHLKNK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
14-184 |
8.26e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.57 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 14 KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQ---PMHgRARAGIGYLPQE--AS 88
Cdd:PRK15079 32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMkddEWR-AVRSDIQMIFQDplAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 89 IFRKLSVADNIMAILET-RKDLDRAGRHRELESLL--------------QEFhishirdslgmslSGGERRRVEIARALA 153
Cdd:PRK15079 111 LNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMlkvgllpnlinrypHEF-------------SGGQCQRIGIARALI 177
|
170 180 190
....*....|....*....|....*....|.
gi 764533248 154 TAPKFILLDEPFAGVDpisVGDIKQIIHHLK 184
Cdd:PRK15079 178 LEPKLIICDEPVSALD---VSIQAQVVNLLQ 205
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-228 |
1.31e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.99 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 18 VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHqpmHGRA--RAGIGYLPQEASIFRKlsv 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK---FGLMdlRKVLGIIPQAPVLFSG--- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 96 adnimailETRKDLDRAGRHR--ELESLLQEFHISHI--RDSLGM---------SLSGGERRRVEIARALATAPKFILLD 162
Cdd:PLN03130 1328 --------TVRFNLDPFNEHNdaDLWESLERAHLKDVirRNSLGLdaevseageNFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 163 EPFAGVDPISVGDIKQIIHHlKNKGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-224 |
1.37e-11 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 63.22 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSRQV----VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAdQGRVL-----IDQQDVTHQP 71
Cdd:PRK11022 1 MALLNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMaekleFNGQDLQRIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 72 MHGRAR---AGIGYLPQEA--SIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGM---SLSGGER 143
Cdd:PRK11022 80 EKERRNlvgAEVAMIFQDPmtSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 144 RRVEIARALATAPKFILLDEPFAGVDpisVGDIKQIIHHL------KNKGIgVLITdHNVRETLDICETAYIVNDGQLIA 217
Cdd:PRK11022 160 QRVMIAMAIACRPKLLIADEPTTALD---VTIQAQIIELLlelqqkENMAL-VLIT-HDLALVAEAAHKIIVMYAGQVVE 234
|
....*..
gi 764533248 218 EGTAEEI 224
Cdd:PRK11022 235 TGKAHDI 241
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-227 |
1.41e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.41 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKT-TCFYMIVGL---VKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQEAsiFR 91
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPRSA--FN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 92 KL-SVADNimaILETRKDLDRAGRHRELESLLQEFHISHIRDSLGM---SLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:PRK10418 94 PLhTMHTH---ARETCLALGKPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 168 VDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK10418 171 LDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-224 |
1.53e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 63.34 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 17 QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRV-------------LIDQQDVTHQPMHGRARAGIGYL 83
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQE--ASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQEFHISHIRDSLGM---SLSGGERRRVEIARALATAPKF 158
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEI 224
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-176 |
1.66e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.78 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 18 VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVlidqqdvTHQpmhGRaragIGYLPQEASIFRKlSVAD 97
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------KHS---GR----ISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 NIMAIL---ETR-KDLDRAGRHRELESLLQEFHISHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISV 173
Cdd:TIGR01271 506 NIIFGLsydEYRyTSVIKACQLEEDIALFPEKDKTVLGEG-GITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTE 584
|
...
gi 764533248 174 GDI 176
Cdd:TIGR01271 585 KEI 587
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-228 |
1.89e-11 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 63.51 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 56 DQGRVLIDQQDVTHQPMHGrARAGIGYLPQEASIFrKLSVADNIMAILE--TRKDLDRAGRHRELESLLQEFHISHIRD- 132
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLF-NMSIYENIKFGKEdaTREDVKRACKFAAIDEFIESLPNKYDTNv 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 133 -SLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVN 211
Cdd:PTZ00265 1353 gPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFN 1432
|
170 180
....*....|....*....|..
gi 764533248 212 D----GQLI-AEGTAEEILANQ 228
Cdd:PTZ00265 1433 NpdrtGSFVqAHGTHEELLSVQ 1454
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
16-164 |
3.76e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 62.28 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTcfymivgLVKadqgrVLIDQQdvthQPMHGRARAG----IGYLPQ-EASIF 90
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTT-------LLK-----LMLGQL----QADSGRIHCGtkleVAYFDQhRAELD 395
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 91 RKLSVADNIMailETRKDLDRAGRHRELESLLQEFHISHIRdslGMS----LSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK11147 396 PEKTVMDNLA---EGKQEVMVNGRPRHVLGYLQDFLFHPKR---AMTpvkaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-228 |
7.16e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 7.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTH-QPMHGRARAGIgyLPQEASIFRKl 93
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAV--VSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNImAILE---TRKDLDRAGR----HRELESLLQEFHIShiRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:PRK10789 404 TVANNI-ALGRpdaTQQEIEHVARlasvHDDILRLPQGYDTE--VGERGVMLSGGQKQRISIARALLLNAEILILDDALS 480
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 167 GVDpisvGDIK-QIIHHLKNKGIG--VLITDHNVRETLDICETaYIVNDGQLIAEGTAEEiLANQ 228
Cdd:PRK10789 481 AVD----GRTEhQILHNLRQWGEGrtVIISAHRLSALTEASEI-LVMQHGHIAQRGNHDQ-LAQQ 539
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-183 |
8.02e-11 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 59.58 E-value: 8.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD---QGRVLIDqqDVTHQPMHGRARAGIGYLPQEasifrk 92
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYN--GIPYKEFAEKYPGEIIYVSEE------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 lsvaDNIMAILETRKDLDRAGRHRELESllqefhishIRdslgmSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS 172
Cdd:cd03233 92 ----DVHFPTLTVRETLDFALRCKGNEF---------VR-----GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSST 153
|
170
....*....|.
gi 764533248 173 VGDIKQIIHHL 183
Cdd:cd03233 154 ALEILKCIRTM 164
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
115-224 |
1.28e-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: 60.80 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 115 HRELESLLqEFHISHIRdsLGMS---LSGGERRRVEIARAL---ATAPKFILLDEPFAGvdpISVGDIKQ---IIHHLKN 185
Cdd:TIGR00630 807 SRKLQTLC-DVGLGYIR--LGQPattLSGGEAQRIKLAKELskrSTGRTLYILDEPTTG---LHFDDIKKlleVLQRLVD 880
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 764533248 186 KGIGVLITDHNvretLDICETA-YIV--------NDGQLIAEGTAEEI 224
Cdd:TIGR00630 881 KGNTVVVIEHN----LDVIKTAdYIIdlgpeggdGGGTVVASGTPEEV 924
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-196 |
2.18e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.92 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 27 ESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRV--------LIDQ------QDVTHQPMHGRARAGIGylPQEASIFRK 92
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeILDEfrgselQNYFTKLLEGDVKVIVK--PQYVDLIPK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 lSVADNIMAILETRKDLDRagrhreLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEpfagvdPIS 172
Cdd:cd03236 102 -AVKGKVGELLKKKDERGK------LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE------PSS 168
|
170 180 190
....*....|....*....|....*....|
gi 764533248 173 VGDIKQ------IIHHLKNKGIGVLITDHN 196
Cdd:cd03236 169 YLDIKQrlnaarLIRELAEDDNYVLVVEHD 198
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-164 |
3.16e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 59.52 E-value: 3.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQdvthqpmhgrarAGIGYL 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN------------ANIGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 84 PQE-ASIFRK-LSVADnIMAILETRKDLDRAGRHrELESLLqeFHISHIRDSLGmSLSGGERRRVEIARALATAPKFILL 161
Cdd:PRK15064 388 AQDhAYDFENdLTLFD-WMSQWRQEGDDEQAVRG-TLGRLL--FSQDDIKKSVK-VLSGGEKGRMLFGKLMMQKPNVLVM 462
|
...
gi 764533248 162 DEP 164
Cdd:PRK15064 463 DEP 465
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
14-195 |
4.07e-10 |
|
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: 57.25 E-value: 4.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 14 KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMI-----VGLVKadqGRVLIDQQ--DVTHQPmhgraraGIGYLPQE 86
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLagrktAGVIT---GEILINGRplDKNFQR-------STGYVEQQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 87 ASIFRKLSVadnimailetrkdldragrhreLESLlqEFHiSHIRDslgmsLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:cd03232 88 DVHSPNLTV----------------------REAL--RFS-ALLRG-----LSVEQRKRLTIGVELAAKPSILFLDEPTS 137
|
170 180
....*....|....*....|....*....
gi 764533248 167 GVDPISVGDIKQIIHHLKNKGIGVLITDH 195
Cdd:cd03232 138 GLDSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-227 |
6.30e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 6.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVG-LVKADQGRVLIdqqdvthqpmhgraRAGIGYLPQEASIFRKlS 94
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI--------------RGTVAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 VADNIMAILE---TR--KDLDRAGRHRELEsLLQEFHISHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEPFAGVD 169
Cdd:PLN03130 695 VRDNILFGSPfdpERyeRAIDVTALQHDLD-LLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 170 PiSVGDI---KQIIHHLKNKgIGVLITdhNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PLN03130 773 A-HVGRQvfdKCIKDELRGK-TRVLVT--NQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-169 |
6.51e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.94 E-value: 6.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 18 VVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRvlidqqdVTHQpmhGRaragIGYLPQEASIFRKlSVAD 97
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-------IKHS---GR----ISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 98 NIMAIL---ETR-KDLDRAGRHRELESLLQEFHISHIRDSlGMSLSGGERRRVEIARALATAPKFILLDEPFAGVD 169
Cdd:cd03291 117 NIIFGVsydEYRyKSVVKACQLEEDITKFPEKDNTVLGEG-GITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-164 |
9.50e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.04 E-value: 9.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 24 LSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLID--------QQDvthQPMHGRAR------AGIGYLPQEASI 89
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqdlivarlQQD---PPRNVEGTvydfvaEGIEEQAEYLKR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 90 FRKLSvadNIMAILETRKDLDRAGR------HRELESLlqEFHISHIRDSLGM-------SLSGGERRRVEIARALATAP 156
Cdd:PRK11147 101 YHDIS---HLVETDPSEKNLNELAKlqeqldHHNLWQL--ENRINEVLAQLGLdpdaalsSLSGGWLRKAALGRALVSNP 175
|
....*...
gi 764533248 157 KFILLDEP 164
Cdd:PRK11147 176 DVLLLDEP 183
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-216 |
1.05e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 57.88 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKAD--QGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKLSVADNIMAILETRKD--LDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKF 158
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLI 216
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-228 |
1.06e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.81 E-value: 1.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 7 QHLAKSYKS-RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVThQPMHGRARAGIGYLPQ 85
Cdd:PRK10790 344 DNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 86 EASIfrklsVADNIMAILETRKDLDRAGRHRELESL-LQEFhISHIRDSL-------GMSLSGGERRRVEIARALATAPK 157
Cdd:PRK10790 423 DPVV-----LADTFLANVTLGRDISEEQVWQALETVqLAEL-ARSLPDGLytplgeqGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 158 FILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITdHNVRETLDiCETAYIVNDGQLIAEGTAEEILANQ 228
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVE-ADTILVLHRGQAVEQGTHQQLLAAQ 565
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-226 |
1.11e-09 |
|
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: 58.03 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 22 VSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIdqqdvthqpmhgraRAGIGYLPQEASIfRKLSVADNIMa 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--------------KGSVAYVPQQAWI-QNDSLRENIL- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 102 ileTRKDLDRAGRHRELE--SLLQEFHISHIRDSL-----GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPiSVG 174
Cdd:TIGR00957 721 ---FGKALNEKYYQQVLEacALLPDLEILPSGDRTeigekGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-HVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 175 diKQIIHH-------LKNKgIGVLITdHNVrETLDICETAYIVNDGQLIAEGTAEEILA 226
Cdd:TIGR00957 797 --KHIFEHvigpegvLKNK-TRILVT-HGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-194 |
1.14e-09 |
|
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: 56.57 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVL---IDQQDVTHQPMHGRARAGIGYLPQEASIFRKlSVAD 97
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 98 NImaILETRKDLDRAGRHRELESLLQEFHISHIRDSL-----GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDpIS 172
Cdd:cd03290 98 NI--TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTeigerGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-IH 174
|
170 180
....*....|....*....|..
gi 764533248 173 VGDikqiihHLKNKGIGVLITD 194
Cdd:cd03290 175 LSD------HLMQEGILKFLQD 190
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-227 |
1.24e-09 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 57.73 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 138 LSGGERRRVEIARALA---TAPKFILLDEP-----FAgvdpisvgDIKQ---IIHHLKNKGIGVLITDHNvretLDICET 206
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPttglhFH--------DIRKlleVLHRLVDKGNTVVVIEHN----LDVIKT 894
|
90 100 110
....*....|....*....|....*....|
gi 764533248 207 A-YIV--------NDGQLIAEGTAEEILAN 227
Cdd:COG0178 895 AdWIIdlgpeggdGGGEIVAEGTPEEVAKV 924
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
115-237 |
1.24e-09 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 57.78 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 115 HRELEsLLQEFHISHIRdsLGMS---LSGGERRRVEIARAL---ATAPKFILLDEPFAGvdpISVGDIKQ---IIHHLKN 185
Cdd:PRK00349 808 ARKLQ-TLVDVGLGYIK--LGQPattLSGGEAQRVKLAKELskrSTGKTLYILDEPTTG---LHFEDIRKlleVLHRLVD 881
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 764533248 186 KGIGVLITDHNvretLDICETA-YIV--------NDGQLIAEGTAEEILANqlvKEVYLGH 237
Cdd:PRK00349 882 KGNTVVVIEHN----LDVIKTAdWIIdlgpeggdGGGEIVATGTPEEVAKV---EASYTGR 935
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
15-227 |
5.77e-09 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 56.02 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 15 SRQV--VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQ------DVTHQPMhgraRAGIGYLPQE 86
Cdd:PRK10261 334 TREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQridtlsPGKLQAL----RRDIQFIFQD 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 87 --ASIFRKLSVADNIMAILETRKDLDRAGRHRELESLLQE--------FHISHirdslgmSLSGGERRRVEIARALATAP 156
Cdd:PRK10261 410 pyASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERvgllpehaWRYPH-------EFSGGQRQRICIARALALNP 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 157 KFILLDEPFAGVDpisVGDIKQIIHHL----KNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEILAN 227
Cdd:PRK10261 483 KVIIADEAVSALD---VSIRGQIINLLldlqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-173 |
7.17e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSY--------KSRQV--VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQ 70
Cdd:PRK11308 3 QPLLQAIDLKKHYpvkrglfkPERLVkaLDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 71 PMHGRARagigyLPQEASIfrklsVADNIMAILETRK--------------DLDRAGRHRELESLLQ------EF----- 125
Cdd:PRK11308 83 DPEAQKL-----LRQKIQI-----VFQNPYGSLNPRKkvgqileepllintSLSAAERREKALAMMAkvglrpEHydryp 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 764533248 126 HIshirdslgmsLSGGERRRVEIARALATAPKFILLDEPFAGVDpISV 173
Cdd:PRK11308 153 HM----------FSGGQRQRIAIARALMLDPDVVVADEPVSALD-VSV 189
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-226 |
1.25e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 54.42 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 1 MAILKAQHLAKSYKSR----QVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKaDQGRVLIDQ---QDVTHQPMH 73
Cdd:PRK15093 1 MPLLDIRNLTIEFKTSdgwvKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTK-DNWRVTADRmrfDDIDLLRLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 74 GRARagigylpqeasifRKLsVADNI-MAILETRKDLD---RAG----------------------RHRELESLLQEFHI 127
Cdd:PRK15093 80 PRER-------------RKL-VGHNVsMIFQEPQSCLDpseRVGrqlmqnipgwtykgrwwqrfgwRKRRAIELLHRVGI 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 128 SHIRD---SLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KNKGIGVLITDHNVRETLDI 203
Cdd:PRK15093 146 KDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQW 225
|
250 260
....*....|....*....|...
gi 764533248 204 CETAYIVNDGQLIAEGTAEEILA 226
Cdd:PRK15093 226 ADKINVLYCGQTVETAPSKELVT 248
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
2-169 |
2.26e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.34 E-value: 2.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 2 AILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMI----VGLVKADQGRVLIDqqDVTHQPMHGRAR 77
Cdd:TIGR00956 60 RGFRKLKKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYD--GITPEEIKKHYR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AGIGYLPQEASIFRKLSVADNI-----MAILETR-KDLDRAGRHRELESL-LQEFHISHIRDS-----LGMSLSGGERRR 145
Cdd:TIGR00956 138 GDVVYNAETDVHFPHLTVGETLdfaarCKTPQNRpDGVSREEYAKHIADVyMATYGLSHTRNTkvgndFVRGVSGGERKR 217
|
170 180
....*....|....*....|....
gi 764533248 146 VEIARALATAPKFILLDEPFAGVD 169
Cdd:TIGR00956 218 VSIAEASLGGAKIQCWDNATRGLD 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-195 |
2.95e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 2.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMI-----VGLVKAD----QGRVL----------IDQQDVtHQPmHGRA 76
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLaervtTGVITGGdrlvNGRPLdssfqrsigyVQQQDL-HLP-TSTV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 77 RAGIGY-----LPQEASIFRKLSVADNIMAILEtrkdldragrhreLESLlqefhishiRDSL----GMSLSGGERRRVE 147
Cdd:TIGR00956 854 RESLRFsaylrQPKSVSKSEKMEYVEEVIKLLE-------------MESY---------ADAVvgvpGEGLNVEQRKRLT 911
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 764533248 148 IARALATAPKFIL-LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDH 195
Cdd:TIGR00956 912 IGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-170 |
9.87e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.90 E-value: 9.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHgraragiGYLPQEASIFRKLSVADN 98
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-------DYRKLFSAVFTDFHLFDQ 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 764533248 99 IMAILETRKD-------LDRAGRHRELEslLQEFHISHIRdslgmsLSGGERRRVEIARALATAPKFILLDEPFAGVDP 170
Cdd:PRK10522 412 LLGPEGKPANpalvekwLERLKMAHKLE--LEDGRISNLK------LSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-195 |
1.02e-07 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 52.09 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 27 ESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVL--IDQQDVThqpmhgRARAGIG---YlpqeasiFRKLSvADNIMA 101
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeePSWDEVL------KRFRGTElqdY-------FKKLA-NGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 102 IL--------------ETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFag 167
Cdd:COG1245 163 AHkpqyvdlipkvfkgTVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS-- 240
|
170 180 190
....*....|....*....|....*....|....
gi 764533248 168 vdpiSVGDIKQ------IIHHLKNKGIGVLITDH 195
Cdd:COG1245 241 ----SYLDIYQrlnvarLIRELAEEGKYVLVVEH 270
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
137-220 |
1.11e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 51.08 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 137 SLSGGERRRVEIARAL---ATAPKFILLDEPFAGvdpISVGDIKQ---IIHHLKNKGIGVLITDHNvretLDICETA-YI 209
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTG---LHFHDVKKlleVLQRLVDKGNTVVVIEHN----LDVIKCAdWI 241
|
90
....*....|....*....
gi 764533248 210 V--------NDGQLIAEGT 220
Cdd:cd03271 242 IdlgpeggdGGGQVVASGT 260
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-171 |
1.51e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 51.55 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 12 SYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGlvkaD--QGRvlidQQDVThqpMHGRARAG---------- 79
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpQGY----SNDLT---LFGRRRGSgetiwdikkh 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 80 IGYLPQEASI-FRKLSVADNImaILETRKD---LDRAGRHRELESLLQEFHISHIRDSLG----MSLSGGERRRVEIARA 151
Cdd:PRK10938 338 IGYVSSSLHLdYRVSTSVRNV--ILSGFFDsigIYQAVSDRQQKLAQQWLDILGIDKRTAdapfHSLSWGQQRLALIVRA 415
|
170 180
....*....|....*....|
gi 764533248 152 LATAPKFILLDEPFAGVDPI 171
Cdd:PRK10938 416 LVKHPTLLILDEPLQGLDPL 435
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-212 |
5.59e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 50.03 E-value: 5.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 14 KSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHGRARAGIGYLPQEASIFRKl 93
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSN- 474
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 94 SVADNIMAILETRKDLD-----------------------RAGRHRELESLLQ------------EFHISHIRDSLGMS- 137
Cdd:PTZ00265 475 SIKNNIKYSLYSLKDLEalsnyynedgndsqenknkrnscRAKCAGDLNDMSNttdsneliemrkNYQTIKDSEVVDVSk 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 138 -------------------------LSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLK-NKGIGVL 191
Cdd:PTZ00265 555 kvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITI 634
|
250 260
....*....|....*....|.
gi 764533248 192 ITDHNVrETLDICETAYIVND 212
Cdd:PTZ00265 635 IIAHRL-STIRYANTIFVLSN 654
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-198 |
1.74e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGL--VKADQGRVLIDQQDVTHQPMHGRARAGI 80
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 ----GYLPQEASIFRKLSVADNIMAILETRKD--LDRAGRHRELESLLQEFHISH--IRDSLGMSLSGGERRRVEIARAL 152
Cdd:PRK09580 81 fmafQYPVEIPGVSNQFFLQTALNAVRSYRGQepLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 764533248 153 ATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVR 198
Cdd:PRK09580 161 VLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQR 206
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-205 |
2.64e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 17 QVVRDVSLSIESGQIVGLLGPNGAGKTTCF----------YM-----IVGLVKADQGRVLI----DQQDVtHQPmHGRAR 77
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMdvlagrktggYIegdirISGFPKKQETFARIsgycEQNDI-HSP-QVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 78 AGIGY-----LPQEASIFRKLSVADNIMAILEtrkdldragrhreLESLlqefhishiRDSL----GMS-LSGGERRRVE 147
Cdd:PLN03140 972 ESLIYsaflrLPKEVSKEEKMMFVDEVMELVE-------------LDNL---------KDAIvglpGVTgLSTEQRKRLT 1029
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 764533248 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHnvRETLDICE 205
Cdd:PLN03140 1030 IAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIH--QPSIDIFE 1085
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-238 |
4.87e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 4.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 137 SLSGGERRRVEIARALATAPKFI--LLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNVR------ETLDICETAY 208
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQmisladRIIDIGPGAG 555
|
90 100 110
....*....|....*....|....*....|.
gi 764533248 209 IVNdGQLIAEGTAEEILAN-QLVKEVYLGHE 238
Cdd:PRK00635 556 IFG-GEVLFNGSPREFLAKsDSLTAKYLRQE 585
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-228 |
5.24e-06 |
|
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: 46.44 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 4 LKAQHLAKSYKS--RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVTHQPMHG-RARAGI 80
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 gylpqeasifrklSVADNIMAILETRKDLDRAGRHRElESLLQEFHISHIRDSL--------------GMSLSGGERRRV 146
Cdd:cd03288 100 -------------ILQDPILFSGSIRFNLDPECKCTD-DRLWEALEIAQLKNMVkslpggldavvtegGENFSVGQRQLF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 147 EIARALATAPKFILLDEPFAGVDpISVGDIKQIIHHLKNKGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGTAEEILA 226
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
..
gi 764533248 227 NQ 228
Cdd:cd03288 244 QE 245
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-195 |
5.64e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 46.73 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 29 GQIVGLLGPNGAGKTTCFYMIVGLVKADQGRV--------LIDQ------QDvthqpmhgraragigYlpqeasiFRKLS 94
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYeeepswdeVLKRfrgtelQN---------------Y-------FKKLY 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 95 vADNIMAIL--------------ETRKDLDRAGRHRELESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13409 157 -NGEIKVVHkpqyvdlipkvfkgKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 764533248 161 LDEpfagvdPISVGDIKQ------IIHHLkNKGIGVLITDH 195
Cdd:PRK13409 236 FDE------PTSYLDIRQrlnvarLIREL-AEGKYVLVVEH 269
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
214-238 |
7.26e-06 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 41.47 E-value: 7.26e-06
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-197 |
8.45e-06 |
|
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: 44.87 E-value: 8.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 26 IESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDqqdvthqpmhgraRAGIGYLPQEasifrklsvadnimailet 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-------------GITPVYKPQY------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 106 rkdldragrhrelesllqefhishirdslgMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKN 185
Cdd:cd03222 70 ------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170
....*....|...
gi 764533248 186 KGI-GVLITDHNV 197
Cdd:cd03222 120 EGKkTALVVEHDL 132
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-213 |
1.17e-05 |
|
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: 44.24 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 19 VRDVSLSIESGQIVGLLGPNGAGKTT----CFY-----MIVGLVK--ADQGRVLIDQ-QDVThqpmhgraRAGIGYLPQE 86
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTlvneGLYasgkaRLISFLPkfSRNKLIFIDQlQFLI--------DVGLGYLTLG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 87 asifRKLSvadnimailetrkdldragrhrelesllqefhishirdslgmSLSGGERRRVEIARALATAPK--FILLDEP 164
Cdd:cd03238 83 ----QKLS------------------------------------------TLSGGELQRVKLASELFSEPPgtLFILDEP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 764533248 165 FAGVDPIsvgDIKQIIHHLK---NKGIGVLITDHNVREtldICETAYIVNDG 213
Cdd:cd03238 117 STGLHQQ---DINQLLEVIKgliDLGNTVILIEHNLDV---LSSADWIIDFG 162
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-196 |
2.16e-05 |
|
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: 43.50 E-value: 2.16e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 136 MSLSGGERRRVEIARALATAPK----FILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHN 196
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-215 |
3.32e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 3.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVlidqqdvthqpmhGRARaGI-- 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAK-GIkl 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GYLPQEASIFRKlsvADNimailETRKDLDRAGrHRELESLLQE------FHISHIRDSLGmSLSGGERRRVEIARALAT 154
Cdd:PRK10636 378 GYFAQHQLEFLR---ADE-----SPLQHLARLA-PQELEQKLRDylggfgFQGDKVTEETR-RFSGGEKARLVLALIVWQ 447
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 155 APKFILLDEPFAGVDPisvgDIKQIIHH--LKNKGIGVLITD--HNVRETLDiceTAYIVNDGQL 215
Cdd:PRK10636 448 RPNLLLLDEPTNHLDL----DMRQALTEalIDFEGALVVVSHdrHLLRSTTD---DLYLVHDGKV 505
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-228 |
3.85e-05 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 44.23 E-value: 3.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 137 SLSGGERRRVEIARALATAPKFIL--LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNvRETldICETAYIVN--- 211
Cdd:TIGR00630 488 TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHD-EDT--IRAADYVIDigp 564
|
90 100
....*....|....*....|..
gi 764533248 212 -----DGQLIAEGTAEEILANQ 228
Cdd:TIGR00630 565 gagehGGEVVASGTPEEILANP 586
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-225 |
1.15e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.89 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 137 SLSGGERRRVEIARALATA---PKFILLDEPFAGvdpISVGDIKQIIH---HLKNKGIGVLITDHNVrETLDICEtaYIV 210
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTG---LHTHDIKALIYvlqSLTHQGHTVVIIEHNM-HVVKVAD--YVL 882
|
90 100
....*....|....*....|...
gi 764533248 211 N--------DGQLIAEGTAEEIL 225
Cdd:PRK00635 883 ElgpeggnlGGYLLASCSPEELI 905
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
3-195 |
1.54e-04 |
|
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 41.46 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQH-LAKSYKSRQVVRDVSLSiESGQIVGLLGPNGAGKTTCFyMIVGLVKAdqgrvlidqqdvthqpMhgrARAGIg 81
Cdd:cd03280 2 LREARHpLLPLQGEKVVPLDIQLG-ENKRVLVITGPNAGGKTVTL-KTLGLLTL----------------M---AQSGL- 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 82 YLPQEASifRKLSVADNIMAiletrkDLdraGRHRELESLLQEF--HISHIRdslgmslsggerrrvEIARAlATAPKFI 159
Cdd:cd03280 60 PIPAAEG--SSLPVFENIFA------DI---GDEQSIEQSLSTFssHMKNIA---------------RILQH-ADPDSLV 112
|
170 180 190
....*....|....*....|....*....|....*..
gi 764533248 160 LLDEPFAGVDPISVGDIKQ-IIHHLKNKGIGVLITDH 195
Cdd:cd03280 113 LLDELGSGTDPVEGAALAIaILEELLERGALVIATTH 149
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-164 |
6.64e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.54 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 16 RQVVRDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQ---DVTHQPMHGRARAGIGYLPQEASIFRK 92
Cdd:PRK10636 14 RVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNwqlAWVNQETPALPQPALEYVIDGDREYRQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 93 LSVAdniMAILETRKDLDR-AGRHRELESlLQEFHI----SHIRDSLGMS----------LSGGERRRVEIARALATAPK 157
Cdd:PRK10636 94 LEAQ---LHDANERNDGHAiATIHGKLDA-IDAWTIrsraASLLHGLGFSneqlerpvsdFSGGWRMRLNLAQALICRSD 169
|
....*..
gi 764533248 158 FILLDEP 164
Cdd:PRK10636 170 LLLLDEP 176
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
3-163 |
1.36e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 3 ILKAQHLAKSYKSRQVVrDVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDQQDVT--HQPMHGRARAGI 80
Cdd:PRK13541 1 MLSLHQLQFNIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINniAKPYCTYIGHNL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 81 GyLPQEASIFRKLSVADNIMAILETrkdldragrhreLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13541 80 G-LKLEMTVFENLKFWSEIYNSAET------------LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWL 146
|
...
gi 764533248 161 LDE 163
Cdd:PRK13541 147 LDE 149
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-225 |
3.18e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 37.87 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVlidqqdvthqPMHGRaragIGYLPQEASIFRKLSVADNI- 99
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----------DRNGE----VSVIAISAGLSGQLTGIENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 100 ---MAILETRKDLDRAGRHRELESLLQEFHISHIRdslgmSLSGGERRRVEIARALATAPKFILLDEpfagvdPISVGDI 176
Cdd:PRK13546 108 fkmLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVK-----KYSSGMRAKLGFSINITVNPDILVIDE------ALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 764533248 177 K------QIIHHLKNKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGTAEEIL 225
Cdd:PRK13546 177 TfaqkclDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-62 |
3.41e-03 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 38.33 E-value: 3.41e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 764533248 21 DVSLSIESGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLI 62
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
136-195 |
3.76e-03 |
|
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: 37.62 E-value: 3.76e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 764533248 136 MSLSGGERRRVEIARALATAPKFIL--LDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDH 195
Cdd:cd03270 136 PTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-197 |
4.52e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 4.52e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 764533248 137 SLSGGERRRVEIARALATAPK---FILLDEPFAGVDPISVGDIKQIIHHLKNKGIGVLITDHNV 197
Cdd:PRK00635 1699 SLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP 1762
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-202 |
4.65e-03 |
|
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: 36.58 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 28 SGQIVGLLGPNGAGKTTCFYMIVGLVKADQGRVLIDqqdvthqpmhgraragigylpqeasifrklsvadnimailetrk 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYI-------------------------------------------- 36
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 108 DLDRagrhreLESLLQEFHISHIRDSLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIH------ 181
Cdd:smart00382 37 DGED------ILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180
....*....|....*....|.
gi 764533248 182 HLKNKGIGVLITDHNVRETLD 202
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
88-210 |
8.11e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 37.19 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 88 SIFRKlSVADNIMAilETRKDLDRAGRHRELESLLQEFHISHIRDSLGM---SLSGGERR------RVEIARALATAPKF 158
Cdd:PRK01156 752 AMIRK-SASQAMTS--LTRKYLFEFNLDFDDIDVDQDFNITVSRGGMVEgidSLSGGEKTavafalRVAVAQFLNNDKSL 828
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 764533248 159 ILLDEPFAGVDPISVGDIKQIIHH-LKNKGI---GVLITDHnvRETLDICETAYIV 210
Cdd:PRK01156 829 LIMDEPTAFLDEDRRTNLKDIIEYsLKDSSDipqVIMISHH--RELLSVADVAYEV 882
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
136-227 |
8.86e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 36.93 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 764533248 136 MSLSGGERRRVEIARALATApkfiL------LDEPfagvdpiSVG----DIKQII---HHLKNKGIGVLITDHNvretLD 202
Cdd:COG0178 484 GTLSGGEAQRIRLATQIGSG----LvgvlyvLDEP-------SIGlhqrDNDRLIetlKRLRDLGNTVIVVEHD----ED 548
|
90 100 110
....*....|....*....|....*....|....
gi 764533248 203 ICETA-YIV--------NDGQLIAEGTAEEILAN 227
Cdd:COG0178 549 TIRAAdYIIdigpgageHGGEVVAQGTPEEILKN 582
|
|
| |
