|
Name |
Accession |
Description |
Interval |
E-value |
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-241 |
1.58e-175 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 481.84 E-value: 1.58e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRK-LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYLGEDFR 240
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGEDFR 239
|
.
6MIT_B 241 L 241
Cdd:COG1137 240 L 240
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-241 |
8.21e-174 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 477.46 E-value: 8.21e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYLGEDFR 240
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFR 240
|
.
6MIT_B 241 L 241
Cdd:PRK10895 241 L 241
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-241 |
1.97e-153 |
|
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: 425.92 E-value: 1.97e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYLGEDFRL 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 |
1.49e-142 |
|
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: 398.07 E-value: 1.49e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDlTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGL-SKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYLG 236
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-238 |
1.00e-77 |
|
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: 234.93 E-value: 1.00e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIRDD-------------LTSEQR-QDRANELMEEFHIEHLRDSLGQALSGGERRRV 146
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLVAAHARLGrgllaallrlpraRREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 147 EIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
250
....*....|...
6MIT_B 226 EDDHVKRVYLGED 238
Cdd:COG0411 242 ADPRVIEAYLGEE 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-226 |
1.22e-77 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 233.80 E-value: 1.22e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGYL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
3.87e-74 |
|
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: 224.86 E-value: 3.87e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIRDDltSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRD--RAEVRADLERVYELFPRlKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYLG 236
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-230 |
6.15e-74 |
|
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: 224.24 E-value: 6.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDLTS---------EQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAA 154
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHV 230
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-227 |
9.76e-72 |
|
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: 218.46 E-value: 9.76e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDltsEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRR---AKRKARLERVYELFPRlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-235 |
6.12e-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: 209.33 E-value: 6.12e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGYL 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYG-LFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE---DDHVKRVYL 235
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREeigEENLEDAFV 233
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
7-229 |
3.49e-63 |
|
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: 197.12 E-value: 3.49e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYLP 84
Cdd:COG1127 9 RNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelRRRIGMLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:COG1127 89 QGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDEP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDH 229
Cdd:COG1127 169 TAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-215 |
7.58e-62 |
|
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: 191.46 E-value: 7.58e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIGYL 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEP--EEVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMavlqirddltseqrqdranelmeefhiehlrdslgqaLSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03230 79 PEEPSLYENLTVRENLK-------------------------------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNL 215
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-234 |
2.75e-61 |
|
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: 192.95 E-value: 2.75e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYL 83
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDN-LMAVLQIRDDLTSEQRQDR--ANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:COG1120 81 PQEPPAPFGLTVRELvALGRYPHLGLFGRPSAEDReaVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVY 234
Cdd:COG1120 161 LDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-234 |
5.51e-60 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 189.14 E-value: 5.51e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARARRGI 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRR--LSVFDNLMAVLQIRDDLT---SEQRQDRANELMEEFHIEHLRD-SLGQaLSGGERRRVEIARALAA 154
Cdd:COG1121 78 GYVPQRAEVDWDfpITVRDVVLMGRYGRRGLFrrpSRADREAVDEALERVGLEDLADrPIGE-LSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGnLIAHGTPQQILEDDHVKRVY 234
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAY 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-227 |
6.92e-60 |
|
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: 188.31 E-value: 6.92e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGY 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQ--EASIFRRlSVFDNLM-AVLQIRddLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:COG1122 80 VFQnpDDQLFAP-TVEEDVAfGPENLG--LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:COG1122 157 VLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-229 |
7.61e-57 |
|
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: 180.78 E-value: 7.61e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLP 84
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDH 229
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-236 |
1.10e-56 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 182.23 E-value: 1.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRGIGY 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE-----PLDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVYLARLK-GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYLG 236
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLE 228
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-224 |
3.15e-56 |
|
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: 178.85 E-value: 3.15e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIG 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDR--KAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLK-GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
1.35e-54 |
|
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: 182.80 E-value: 1.35e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGR-----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-- 76
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 77 RRGIGYLPQ--EASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALA 153
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-226 |
6.55e-54 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 176.83 E-value: 6.55e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE---KRNV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMR-GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 161 LDEPFAGVDP---ISV-IDIKRIiehLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:COG3842 159 LDEPLSALDAklrEEMrEELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYE 225
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-226 |
2.88e-53 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 174.95 E-value: 2.88e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsLLPLHARaRRGIGY 82
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDL-FTNLPPR-ERRVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVR-PPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 163 EPFAGVDPISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:COG1118 159 EPFGALDAKVRKELRRwLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYD 223
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-219 |
5.31e-53 |
|
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: 170.15 E-value: 5.31e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRGIGYL 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-----PLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLK-GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
6-219 |
1.21e-52 |
|
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: 169.25 E-value: 1.21e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARARRGIGYLPQ 85
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------EKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 EASIFR--RLSVFDNLMAVLQIR----DDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:cd03235 76 RRSIDRdfPISVRDVVLMGLYGHkglfRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGnLIAHG 219
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLNRT-VVASG 213
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-219 |
3.73e-52 |
|
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: 168.08 E-value: 3.73e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYL 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE---RRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03259 157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-224 |
1.31e-49 |
|
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: 161.77 E-value: 1.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIGYLPQ 85
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 EASIFRRLSVFDNL--MAVLQirdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03265 81 DLSVDDELTGWENLyiHARLY---GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:cd03265 158 PTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-219 |
2.73e-49 |
|
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: 159.52 E-value: 2.73e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 5 TAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLP 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QeasifrrlsvfdnlmavlqirddltseqrqdraneLMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:cd03214 80 Q-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 165 FAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-213 |
3.90e-49 |
|
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: 160.33 E-value: 3.90e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLP 84
Cdd:cd03225 3 KNLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 Q--EASIFRrLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:cd03225 82 QnpDDQFFG-PTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-224 |
4.71e-49 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 162.94 E-value: 4.71e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRGIGYLPQEASIF 90
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREP--RKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 91 RRLSVFDNL--MAVLQirdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGV 168
Cdd:TIGR01188 79 EDLTGRENLemMGRLY---GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:TIGR01188 156 DPRTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-232 |
8.29e-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: 160.00 E-value: 8.29e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDltseQRQDRANELMEEFHIEH-LRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPR----RSRKIPDEIYELFPVLKeMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDhVKR 232
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDK-VRR 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-195 |
1.73e-48 |
|
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: 158.41 E-value: 1.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIG 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLMAVLQIRDDLTSEqrqDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYGLRADR---EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-230 |
1.82e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 160.26 E-value: 1.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARA 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV------TGP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 77 RRGIGYLPQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANP 156
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 157 KFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGnliahgtPQQILEDDHV 230
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVLSAR-------PGRIVEEIDV 225
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-211 |
1.42e-46 |
|
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: 154.17 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllplhARARRG 79
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV------TGPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQG-VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
6MIT_B 160 LLDEPFAGVDPISVIDIKR-IIEHLRDSGLGVLITDHNVRETLAVCERAYIVS 211
Cdd:cd03293 154 LLDEPFSALDALTREQLQEeLLDIWRETGKTVLLVTHDIDEAVFLADRVVVLS 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-225 |
2.89e-46 |
|
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: 154.00 E-value: 2.89e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGY 82
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIrDDLTSEQRQDRANELMEEFHIE--HLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKL-LKWPKEKIRERADELLALVGLDpaEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLqQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIL 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-213 |
4.22e-46 |
|
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: 151.57 E-value: 4.22e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPLHARARRGIGY 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMavlqirddltseqrqdranelmeefhiehlrdslgQALSGGERRRVEIARALAANPKFILLD 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIA-----------------------------------LGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQG 213
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-166 |
5.27e-46 |
|
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: 150.11 E-value: 5.27e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIGYLPQEASIFRRLSVFDN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL-RKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 99 LMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSL----GQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:pfam00005 80 LRLGLLLK-GLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-238 |
6.67e-46 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 153.61 E-value: 6.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMaVLQIRDDLT--------------SEQR-QDRANELMEEFHIEHLRDSLGQALSGGERRRVEI 148
Cdd:PRK11300 86 FQHVRLFREMTVIENLL-VAQHQQLKTglfsgllktpafrrAESEaLDRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
250
....*....|.
6MIT_B 228 DHVKRVYLGED 238
Cdd:PRK11300 245 PDVIKAYLGEA 255
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-238 |
7.21e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 153.29 E-value: 7.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGI 80
Cdd:COG3638 3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLM-----------AVLQIrddLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIA 149
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLagrlgrtstwrSLLGL---FPPEDRE-RALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 150 RALAANPKFILLDEPFAGVDPISvidIKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQiL 225
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKT---ARQVMDLLRRiareDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE-L 234
|
250
....*....|...
6MIT_B 226 EDDHVKRVYLGED 238
Cdd:COG3638 235 TDAVLREIYGGEA 247
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-219 |
1.31e-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: 151.37 E-value: 1.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhARARRG 79
Cdd:cd03266 2 ITADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP--AEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRLSVFDNL--MAVLQirdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLeyFAGLY---GLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-213 |
4.18e-45 |
|
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: 148.16 E-value: 4.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 5 TAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLP 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QeasifrrlsvfdnlmavlqirddltseqrqdranelmeefhiehlrdslgqaLSGGERRRVEIARALAANPKFILLDEP 164
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
8.05e-45 |
|
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: 156.99 E-value: 8.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---GNIIIDDEDISLLPLHARARR 78
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 79 gIGYLPQEA-SIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:COG1123 85 -IGMVFQDPmTQLNPVTVGDQIAEALENLG-LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-219 |
1.57e-44 |
|
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: 148.52 E-value: 1.57e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhARARRGIGYL 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN---IEALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLM---AVLQIRDdltseqrqDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:cd03268 78 IEAPGFYPNLTARENLRllaRLLGIRK--------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03268 150 LDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-234 |
1.65e-44 |
|
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: 149.26 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGI 80
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDN-LMAVL-------QIRDDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARAL 152
Cdd:cd03256 81 GMIFQQFNLIERLSVLENvLSGRLgrrstwrSLFGLFPKEEKQ-RALAALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 153 AANPKFILLDEPFAGVDPISVidiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQiLEDD 228
Cdd:cd03256 160 MQQPKLILADEPVASLDPASS---RQVMDLLKRinreEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDE 235
|
....*.
6MIT_B 229 HVKRVY 234
Cdd:cd03256 236 VLDEIY 241
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
2.99e-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: 148.80 E-value: 2.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAY----KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRg 79
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQ--EASIFRRLSVFDNLMAVLQIrddLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANP 156
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDRILAEPLRI---HGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 157 KFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAG 229
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-217 |
3.38e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 148.27 E-value: 3.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MAT-LTAKNLAKAYK----GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAR 75
Cdd:COG1136 1 MSPlLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 76 A---RRGIGYLPQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARAL 152
Cdd:COG1136 81 ArlrRRHIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNvRETLAVCERAYIVSQGNLIA 217
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVS 224
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-226 |
5.15e-44 |
|
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: 148.26 E-value: 5.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGY 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ---ERNVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIR---DDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 160 LLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYD 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-219 |
6.09e-44 |
|
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: 147.65 E-value: 6.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRG 79
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 --IGYLPQEA--SIFRRLSVFDNLMAVLQIRDDLT-SEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALA 153
Cdd:cd03257 82 keIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSkKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARALA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-219 |
1.55e-43 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 145.80 E-value: 1.55e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGeIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGYL 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNL--MAVLQirdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:cd03264 78 PQEFGVYPNFTVREFLdyIAWLK---GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 162 DEPFAGVDPISVIdikRIIEHLRDSGLG--VLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03264 155 DEPTAGLDPEERI---RFRNLLSELGEDriVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-226 |
3.73e-43 |
|
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: 145.94 E-value: 3.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKgRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGIGYL 83
Cdd:cd03299 1 LKVENLSKDWK-EFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLP---PEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDLTSEqRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKE-IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 164 PFAGVDP---ISVI-DIKRIIehlRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:cd03299 156 PFSALDVrtkEKLReELKKIR---KEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFK 219
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-215 |
5.15e-43 |
|
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: 144.94 E-value: 5.15e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKG----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 77 RRGIGYLPQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANP 156
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAG-VPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 157 KFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNvRETLAVCERAYIVSQGNL 215
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
7-196 |
5.52e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 144.81 E-value: 5.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYL 83
Cdd:COG2884 5 ENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylRRRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:COG2884 85 FQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190
....*....|....*....|....*....|...
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
Cdd:COG2884 164 PTGNLDPETSWEIMELLEEINRRGTTVLIATHD 196
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-241 |
5.70e-43 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 148.69 E-value: 5.70e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARARRgIGYLPQEA 87
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRK-VGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 88 SIFRRLSVFDNL---MAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:PRK10851 84 ALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDS--GLGVLITdHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRV--YLGEDFR 240
Cdd:PRK10851 164 FGALDAQVRKELRRWLRQLHEElkFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVleFMGEVNR 242
|
.
6MIT_B 241 L 241
Cdd:PRK10851 243 L 243
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-170 |
1.68e-42 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 147.14 E-value: 1.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGI 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLP---PKDRNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170
....*....|
6MIT_B 161 LDEPFAGVDP 170
Cdd:COG3839 157 LDEPLSNLDA 166
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
8.60e-42 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 141.49 E-value: 8.60e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYL 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE-WRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRlSVFDNLMAVLQIRDDLTSEqrqDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRERKFDR---ERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 163 EPFAGVDPISvidiKRIIEHL-----RDSGLGVLITDHNVRETLAVCERAYIVSQGNL 215
Cdd:COG4619 156 EPTSALDPEN----TRRVEELlreylAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-234 |
1.31e-41 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 142.60 E-value: 1.31e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIG 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASI---FRRLSVfdnlmaVLQIRDDLTSEQRQDRA--NELMEEFHIEHLRDSLGQALSGGERRRVEIARALA--- 153
Cdd:PRK13548 80 VLPQHSSLsfpFTVEEV------VAMGRAPHGLSRAEDDAlvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlw 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 154 ---ANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDH 229
Cdd:PRK13548 154 epdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPET 233
|
....*
6MIT_B 230 VKRVY 234
Cdd:PRK13548 234 LRRVY 238
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-234 |
2.04e-41 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 141.79 E-value: 2.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYL 83
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR-RAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASI---FRrlsvfdnlmaVLQI----RDDLTSEQRQDR--ANELMEEFHIEHLRDSLGQALSGGERRRVEIARALA- 153
Cdd:COG4559 81 PQHSSLafpFT----------VEEVvalgRAPHGSSAAQDRqiVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAq 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 154 ------ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:COG4559 151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTD 230
|
....*..
6MIT_B 228 DHVKRVY 234
Cdd:COG4559 231 ELLERVY 237
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-224 |
2.00e-39 |
|
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: 135.77 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDISLLPLHARA-R 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIPgaPDEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 RGIGYLPQEASIFRrLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHI--EHLRDSLGQALSGGERRRVEIARALAAN 155
Cdd:cd03260 81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwdEVKDRLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-226 |
5.20e-39 |
|
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: 135.06 E-value: 5.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYLPQE 86
Cdd:cd03300 4 ENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH---KRPVNTVFQN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ASIFRRLSVFDNLMAVLQIRDDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:cd03300 81 YALFPHLTVFENIAFGLRLKKLPKAEIKE-RVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 167 GVDpisvidiKRIIEHL--------RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:cd03300 160 ALD-------LKLRKDMqlelkrlqKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYE 220
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-225 |
5.94e-39 |
|
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: 135.11 E-value: 5.94e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhaRARRGIGYL 83
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPR--AALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLM--AVLQirdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:TIGR03864 80 FQQPTLDLDLSVRQNLRyhAALH---GLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVREtLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:TIGR03864 157 DEPTVGLDPASRAAITAHVRALaRDQGLSVLWATHLVDE-IEASDRLVVLHRGRVLADGAAAELR 220
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-226 |
8.01e-39 |
|
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: 142.67 E-value: 8.01e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIG 81
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-RRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRlSVFDNLMavlqIRDDLTSEQRQDRANEL--MEEFhIEHLRDSL-------GQALSGGERRRVEIARAL 152
Cdd:COG2274 553 VVLQDVFLFSG-TIRENIT----LGDPDATDEEIIEAARLagLHDF-IEALPMGYdtvvgegGSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 153 AANPKFILLDEPFAGVDPISVidiKRIIEHLRDSGLG---VLITdHNvRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:COG2274 627 LRNPRILILDEATSALDAETE---AIILENLRRLLKGrtvIIIA-HR-LSTIRLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-226 |
3.26e-38 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 134.93 E-value: 3.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllPLHAR-ARRGI 80
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV---PSRARhARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQeasifrrlsvFDNLMAVLQIRDDL---------TSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARA 151
Cdd:PRK13537 83 GVVPQ----------FDNLDPDFTVRENLlvfgryfglSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:PRK13537 153 LVNDPDVLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-213 |
4.08e-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: 130.58 E-value: 4.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGR--RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIG 81
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL-RKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRlSVFDNLmavlqirddltseqrqdranelmeefhiehlrdslgqaLSGGERRRVEIARALAANPKFILL 161
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQG 213
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIA-HRL-STIRDADRIIVLDDG 170
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-219 |
4.18e-38 |
|
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: 132.03 E-value: 4.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNsGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID-----DEDISL-LPLHaraRRGIGYLPQEASIFRRLS 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfDSRKKInLPPQ---QRKIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLMAVLQIrddLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPIS-- 172
Cdd:cd03297 92 VRENLAFGLKR---KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALrl 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
6MIT_B 173 --VIDIKRIIEHLrdsGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03297 169 qlLPELKQIKKNL---NIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-237 |
5.89e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 132.19 E-value: 5.89e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVveDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLharARRGIGYL 83
Cdd:COG3840 2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP---AERPVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLmaVLQIRDD--LTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:COG3840 77 FQENNLFPHLTVAQNI--GLGLRPGlkLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL--EDDHVKRVYLGE 237
Cdd:COG3840 154 DEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLdgEPPPALAAYLGI 232
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-237 |
1.01e-37 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 132.16 E-value: 1.01e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:COG4674 11 LYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQ--------IRDDLTSEQRqDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAAN 155
Cdd:COG4674 91 FQKPTVFEELTVFENLELALKgdrgvfasLFARLTAEER-DRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 156 PKFILLDEPFAGvdpISVIDIKRIIEHLRD--SGLGVLITDHN---VREtlaVCERAYIVSQGNLIAHGTPQQILEDDHV 230
Cdd:COG4674 170 PKLLLLDEPVAG---MTDAETERTAELLKSlaGKHSVVVVEHDmefVRQ---IARKVTVLHQGSVLAEGSLDEVQADPRV 243
|
....*..
6MIT_B 231 KRVYLGE 237
Cdd:COG4674 244 IEVYLGR 250
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-195 |
1.13e-37 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 130.68 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---GNIIIDDEDISLLPLHaraRRG 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFsasGEVLLNGRRLTALPAE---QRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRLSVFDNLMavLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLA--FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190
....*....|....*....|....*....|....*..
6MIT_B 160 LLDEPFAGVDPISVIDIKR-IIEHLRDSGLGVLITDH 195
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-226 |
1.52e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 134.96 E-value: 1.52e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYL 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY---QRPINMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQiRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 164 PFAGVDP-------ISVIDIkriiehLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:PRK11607 176 PMGALDKklrdrmqLEVVDI------LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYE 239
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
2.04e-37 |
|
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: 137.59 E-value: 2.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRG 79
Cdd:COG4987 332 PSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL-RRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRlSVFDNL-MAvlqiRDDLTSEQ-RQ--DRANelMEEFhIEHLRDSL-------GQALSGGERRRVEI 148
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLrLA----RPDATDEElWAalERVG--LGDW-LAALPDGLdtwlgegGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 149 ARALAANPKFILLDEPFAGVDPISVIDI-KRIIEHLRDSGLgVLITDHnvRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGRTV-LLITHR--LAGLERMDRILVLEDGRIVEQGTHEELLAQ 559
|
.
6MIT_B 228 D 228
Cdd:COG4987 560 N 560
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
3.89e-37 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 130.38 E-value: 3.89e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHieHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYELFPRLH--ERRIQRAGTMSGGEQQMLAIGRALMSQPRLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYLG 236
Cdd:PRK11614 161 LDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
6.32e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 129.73 E-value: 6.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-RRGIGY 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLM-AVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTlAPIKVKK-MSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNV---REtlaVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMgfaRE---VADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-169 |
1.74e-36 |
|
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: 127.76 E-value: 1.74e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGIGYL 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLP---PKDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDE-RVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
....*.
6MIT_B 164 PFAGVD 169
Cdd:cd03301 157 PLSNLD 162
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-228 |
2.39e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 129.11 E-value: 2.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQEASIFRRL 93
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 SVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
Cdd:PRK11831 100 NVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 174 IDIKRIIEHLrDSGLGV--LITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:PRK11831 180 GVLVKLISEL-NSALGVtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-238 |
3.86e-36 |
|
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: 130.61 E-value: 3.86e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE---DISL---LPLHaraRRGIGYLPQEASIFRRLS 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgifLPPH---RRRIGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLMAVlqiRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
Cdd:COG4148 94 VRGNLLYG---RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 175 DIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYLGED 238
Cdd:COG4148 171 EILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEE 235
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
13-234 |
4.02e-36 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 127.89 E-value: 4.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG-IVPRDAGNIIIDDED---ISLLPLharaRRGIGYLPQE-- 86
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGdLPPTYGNDVRLFGERrggEDVWEL----RKRIGLVSPAlq 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ASIFRRLSVFD----NLMAVLQIRDDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:COG1119 89 LRFPRDETVLDvvlsGFFDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLILD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLG--VLITdHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVY 234
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAEGAPtlVLVT-HHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSEAF 240
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
3-228 |
5.69e-36 |
|
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: 133.34 E-value: 5.69e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIG 81
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQIA 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRrLSVFDNL-MAvlqiRDDLTSEQRQD---RANelMEEFhIEHLRDSL-------GQALSGGERRRVEIAR 150
Cdd:COG4988 415 WVPQNPYLFA-GTIRENLrLG----RPDASDEELEAaleAAG--LDEF-VAALPDGLdtplgegGRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVrETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRL-ALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
8-230 |
6.04e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 129.95 E-value: 6.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 8 NLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIsllPLHAR-ARRGIGYLPQe 86
Cdd:PRK13536 46 GVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARlARARIGVVPQ- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 asifrrlsvFDNLMAVLQIRDDLTSEQRQDRAN---------ELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:PRK13536 122 ---------FDNLDLEFTVRENLLVFGRYFGMStreieavipSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILeDDHV 230
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALI-DEHI 264
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-195 |
8.23e-36 |
|
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: 126.11 E-value: 8.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-RRGIGY 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|...
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-228 |
1.12e-35 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 1.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARaRRGIGY 82
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsPRDAQ-AAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIR-----DDltSEQRQdRANELMEEFHIE-HLRDSLGQaLSGGERRRVEIARALAANP 156
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRrggliDW--RAMRR-RARELLARLGLDiDPDTPVGD-LSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 157 KFILLDEPFAgvdPISVIDIKR---IIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:COG1129 160 RVLILDEPTA---SLTEREVERlfrIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDE 231
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-234 |
1.42e-35 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 126.67 E-value: 1.42e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGY 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQ-----EASIFRRL-----SVFDNLMAVLQIRDdltsEQRQDRAnelMEEFHIEHLRDSLGQALSGGERRRVEIARAL 152
Cdd:PRK11231 81 LPQhhltpEGITVRELvaygrSPWLSLWGRLSAED----NARVNQA---MEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKR 232
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRT 233
|
..
6MIT_B 233 VY 234
Cdd:PRK11231 234 VF 235
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-225 |
2.52e-35 |
|
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: 125.39 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHAR--ARRGI 80
Cdd:cd03258 5 KNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkARRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIrDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:cd03258 85 GMIFQHFNLLSSRTVFENVALPLEI-AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 161 LDEPFAGVDPISVidiKRIIEHLRDS----GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:cd03258 164 CDEATSALDPETT---QSILALLRDInrelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVF 229
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-198 |
3.68e-35 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 125.18 E-value: 3.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvPR---DAGNIIIDDEDISLLPLHARARRGI 80
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGH-PKyevTSGSILLDGEDILELSPDERARAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYL---PQEasiFRRLSVFDNLMAVLQIR--DDLTSEQRQDRANELMEEFHI--EHLRDSLGQALSGGERRRVEIARALA 153
Cdd:COG0396 80 FLAfqyPVE---IPGVSVSNFLRTALNARrgEELSAREFLKLLKEKMKELGLdeDFLDRYVNEGFSGGEKKRNEILQMLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
6MIT_B 154 ANPKFILLDEPFAGVDpisvID----IKRIIEHLRDSGLGVLITDHNVR 198
Cdd:COG0396 157 LEPKLAILDETDSGLD----IDalriVAEGVNKLRSPDRGILIITHYQR 201
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
4.19e-35 |
|
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: 122.54 E-value: 4.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARaRRGIGY 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAsPRDAR-RAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQeasifrrlsvfdnlmavlqirddltseqrqdranelmeefhiehlrdslgqaLSGGERRRVEIARALAANPKFILLD 162
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAH 218
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-227 |
5.76e-35 |
|
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: 127.54 E-value: 5.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIS------LLPLHaraRRGIGYLPQEASIFRRLS 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFdsrkgiFLPPE---KRRIGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLmavLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
Cdd:TIGR02142 92 VRGNL---RYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
6MIT_B 175 DIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:TIGR02142 169 EILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-206 |
1.12e-34 |
|
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: 125.94 E-value: 1.12e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP---RDAGNIIIDDEDISLLPLHA-R 75
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 76 ARRG--IGYLPQE--ASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQ---ALSGGERRRVEI 148
Cdd:COG0444 82 KIRGreIQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 149 ARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRD----SGLGVL-ITdHN---VREtlaVCER 206
Cdd:COG0444 162 ARALALEPKLLIADEPTTALD---VTIQAQILNLLKDlqreLGLAILfIT-HDlgvVAE---IADR 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-215 |
1.92e-34 |
|
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: 121.77 E-value: 1.92e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAkaykGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:cd03215 5 LEVRGLS----VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 P---QEASIFRRLSVFDNLmavlqirddltseqrqdranelmeefhiehlrdSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:cd03215 81 PedrKREGLVLDLSVAENI---------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNL 215
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-220 |
4.93e-34 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 124.80 E-value: 4.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGI 80
Cdd:COG1135 5 ENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAARRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIrDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:COG1135 85 GMIFQHFNLLSSRTVAENVALPLEI-AGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 161 LDEPFAGVDPI---SVID-IKRIIEHLrdsGLG-VLITD--HNVREtlaVCERAYIVSQGNLIAHGT 220
Cdd:COG1135 164 CDEATSALDPEttrSILDlLKDINREL---GLTiVLITHemDVVRR---ICDRVAVLENGRIVEQGP 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-241 |
1.05e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 122.49 E-value: 1.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-----SLLplHARAR 77
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydkkSLL--EVRKT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 RGIGYLPQEASIFRRLSVFDNLMAVLQIRddLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:PRK13639 80 VGIVFQNPDDQLFAPTVEEDVAFGPLNLG--LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRvylGE 237
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIETIR---KA 234
|
....
6MIT_B 238 DFRL 241
Cdd:PRK13639 235 NLRL 238
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-226 |
1.32e-33 |
|
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: 119.94 E-value: 1.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGiVPR---DAGNIIIDDEDISLLPLHARARRGI 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKyevTEGEILFKGEDITDLPPEERARLGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVfdnlmavlqirddltseqrqdranelmeefhIEHLRDsLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:cd03217 80 FLAFQYPPEIPGVKN-------------------------------ADFLRY-VNEGFSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAV-CERAYIVSQGNLIAHGTPQQILE 226
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKELALE 194
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-207 |
1.36e-33 |
|
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: 120.05 E-value: 1.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 5 TAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplhARARRGIGYL 83
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEA-SIFRRLSVFDNLMavlqIRDDLTSEqRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:cd03226 77 MQDVdYQLFTDSVREELL----LGLKELDA-GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERA 207
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRV 196
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-241 |
2.31e-33 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 120.72 E-value: 2.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDEDISLLPLHARARRGiGYLPQEASifrrlSVFdnLMA 101
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHR-AYLSQQQS-----PPF--AMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 102 VLQ-----IRDDLTSEQRQDRANELMEEFHIE-HLRDSLGQaLSGGERRRVEIARAL-----AANP--KFILLDEPFAGV 168
Cdd:COG4138 86 VFQylalhQPAGASSEAVEQLLAQLAEALGLEdKLSRPLTQ-LSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYlGEDFRL 241
Cdd:COG4138 165 DVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF-GVKFRR 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-201 |
9.77e-33 |
|
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: 9.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARA 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT----GPGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 77 RRGIGYlpQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANP 156
Cdd:COG4525 77 DRGVVF--QKDALLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
6MIT_B 157 KFILLDEPFAGVDPISVidiKRIIEHL----RDSGLGVLITDHNVRETL 201
Cdd:COG4525 154 RFLLMDEPFGALDALTR---EQMQELLldvwQRTGKGVFLITHSVEEAL 199
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
7-221 |
3.04e-32 |
|
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: 124.36 E-value: 3.04e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlPLHArARRGIGYLP 84
Cdd:TIGR01257 932 KNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDA-VRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QEASIFRRLSVFDNLMAVLQIRDDlTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQLKGR-SWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 165 FAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTP 221
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYR-SGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-219 |
3.75e-32 |
|
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: 117.43 E-value: 3.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisLLPLHARAR--RGIGY-LPQEASI 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG----LVPWKRRKKflRRIGVvFGQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 90 FRRLSVFDNLmAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVD 169
Cdd:cd03267 107 WWDLPVIDSF-YLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
6MIT_B 170 PISVIDIKRII-EHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03267 186 VVAQENIRNFLkEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-234 |
5.39e-32 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 117.11 E-value: 5.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 5 TAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLP 84
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR-LAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QEASIFRRLSVFDnlmavL---------QIRddLTSEQRQ--DRAnelMEEFHIEHLRDSLGQALSGGERRRVEIARALA 153
Cdd:COG4604 82 QENHINSRLTVRE-----LvafgrfpysKGR--LTAEDREiiDEA---IAYLDLEDLADRYLDELSGGQRQRAFIAMVLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVreTLAVCERAYIVS--QGNLIAHGTPQQILEDDHV 230
Cdd:COG4604 152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDI--NFASCYADHIVAmkDGRVVAQGTPEEIITPEVL 229
|
....
6MIT_B 231 KRVY 234
Cdd:COG4604 230 SDIY 233
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-217 |
6.28e-32 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 121.66 E-value: 6.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAkaykGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:COG1129 257 LEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 P---QEASIFRRLSVFDNLmaVLQIRDDLT-----SEQRQDR-ANELMEEFHIEHlrDSLGQA---LSGGERRRVEIARA 151
Cdd:COG1129 333 PedrKGEGLVLDLSIRENI--TLASLDRLSrggllDRRRERAlAEEYIKRLRIKT--PSPEQPvgnLSGGNQQKVVLAKW 408
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 152 LAANPKFILLDEPFAGVDpisvI----DIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIA 217
Cdd:COG1129 409 LATDPKVLILDEPTRGID----VgakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-222 |
1.05e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 116.27 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISL-LPLHARA----RRGIG 81
Cdd:COG4161 6 KNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDFsQKPSEKAirllRQKVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNL----MAVLqirdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:COG4161 86 MVFQQYNLWPHLTVMENLieapCKVL----GLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNV---RET---LAVCERAYIVSQGNLIAHGTPQ 222
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVefaRKVasqVVYMEKGRIIEQGDASHFTQPQ 232
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-219 |
1.98e-31 |
|
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: 114.19 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKG------RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG--IVPRDAGNIIIDDEdisllPL 72
Cdd:cd03213 1 GVTLSFRNLTVTVKSspsksgKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGR-----PL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 73 HARA-RRGIGYLPQEASIFRRLSVFDNLMAVLQIRddltseqrqdranelmeefhiehlrdslgqALSGGERRRVEIARA 151
Cdd:cd03213 76 DKRSfRKIIGYVPQDDILHPTLTVRETLMFAAKLR------------------------------GLSGGERKRVSIALE 125
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR-ETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03213 126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
11-198 |
6.77e-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: 6.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---GNIIIDDEDISllplHARARRGIGYLPQEA 87
Cdd:cd03234 15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRK----PDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 88 SIFRRLSVFDNL--MAVLQIRDDLTSEQRQDR-ANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:cd03234 91 ILLPGLTVRETLtyTAILRLPRKSSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
|
170 180 190
....*....|....*....|....*....|....
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR 198
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPR 204
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-223 |
1.34e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 118.21 E-value: 1.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARArRGIGY 82
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRsPRDAIA-LGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLM----AVLQIRDDLTSEQRqdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKF 158
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVlglePTKGGRLDRKAARA--RIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARI 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQ 223
Cdd:COG3845 163 LILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-227 |
4.02e-30 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 116.83 E-value: 4.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAY----KGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAG--NIIIDDEDISL----LPLHAR 75
Cdd:TIGR03269 283 RNVSKRYisvdRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevNVRVGDEWVDMtkpgPDGRGR 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 76 ARRGIGYLPQEASIFRRLSVFDNLMAVLQIrdDLTSEQRQDRANELM-----EEFHIEHLRDSLGQALSGGERRRVEIAR 150
Cdd:TIGR03269 363 AKRYIGILHQEYDLYPHRTVLDNLTEAIGL--ELPDELARMKAVITLkmvgfDEEKAEEILDKYPDELSEGERHRVALAQ 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:TIGR03269 441 VLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-164 |
5.89e-30 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 116.32 E-value: 5.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisllplhARARrgIGYLPQ 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP----------KGLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 EASIFRRLSVFDNLMAVLQIRDDL------------TSEQRQDRANELMEEFH----------IEHLRDSLG-------- 135
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALeaeleeleaklaEPDEDLERLAELQEEFEalggweaearAEEILSGLGfpeedldr 148
|
170 180 190
....*....|....*....|....*....|.
6MIT_B 136 --QALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:COG0488 149 pvSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-219 |
7.96e-30 |
|
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: 110.66 E-value: 7.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLharARRGIGYLPQEASIFRRLSVFDNLM 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 101 AVLQIRDDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRII 180
Cdd:cd03298 93 LGLSPGLKLTAEDRQ-AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
6MIT_B 181 EHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-232 |
9.43e-30 |
|
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: 111.97 E-value: 9.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLPQEASIFRRLSV 95
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSrkeLRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 FDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPIsvid 175
Cdd:cd03294 120 LENVAFGLEVQG-VPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL---- 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 176 IKR-IIEHL----RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE---DDHVKR 232
Cdd:cd03294 195 IRReMQDELlrlqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTnpaNDYVRE 259
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
7-228 |
2.00e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 111.24 E-value: 2.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL-HARARRGIgyl 83
Cdd:PRK13632 11 ENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLkEIRKKIGI--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 pqeasIFRRLsvfDNLMAVLQIRDD---------LTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAA 154
Cdd:PRK13632 88 -----IFQNP---DNQFIGATVEDDiafglenkkVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLIT-DHNVRETLaVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-164 |
2.15e-29 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 112.13 E-value: 2.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGR-----------RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPL 72
Cdd:COG4608 8 LEVRDLKKHFPVRgglfgrtvgvvKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 73 HARA--RRGIGYLPQE--ASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELME-----EFHIE---HlrdslgqALSG 140
Cdd:COG4608 88 RELRplRRRMQMVFQDpyASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLElvglrPEHADrypH-------EFSG 160
|
170 180
....*....|....*....|....
6MIT_B 141 GERRRVEIARALAANPKFILLDEP 164
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEP 184
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-201 |
2.45e-29 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 110.56 E-value: 2.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRGIGYl 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE----GPGAERGVVF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 pQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:PRK11248 77 -QNEGLLPWRNVQDNVAFGLQLA-GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|....*....
6MIT_B 164 PFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETL 201
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIEEAV 193
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-227 |
2.63e-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: 111.00 E-value: 2.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI------SLLPLharaRRGIGYLPQ--EA 87
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkkkKLKDL----RKKVGLVFQfpEH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 88 SIFRRlSVFD-------NLmavlqirdDLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:TIGR04521 94 QLFEE-TVYKdiafgpkNL--------GLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 160 LLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:TIGR04521 165 ILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSD 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-238 |
3.53e-29 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 113.01 E-value: 3.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASI---FRRLSVFDnlMAVLQIRDDLTSEQRQDRA--NELMEEFHIEHLRDSLGQALSGGERRRVEIARALAAN 155
Cdd:PRK09536 80 ASVPQDTSLsfeFDVRQVVE--MGRTPHRSRFDTWTETDRAavERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVK---- 231
Cdd:PRK09536 158 TPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRaafd 237
|
....*...
6MIT_B 232 -RVYLGED 238
Cdd:PRK09536 238 aRTAVGTD 245
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-228 |
4.80e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 114.11 E-value: 4.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 12 AY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLHARaRRGIGYLPQE 86
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKST----LVNLLLRfydpTSGRILIDGVDIRDLTLESL-RRQIGVVPQD 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ASIFRRlSVFDNL-MAvlqiRDDLTSEQ-----RQDRANELmeefhIEHLRDSL-------GQALSGGERRRVEIARALA 153
Cdd:COG1132 423 TFLFSG-TIRENIrYG----RPDATDEEveeaaKAAQAHEF-----IEALPDGYdtvvgerGVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVReTLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIA-HRLS-TIRNADRILVLDDGRIVEQGTHEELLARG 565
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
2-226 |
5.06e-29 |
|
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: 114.07 E-value: 5.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRG 79
Cdd:COG4618 329 GRLSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELG 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 --IGYLPQEASIFRRlSVFDNlmavlqI-R-DDLTSEQ-----RQDRANELmeefhIEHLRD-------SLGQALSGGER 143
Cdd:COG4618 406 rhIGYLPQDVELFDG-TIAEN------IaRfGDADPEKvvaaaKLAGVHEM-----ILRLPDgydtrigEGGARLSGGQR 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 144 RRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVReTLAVCERAYIVSQGNLIAHGTPQQ 223
Cdd:COG4618 474 QRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
...
6MIT_B 224 ILE 226
Cdd:COG4618 553 VLA 555
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-227 |
5.56e-29 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 111.96 E-value: 5.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYLPQE 86
Cdd:PRK09452 18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE---NRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFa 166
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQ-KTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESL- 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 167 gvdpiSVIDIK-RI-----IEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK09452 173 -----SALDYKlRKqmqneLKALqRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEE 235
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-195 |
9.76e-29 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 107.32 E-value: 9.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 12 AYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiiiddedisllpLHARARRGIGYLPQEASIFR 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT------------VRRAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 92 RL--SVFDNL-MAVLQIRDDLTSEQRQDRA--NELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:NF040873 69 SLplTVRDLVaMGRWARRGLWRRLTRDDRAavDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180
....*....|....*....|....*....
6MIT_B 167 GVDPISVIDIKRIIEHLRDSGLGVLITDH 195
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-220 |
1.16e-28 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 108.18 E-value: 1.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGI--VPRD-----AGNII-----IDDEDISLLplha 74
Cdd:PRK11124 6 NGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSS-LLRVLNLleMPRSgtlniAGNHFdfsktPSDKAIREL---- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 75 raRRGIGYLPQEASIFRRLSVFDNL----MAVLqirdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIAR 150
Cdd:PRK11124 81 --RRNVGMVFQQYNLWPHLTVQQNLieapCRVL----GLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGT 220
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-196 |
1.50e-28 |
|
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: 107.49 E-value: 1.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA--RRGIGYL 83
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03292 84 FQDFRLLPDRNVYENVAFALEVTGVPPREIRK-RVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADE 162
|
170 180 190
....*....|....*....|....*....|...
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
Cdd:cd03292 163 PTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
7-228 |
2.76e-28 |
|
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: 106.93 E-value: 2.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQ 85
Cdd:cd03254 6 ENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK-SLRSMIGVVLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 EASIFRRlSVFDNL-MAVLQIRDDLTSE-QRQDRANELmeefhIEHLRDSL-------GQALSGGERRRVEIARALAANP 156
Cdd:cd03254 85 DTFLFSG-TIMENIrLGRPNATDEEVIEaAKEAGAHDF-----IMKLPNGYdtvlgenGGNLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 157 KFILLDEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:cd03254 159 KILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDELLAKK 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
3.23e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 107.97 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRG 79
Cdd:PRK13652 1 MHLIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR-EVRKF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQ--EASIFRrlSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:PRK13652 80 VGLVFQnpDDQIFS--PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI-LEDDHVKRVYL 235
Cdd:PRK13652 158 VLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARVHL 237
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-240 |
4.91e-28 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 106.94 E-value: 4.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPrDAGNIIIDDEDISLLPLHARARRGiGYLPQEASIFRRLSVFDNLMa 101
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTPPFAMPVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 102 vLQIRDDLTSEQRQDRANELMEEFhieHLRDSLG---QALSGGERRRVEIARAL-----AANP--KFILLDEPFAGVDPI 171
Cdd:PRK03695 92 -LHQPDKTRTEAVASALNEVAEAL---GLDDKLGrsvNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVA 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 172 SVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVYlGEDFR 240
Cdd:PRK03695 168 QQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF-GVNFR 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-169 |
7.81e-28 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 108.96 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlhaRARRGI 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVP---PAERGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLMAVLQIRDDLTSEqRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLAGAKKEE-INQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFL 156
|
....*....
6MIT_B 161 LDEPFAGVD 169
Cdd:PRK11000 157 LDEPLSNLD 165
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
7-232 |
1.57e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 105.87 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---------GNIIIDDEDISLLPLHARAR 77
Cdd:PRK09984 8 EKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagshiellGRTVQREGRLARDIRKSRAN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 rgIGYLPQEASIFRRLSVFDN-LMAVL-------QIRDDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIA 149
Cdd:PRK09984 88 --TGYIFQQFNLVNRLSVLENvLIGALgstpfwrTCFSWFTREQKQ-RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 150 RALAANPKFILLDEPFAGVDPISVidiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESA---RIVMDTLRDinqnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFD 241
|
....*....
6MIT_B 226 ED--DHVKR 232
Cdd:PRK09984 242 NErfDHLYR 250
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
15-232 |
2.25e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 106.09 E-value: 2.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIS-----LLPLharaRRGIGYLPQE--- 86
Cdd:PRK13636 18 GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrkgLMKL----RESVGMVFQDpdn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ----ASIFRRLSvfdnlMAVLQIRddLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:PRK13636 94 qlfsASVYQDVS-----FGAVNLK--LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLD 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 163 EPFAGVDPISVIDI-KRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKR 232
Cdd:PRK13636 167 EPTAGLDPMGVSEImKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAEKEMLR 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-227 |
3.16e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.83 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI-SLLPLHA----- 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQqkgli 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 75 -RARRGIGYLPQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALA 153
Cdd:PRK11264 81 rQLRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
7-219 |
3.27e-27 |
|
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: 103.82 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLP 84
Cdd:cd03245 6 RNVSFSYPNqeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD-PADLRRNIGYVP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QEASIFRRlSVFDNLMAVLQIRDDltseQRQDRANEL--MEEFHIEHLR-DSL-----GQALSGGERRRVEIARALAANP 156
Cdd:cd03245 85 QDVTLFYG-TLRDNITLGAPLADD----ERILRAAELagVTDFVNKHPNgLDLqigerGRGLSGGQRQAVALARALLNDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 157 KFILLDEPFAGVDPISVidiKRIIEHLRDSGLG---VLITdHNVReTLAVCERAYIVSQGNLIAHG 219
Cdd:cd03245 160 PILLLDEPTSAMDMNSE---ERLKERLRQLLGDktlIIIT-HRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-217 |
5.59e-27 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 107.81 E-value: 5.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNL-AKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
Cdd:COG3845 258 LEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEasifrRL--------SVFDNLMAVLQIRDDLTS------EQRQDRANELMEEFHIehlR----DSLGQALSGGERR 144
Cdd:COG3845 338 IPED-----RLgrglvpdmSVAENLILGRYRRPPFSRggfldrKAIRAFAEELIEEFDV---RtpgpDTPARSLSGGNQQ 409
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 145 RVEIARALAANPKFILLDEPFAGVDPISVIDI-KRIIEhLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIA 217
Cdd:COG3845 410 KVILARELSRDPKLLIAAQPTRGLDVGAIEFIhQRLLE-LRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVG 482
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
3-206 |
7.33e-27 |
|
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: 107.76 E-value: 7.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIG 81
Cdd:TIGR02857 321 SLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIA 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRlSVFDNLMAVLQIRDDLTSEQRQDRA--NELMEEF--HIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:TIGR02857 400 WVPQHPFLFAG-TIAENIRLARPDASDAEIREALERAglDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNvRETLAVCER 206
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT-HR-LALAALADR 525
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-195 |
7.56e-27 |
|
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: 102.44 E-value: 7.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHarARRGIGYL 83
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE--PHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAvlqIRDDLTSEQRQdrANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:TIGR01189 79 GHLPGLKPELSALENLHF---WAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153
|
170 180 190
....*....|....*....|....*....|...
6MIT_B 164 PFAGVDPISVIDIKRIIE-HLRDSGlGVLITDH 195
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRaHLARGG-IVLLTTH 185
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-224 |
7.96e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.96 E-value: 7.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaraRRGIGYLPQE 86
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ---QRDICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKML-GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 167 GVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-196 |
1.44e-26 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.87 E-value: 1.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISlLPLHARArrgIGY 82
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID-DPDVAEA---CHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIRDdlTSEQRQDRANELMEEFHIEHLRdslGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:PRK13539 78 LGHRNAMKPALTVAENLEFWAAFLG--GEELDIAAALEAVGLAPLAHLP---FGYLSAGQKRRVALARLLVSNRPIWILD 152
|
170 180 190
....*....|....*....|....*....|....*
6MIT_B 163 EPFAGVDPISVIDIKRII-EHLRDSGLgVLITDHN 196
Cdd:PRK13539 153 EPTAALDAAAVALFAELIrAHLAQGGI-VIAATHI 186
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-227 |
1.78e-26 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 102.48 E-value: 1.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA-RRGIGYLPQ 85
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 EASIFRRLSVFDNLM-AVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:PRK09493 85 QFYLFPHLTALENVMfGPLRVRG-ASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
2.05e-26 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 106.43 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI--VPRDAGNII-------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 62 --------IDDEDISLL----PLHARARRGIGYLPQEA-SIFRRLSVFDNLMAVLQiRDDLTSEQRQDRANELMEEFHIE 128
Cdd:TIGR03269 81 pcpvcggtLEPEEVDFWnlsdKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 129 HLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI-KRIIEHLRDSGLGVLITDH--NVRETLAvcE 205
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhNALEEAVKASGISMVLTSHwpEVIEDLS--D 237
|
250 260
....*....|....*....|.
6MIT_B 206 RAYIVSQGNLIAHGTPQQILE 226
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVA 258
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-164 |
2.47e-26 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 106.30 E-value: 2.47e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplharaRRG---- 79
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV----------------KLGetvk 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFR-RLSVFDNLMavlQIRDDLTSeqrqdranelmeefhiEHLRDSLGQ-------------ALSGGERRR 145
Cdd:COG0488 380 IGYFDQHQEELDpDKTVLDELR---DGAPGGTE----------------QEVRGYLGRflfsgddafkpvgVLSGGEKAR 440
|
170
....*....|....*....
6MIT_B 146 VEIARALAANPKFILLDEP 164
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEP 459
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-198 |
2.72e-26 |
|
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: 101.66 E-value: 2.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYK-GR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR-- 77
Cdd:TIGR02211 2 LKCENLGKRYQeGKldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 -RGIGYLPQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANP 156
Cdd:TIGR02211 82 nKKLGFIYQFHHLLPDFTALENVAMPLLIGK-KSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|...
6MIT_B 157 KFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVR 198
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLE 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
7-231 |
3.17e-26 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 106.02 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE 86
Cdd:PRK09700 9 AGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ASIFRRLSVFDNLM-------AVLQIRDDLTSEQRQdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:PRK09700 89 LSVIDELTVLENLYigrhltkKVCGVNIIDWREMRV-RAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVI 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVK 231
Cdd:PRK09700 168 IMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-196 |
1.54e-25 |
|
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: 103.98 E-value: 1.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKG-RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
Cdd:TIGR02868 333 PTLELRDLSAGYPGaPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-V 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRlSVFDNLMAVlqiRDDLTSEQRQDRANELMEEFHIEHLRDSL-------GQALSGGERRRVEIARALA 153
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLA---RPDATDEELWAALERVGLADWLRALPDGLdtvlgegGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
6MIT_B 154 ANPKFILLDEPFAGVDPisvIDIKRIIEHLRD--SGLGVLITDHN 196
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDA---ETADELLEDLLAalSGRTVVLITHH 529
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
18-216 |
1.65e-25 |
|
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: 100.65 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHARA-RRGIGYLPQEA--SIFRRL 93
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdRKQRRAfRRDVQLVFQDSpsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 SVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHI--EHLrDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrsEDA-DKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMV 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
6MIT_B 172 SVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGNLI 216
Cdd:TIGR02769 185 LQAVILELLRKLQqAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-213 |
2.35e-25 |
|
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: 99.43 E-value: 2.35e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MAT-LTAKNLAKAYK-----GRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDE----DIS 68
Cdd:COG4778 1 MTTlLEVENLSKTFTlhlqgGKRlpVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 69 LLP----LHARaRRGIGYLPQEASIFRRLSVFDNLMAVLqIRDDLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGER 143
Cdd:COG4778 81 QASpreiLALR-RRTIGYVSQFLRVIPRVSALDVVAEPL-LERGVDREEARARARELLARLNLpERLWDLPPATFSGGEQ 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 144 RRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVL-IT-DHNVREtlAVCERAYIVSQG 213
Cdd:COG4778 159 QRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFhDEEVRE--AVADRVVDVTPF 228
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-216 |
3.82e-25 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 99.76 E-value: 3.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKG---------RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 72 LHARA--RRGIGYLPQEA--SIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELME--EFHIEHLrDSLGQALSGGERRR 145
Cdd:PRK10419 81 RAQRKafRRDIQMVFQDSisAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRavDLDDSVL-DKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 146 VEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETLAVCERAYIVSQGNLI 216
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQqFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-225 |
4.72e-25 |
|
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: 102.81 E-value: 4.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIGYLPQEASIFRRlSV 95
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKH-IGYLPQDVELFPG-TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 FDNlmaVLQIRDDLTSEQ-----RQDRANELMEEFhiEHLRDSL----GQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:TIGR01842 409 AEN---IARFGENADPEKiieaaKLAGVHELILRL--PDGYDTVigpgGATLSGGQRQRIALARALYGDPKLVVLDEPNS 483
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVReTLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:TIGR01842 484 NLDEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-226 |
6.27e-25 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 100.16 E-value: 6.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplharaRRGIGYLpqeasifRR 92
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF--------KRRKEFA-------RR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 93 LSV-----------------FDNLMAVLQIRDdltsEQRQDRANELMEEFHIEHLrdsLGQA---LSGGERRRVEIARAL 152
Cdd:COG4586 97 IGVvfgqrsqlwwdlpaidsFRLLKAIYRIPD----AEYKKRLDELVELLDLGEL---LDTPvrqLSLGQRMRCELAAAL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:COG4586 170 LHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKE 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-228 |
6.40e-25 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 102.44 E-value: 6.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIS-LLPLHARArRGIGY 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArLTPAKAHQ-LGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFDNLMAVLQIRDDLTSeqrqdRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQ-----KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-228 |
1.06e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 99.39 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGR-----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTF-YMVVGIVPrDAGNIIIDDEDISLLPLHARAR 77
Cdd:PRK13651 3 IKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIeHLNALLLP-DTGTIEWIFKDEKNKKKTKEKE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 RGIGYLPQEASIFRRLSVFDNLM----AVLQ----------IRDDL---------TSEQRQDRANELME--EFHIEHLRD 132
Cdd:PRK13651 82 KVLEKLVIQKTRFKKIKKIKEIRrrvgVVFQfaeyqlfeqtIEKDIifgpvsmgvSKEEAKKRAAKYIElvGLDESYLQR 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 133 SlGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQ 212
Cdd:PRK13651 162 S-PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
250
....*....|....*.
6MIT_B 213 GNLIAHGTPQQILEDD 228
Cdd:PRK13651 241 GKIIKDGDTYDILSDN 256
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-225 |
2.35e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 23 SLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisllplHAR---ARRGIGYLPQEASIFRRLSVFDNL 99
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 100 MAVLQIRDDLTSEQRQDRAnELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRI 179
Cdd:PRK10771 93 GLGLNPGLKLNAAQREKLH-AIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
6MIT_B 180 IEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELL 218
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-220 |
2.50e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 98.72 E-value: 2.50e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAY--KGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGI 80
Cdd:PRK11153 5 KNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEasiFRRLS---VFDNLMAVLQIrDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:PRK11153 85 GMIFQH---FNLLSsrtVFDNVALPLEL-AGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 158 FILLDEPFAGVDPI---SVID-IKRIIEHLrdsGLG-VLITdHN---VREtlaVCERAYIVSQGNLIAHGT 220
Cdd:PRK11153 161 VLLCDEATSALDPAttrSILElLKDINREL---GLTiVLIT-HEmdvVKR---ICDRVAVIDAGRLVEQGT 224
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-224 |
3.20e-24 |
|
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: 100.86 E-value: 3.20e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdiSLLPLHARARRGIG 81
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGK--SILTNISDVHQNMG 2015
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGREHLYLYARLRG-VPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLL 2094
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:TIGR01257 2095 DEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
21-237 |
6.21e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 99.35 E-value: 6.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLP---QEASIFRRLSVFD 97
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrQSSGLYLDAPLAW 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 98 NLMAVLQirDDLTSEQRQDRANELMEEFH------IEHLRDSLGqALSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
Cdd:PRK15439 361 NVCALTH--NRRGFWIKPARENAVLERYRralnikFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 172 SVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNlIAHGTPQQILEDDHVKRVYLGE 237
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGE-ISGALTGAAINVDTIMRLAFGE 502
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-234 |
1.04e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 96.01 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIG 81
Cdd:PRK10575 10 TTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDnLMAVLQI-------RDDLTSEQRQDRANELMEefhIEHLRDSLGQALSGGERRRVEIARALAA 154
Cdd:PRK10575 89 YLPQQLPAAEGMTVRE-LVAIGRYpwhgalgRFGAADREKVEEAISLVG---LKPLAHRLVDSLSGGERQRAWIAMLVAQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 155 NPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRV 233
Cdd:PRK10575 165 DSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQI 244
|
.
6MIT_B 234 Y 234
Cdd:PRK10575 245 Y 245
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-221 |
1.27e-23 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 94.40 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRRlsvf 96
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-DLRSSLTIIPQDPTLFSG---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 97 dnlmavlQIRDDLTSEQRQDRAnELMEEFHIEhlrdSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDI 176
Cdd:cd03369 97 -------TIRSNLDPFDEYSDE-EIYGALRVS----EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
6MIT_B 177 KRIIeHLRDSGLGVLITDHNVReTLAVCERAYIVSQGNLIAHGTP 221
Cdd:cd03369 165 QKTI-REEFTNSTILTIAHRLR-TIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-238 |
2.04e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.41 E-value: 2.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LHARARRGIGYLPQEASIFRRLSV 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 FDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
Cdd:PRK10070 124 LDNTAFGMELAG-INAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 176 IKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE---DDHVKRVYLGED 238
Cdd:PRK10070 203 MQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNnpaNDYVRTFFRGVD 269
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-215 |
2.65e-23 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 92.28 E-value: 2.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARaRRGIG 81
Cdd:cd03246 1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL-GDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRlSVFDNLmavlqirddltseqrqdranelmeefhiehlrdslgqaLSGGERRRVEIARALAANPKFILL 161
Cdd:cd03246 80 YLPQDDELFSG-SIAENI--------------------------------------LSGGQRQRLGLARALYGNPRILVL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvRETLAVCERAYIVSQGNL 215
Cdd:cd03246 121 DEPNSHLDVEGERALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-195 |
2.79e-23 |
|
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: 93.33 E-value: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddEDISLLPLHARARRGIGYL 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLL--NGGPLDFQRDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANelmeefhIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03231 79 GHAPGIKTTLSVLENLRFWHADHSDEQVEEALARVG-------LNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|...
6MIT_B 164 PFAGVDPISVIDI-KRIIEHLRDSGLGVLITDH 195
Cdd:cd03231 152 PTTALDKAGVARFaEAMAGHCARGGMVVLTTHQ 184
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-222 |
3.23e-23 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 94.03 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTA-KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIiddedisllplHARARRg 79
Cdd:PRK09544 1 MTSLVSlENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLR- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQ----EASIFRRLSVFDNLMAVLQIRDDLTSEQRqdranelmeeFHIEHLRDSLGQALSGGERRRVEIARALAAN 155
Cdd:PRK09544 69 IGYVPQklylDTTLPLTVNRFLRLRPGTKKEDILPALKR----------VQAGHLIDAPMQKLSGGETQRVLLARALLNR 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQgNLIAHGTPQ 222
Cdd:PRK09544 139 PQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPE 205
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-198 |
3.50e-23 |
|
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: 93.86 E-value: 3.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG----IVPRdaGNIIIDDEDISLLPLHARARRG 79
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsyEVTS--GTILFKGQDLLELEPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRAN--ELMEE------FHIEHLRDSLGQALSGGERRRVEIARA 151
Cdd:TIGR01978 79 LFLAFQYPEEIPGVSNLEFLRSALNARRSARGEEPLDLLDfeKLLKEklalldMDEEFLNRSVNEGFSGGEKKRNEILQM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
6MIT_B 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR 198
Cdd:TIGR01978 159 ALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR 205
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-228 |
3.72e-23 |
|
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: 93.45 E-value: 3.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 14 KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLHArARRGIGYLPQEASI 89
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKST----LVNLIPRfydvDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVFL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 90 FRRlSVFDNLMAVlqiRDDLTSEQRQD--RANELMEefHIEHLRDSL-------GQALSGGERRRVEIARALAANPKFIL 160
Cdd:cd03251 88 FND-TVAENIAYG---RPGATREEVEEaaRAANAHE--FIMELPEGYdtvigerGVKLSGGQRQRIAIARALLKDPPILI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:cd03251 162 LDEATSALDTESERLVQAALERLM-KNRTTFVIAHRL-STIENADRIVVLEDGKIVERGTHEELLAQG 227
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
16-236 |
4.20e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 94.73 E-value: 4.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI---SLLPLHARARRGIGYLPQEASIFRR 92
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDItdkKVKLSDIRKKVGLVFQYPEYQLFEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 93 LSVFDnlMAVLQIRDDLTSEQRQDRANELMEEFHI--EHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDP 170
Cdd:PRK13637 100 TIEKD--IAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDP 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 171 ISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL-EDDHVKRVYLG 236
Cdd:PRK13637 178 KGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFkEVETLESIGLA 245
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-215 |
5.39e-23 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 93.59 E-value: 5.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHArARRGIGYL 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTA-----PLAE-AREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMavLQIRDDLTSEQRQ--------DRANELmeefhiehlrdslGQALSGGERRRVEIARALAAN 155
Cdd:PRK11247 87 FQDARLLPWKKVIDNVG--LGLKGQWRDAALQalaavglaDRANEW-------------PAALSGGQKQRVALARALIHR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 156 PKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNL 215
Cdd:PRK11247 152 PGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-225 |
7.23e-23 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 93.92 E-value: 7.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplharARRGIGYL 83
Cdd:PRK13638 2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDY------SKRGLLAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQE-ASIFR--RLSVF----DNLMAvLQIRD-DLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAAN 155
Cdd:PRK13638 76 RQQvATVFQdpEQQIFytdiDSDIA-FSLRNlGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:PRK13638 155 ARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-213 |
8.09e-23 |
|
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: 92.53 E-value: 8.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRGIGYlpQEASIFRRLSVFDN 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT----EPGPDRMVVF--QNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 99 L-MAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177
Cdd:TIGR01184 75 IaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
6MIT_B 178 -RIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
Cdd:TIGR01184 155 eELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-195 |
1.04e-22 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 91.79 E-value: 1.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARA--RRGIG 81
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIR----RQRDeyHQDLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLMAVLQIRDdltsEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:PRK13538 78 YLGHQPGIKTELTALENLRFYQRLHG----PGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*
6MIT_B 162 DEPFAGVDPISVIDIKRIIE-HLRDSGLgVLITDH 195
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLAqHAEQGGM-VILTTH 187
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-213 |
1.34e-22 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 89.82 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplharaRRGIGYL 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS------------TVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQeasifrrlsvfdnlmavlqirddltseqrqdranelmeefhiehlrdslgqaLSGGERRRVEIARALAANPKFILLDE 163
Cdd:cd03221 69 EQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
6MIT_B 164 PFAGVDPISvidIKRIIEHLRDSGLGVLITDHNvRETL-AVCERAYIVSQG 213
Cdd:cd03221 97 PTNHLDLES---IEALEEALKEYPGTVILVSHD-RYFLdQVATKIIELEDG 143
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-224 |
1.37e-22 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 92.53 E-value: 1.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTF------------YMVVGIVPRDAGNIIIDDEDISLLp 71
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmndlnpeVTITGSIVYNGHNIYSPRTDTVDL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 72 lharaRRGIGYLPQEASIFRrLSVFDNLMAVLQIRDdLTSEQRQDRANE-------LMEEFHiEHLRDSlGQALSGGERR 144
Cdd:PRK14239 85 -----RKEIGMVFQQPNPFP-MSIYENVVYGLRLKG-IKDKQVLDEAVEkslkgasIWDEVK-DRLHDS-ALGLSGGQQQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDRTGFFLDGDLIEYNDTKQM 234
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-226 |
1.70e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 95.58 E-value: 1.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNI-----IIDDEDISllplharARRGIGYLPQEASIFRRL 93
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIA-------TRRRVGYMSQAFSLYGEL 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 SVFDNLmaVLQIR-DDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
Cdd:NF033858 355 TVRQNL--ELHARlFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 173 VIDIKRIIEHL-RDSGLGVLITDHNVRETlAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:NF033858 433 RDMFWRLLIELsREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAALVA 486
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-223 |
2.12e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 95.50 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTT-----TFYMVVGIVprDAGNIIIDDEDISLLPLHARArrgiGYLPQEASIFRRLSV 95
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKGVK--GSGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 FDNLM--AVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSL-GQA-----LSGGERRRVEIARALAANPKFILLDEPFAG 167
Cdd:TIGR00955 117 REHLMfqAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRiGVPgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 168 VDPISVIDIKRIIEHLRDSGLGVLITDHNVRETL-AVCERAYIVSQGNLIAHGTPQQ 223
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQ 253
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-197 |
2.37e-22 |
|
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: 91.70 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 25 TVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplhararrgigYLPQEASIFRRLSVFDNLMAVlq 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKPQYIKADYEGTVRDLLSSI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 105 IRDDLTSEQRQdraNELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDP----ISVIDIKRII 180
Cdd:cd03237 86 TKDFYTHPYFK---TEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRFA 162
|
170
....*....|....*..
6MIT_B 181 EHLRDsglGVLITDHNV 197
Cdd:cd03237 163 ENNEK---TAFVVEHDI 176
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-229 |
2.98e-22 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 91.91 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA---RRGI 80
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSeaeRRRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 -----GYLPQEASIFRRLSVF------DNLMAVLQ-----IRddltseqrqDRANELMEEFHIEHLR-DSLGQALSGGER 143
Cdd:PRK11701 87 lrtewGFVHQHPRDGLRMQVSaggnigERLMAVGArhygdIR---------ATAGDWLERVEIDAARiDDLPTTFSGGMQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 144 RRVEIARALAANPKFILLDEPFAGVDpISV----IDIKRIIehLRDSGLGVLITDHNvretLAVC----ERAYIVSQGNL 215
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLD-VSVqarlLDLLRGL--VRELGLAVVIVTHD----LAVArllaHRLLVMKQGRV 230
|
250
....*....|....
6MIT_B 216 IAHGTPQQILEDDH 229
Cdd:PRK11701 231 VESGLTDQVLDDPQ 244
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-199 |
3.46e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 90.93 E-value: 3.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRRlS 94
Cdd:PRK10247 19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE-IYRQQVSYCAQTPTLFGD-T 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLMAVLQIRDDLTSEQRQdrANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
Cdd:PRK10247 97 VYDNLIFPWQIRNQQPDPAIF--LDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174
|
170 180
....*....|....*....|....*.
6MIT_B 175 DIKRIIEHL-RDSGLGVLITDHNVRE 199
Cdd:PRK10247 175 NVNEIIHRYvREQNIAVLWVTHDKDE 200
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-232 |
3.72e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 91.25 E-value: 3.72e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TF---YMVVGIVpRDAGNIIIDDEDI---SLLPLHA 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLnrmNDLIPGA-RVEGEILLDGEDIydpDVDVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 75 RARrgIGYLPQEASIFRrLSVFDNLMAVLQIRDDLTSEQRQDRANE------LMEEFHiEHLRDSlGQALSGGERRRVEI 148
Cdd:COG1117 91 RRR--VGMVFQKPNPFP-KSIYDNVAYGLRLHGIKSKSELDEIVEEslrkaaLWDEVK-DRLKKS-ALGLSGGQQQRLCI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:COG1117 166 ARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNP 244
|
....
6MIT_B 229 HVKR 232
Cdd:COG1117 245 KDKR 248
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-225 |
3.82e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 92.08 E-value: 3.82e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYM-------VVGIvpRDAGNIIIDDEDISLLPLHARA 76
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGY--RYSGDVLLGGRSIFNYRDVLEF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 77 RRGIGYLPQEASIFRrLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHI-EHLRDSLGQA---LSGGERRRVEIARAL 152
Cdd:PRK14271 100 RRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLCLARTL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 153 AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:PRK14271 179 AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLF 250
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
7-226 |
4.67e-22 |
|
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: 90.75 E-value: 4.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQ 85
Cdd:cd03253 4 ENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 EASIFRRlSVFDNlmaVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSL-------GQALSGGERRRVEIARALAANPKF 158
Cdd:cd03253 83 DTVLFND-TIGYN---IRYGRPDATDEEVIEAAKAAQIHDKIMRFPDGYdtivgerGLKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVReTLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLS-TIVNADKIIVLKDGRIVERGTHEELLA 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-228 |
6.07e-22 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 93.84 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEdisllPLHARA----- 76
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGE-----ELQASNirdte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 77 RRGIGYLPQEASIFRRLSVFDNLMavlqIRDDLTSEQRQD------RANELMEEFHIEHLRDSLGQALSGGERRRVEIAR 150
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIF----LGNEITPGGIMDydamylRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:PRK13549 157 ALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDD 234
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-227 |
7.21e-22 |
|
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: 93.60 E-value: 7.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPL 72
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSE-GEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 73 HA--RARRGIGYLPQE--ASIFRRLSVFDNL---MAVLQIrdDLTSEQRQDRANELMEEFHIEhlRDSLGQ---ALSGGE 142
Cdd:COG4172 355 RAlrPLRRRMQVVFQDpfGSLSPRMTVGQIIaegLRVHGP--GLSAAERRARVAEALEEVGLD--PAARHRyphEFSGGQ 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 143 RRRVEIARALAANPKFILLDEpfagvdPISVIDI---KRIIEHLRD----SGLG-VLITdHN---VRetlAVCERAYIVS 211
Cdd:COG4172 431 RQRIAIARALILEPKLLVLDE------PTSALDVsvqAQILDLLRDlqreHGLAyLFIS-HDlavVR---ALAHRVMVMK 500
|
250
....*....|....*.
6MIT_B 212 QGNLIAHGTPQQILED 227
Cdd:COG4172 501 DGKVVEQGPTEQVFDA 516
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-228 |
1.05e-21 |
|
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: 92.97 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA--GNIIIDDEDISLLPLHARARRGIG 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLMAVLQIRDD---LTSEQRQDRANELMEEFHIEHLRDSLGQA-LSGGERRRVEIARALAANPK 157
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFLGNEITLPggrMAYNAMYLRAKNLLRELQLDADNVTRPVGdYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDD 232
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-193 |
1.28e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 89.97 E-value: 1.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIV-----PRDAGNIIIDDEDISLLPLhAR 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelypeARVSGEVYLDGQDIFKMDV-IE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 76 ARRGIGYLPQEASIFRRLSVFDNLMAVLQIRDDLTSEQR-QDRANELMEEFHI-EHLRDSLGQ---ALSGGERRRVEIAR 150
Cdd:PRK14247 80 LRRRVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIAR 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
6MIT_B 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLIT 193
Cdd:PRK14247 160 ALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT 202
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-229 |
1.44e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 90.46 E-value: 1.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARA----R 77
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG-----MVLSEETvwdvR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 RGIGYLPQEAsifrrlsvfDNLMAVLQIRDDLT---------SEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEI 148
Cdd:PRK13635 81 RQVGMVFQNP---------DNQFVGATVQDDVAfglenigvpREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD-SGLGVLITDHNVRETlAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK13635 152 AGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKS 230
|
..
6MIT_B 228 DH 229
Cdd:PRK13635 231 GH 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-215 |
1.50e-21 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 92.54 E-value: 1.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 6 AKNLAKayKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PLHArARRGIGYLP 84
Cdd:PRK09700 268 VRNVTS--RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRsPLDA-VKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 Q---EASIFRRLSVFDNlMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRD-------SLGQ---ALSGGERRRVEIARA 151
Cdd:PRK09700 345 EsrrDNGFFPNFSIAQN-MAISRSLKDGGYKGAMGLFHEVDEQRTAENQREllalkchSVNQnitELSGGNQQKVLISKW 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNL 215
Cdd:PRK09700 424 LCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-195 |
2.06e-21 |
|
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: 87.75 E-value: 2.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR--VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplHARARRGIG 81
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFrrlsvfdnlmavlqirdDLTseqrqdranelmeefhiehLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:cd03247 79 VLNQRPYLF-----------------DTT-------------------LRNNLGRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190
....*....|....*....|....*....|....*
6MIT_B 162 DEPFAGVDPISVIDIKRII-EHLRDSGLgVLITDH 195
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIfEVLKDKTL-IWITHH 156
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-225 |
2.30e-21 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 89.26 E-value: 2.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-----PLHARARR 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgQLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 79 GIGYLP-------QEASIFRRLSVFDNLM-AVLQIRDdLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIA 149
Cdd:PRK10619 86 QLRLLRtrltmvfQHFNLWSHMTVLENVMeAPIQVLG-LSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-234 |
5.70e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 88.50 E-value: 5.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgIG 81
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLMAVLQIRDDLTSEQR---QDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKF 158
Cdd:PRK10253 85 LLAQNATTPGDITVQELVARGRYPHQPLFTRWRkedEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 159 ILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHVKRVY 234
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-227 |
6.79e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.83 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIG 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLMAVLQIRDDLTS---EQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKF 158
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIFLGREFVNRFGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTED 231
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-169 |
7.44e-21 |
|
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: 87.49 E-value: 7.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR-- 77
Cdd:COG4181 9 IELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 -RGIGYLPQEASIFRRLSVFDNLMAVLQIRDDltsEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANP 156
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGR---RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170
....*....|...
6MIT_B 157 KFILLDEPFAGVD 169
Cdd:COG4181 166 AILFADEPTGNLD 178
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-226 |
9.55e-21 |
|
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: 87.21 E-value: 9.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLHARaRRGIGYLPQEASIFRRl 93
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLERfydpTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEPVLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 SVFDNlmaVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSL-------GQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:cd03249 92 TIAEN---IRYGKPDATDEEVEEAAKKANIHDFIMSLPDGYdtlvgerGSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 167 GVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:cd03249 169 ALDAESEKLVQEALDRAM-KGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMA 226
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-221 |
1.61e-20 |
|
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: 86.39 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRRlSVFD 97
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-DLRSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 98 NLmavlqirdDLTSEQRQDRANELMEE----FHIEHLRDSL-------GQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:cd03244 97 NL--------DPFGEYSDEELWQALERvglkEFVESLPGGLdtvveegGENLSVGQRQLLCLARALLRKSKILVLDEATA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 167 GVDPISVIDIKRII-EHLRDSglGVLITDHNVrETLAVCERAYIVSQGNLIAHGTP 221
Cdd:cd03244 169 SVDPETDALIQKTIrEAFKDC--TVLTIAHRL-DTIIDSDRILVLDKGRVVEFDSP 221
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-228 |
2.47e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 89.39 E-value: 2.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymVVGIVPR----DAGNIIIDDEDISLLPLhARARRGIGYLPQEASIF 90
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKST----LVNLIPRfyepDSGQILLDGHDLADYTL-ASLRRQVALVSQDVVLF 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 91 RRlSVFDNL---------MAvlQIRDDLTSEQRQDRANELMEEFHIEhlRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:TIGR02203 419 ND-TIANNIaygrteqadRA--EIERALAAAYAQDFVDKLPLGLDTP--IGENGVLLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHLRDsGLGVLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:TIGR02203 494 DEATSALDNESERLVQAALERLMQ-GRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNELLARN 558
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-225 |
2.68e-20 |
|
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: 86.00 E-value: 2.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlS 94
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQENVLFNR-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNL------MAVLQIRDDLTSEQRQDRANELMEEFhiEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGV 168
Cdd:cd03252 92 IRDNIaladpgMSMERVIEAAKLAGAHDFISELPEGY--DTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 169 DPISVidiKRIIEHLRD--SGLGVLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:cd03252 170 DYESE---HAIMRNMHDicAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELL 224
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-236 |
3.76e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 86.48 E-value: 3.76e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRGI 80
Cdd:PRK15056 5 AGIVVNDVTVTWRnGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKNLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVF--DNLM-------AVLQIRddlTSEQRQDRANELMEEFHIEHLRDSLGQaLSGGERRRVEIARA 151
Cdd:PRK15056 81 AYVPQSEEVDWSFPVLveDVVMmgryghmGWLRRA---KKRDRQIVTAALARVDMVEFRHRQIGE-LSGGQKKRVFLARA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVsQGNLIAHGTPQQILEDDHVK 231
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLE 235
|
....*
6MIT_B 232 RVYLG 236
Cdd:PRK15056 236 LAFSG 240
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-232 |
4.40e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 86.24 E-value: 4.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVVGIVPRDAGNIIID------DEDISLLPLHA-RA 76
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKST-FLKCLNRMNELESEVRVEgrveffNQNIYERRVNLnRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 77 RRGIGYLPQEASIFRrLSVFDNLMAVLQI--------RDDLTSEQRQDRanELMEEfhIEHLRDSLGQALSGGERRRVEI 148
Cdd:PRK14258 87 RRQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrpkleIDDIVESALKDA--DLWDE--IKHKIHKSALDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCE-RAYIVSQ----GNLIAHGTPQ 222
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDfTAFFKGNenriGQLVEFGLTK 241
|
250
....*....|
6MIT_B 223 QILEDDHVKR 232
Cdd:PRK14258 242 KIFNSPHDSR 251
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-169 |
4.70e-20 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 87.21 E-value: 4.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-PlharARR 78
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELeP----ADR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 79 GIGYLPQEASIFRRLSVFDNLMAVLQIR--DDLTSEQRQDRANELMEefhIEHLRDSLGQALSGGERRRVEIARALAANP 156
Cdd:PRK11650 77 DIAMVFQNYALYPHMSVRENMAYGLKIRgmPKAEIEERVAEAARILE---LEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
|
170
....*....|...
6MIT_B 157 KFILLDEPFAGVD 169
Cdd:PRK11650 154 AVFLFDEPLSNLD 166
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
17-236 |
6.67e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 85.94 E-value: 6.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-------EDISLLPLhaRARRGIGYLPQEASI 89
Cdd:PRK13643 20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDivvsstsKQKEIKPV--RKKVGVVFQFPESQL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 90 FRRLSVFDnlMAVLQIRDDLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGV 168
Cdd:PRK13643 98 FEETVLKD--VAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 169 DPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED-DHVKRVYLG 236
Cdd:PRK13643 176 DPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEvDFLKAHELG 244
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-199 |
7.20e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 85.60 E-value: 7.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDI---SLLPLHAR 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPgfRVEGKVTFHGKNLyapDVDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 76 ARrgIGYLPQEASIFRRlSVFDNLMAVLQIR------DDLTseQRQDRANELMEEFHiEHLRDSlGQALSGGERRRVEIA 149
Cdd:PRK14243 91 RR--IGMVFQKPNPFPK-SIYDNIAYGARINgykgdmDELV--ERSLRQAALWDEVK-DKLKQS-GLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
6MIT_B 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRE 199
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HNMQQ 212
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
7-236 |
8.17e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 8.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---IDDEDISLLPlHARARRGIGY 82
Cdd:PRK13644 5 ENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLvsgIDTGDFSKLQ-GIRKLVGIVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 LPQEASIFRRLSVFD------NL-MAVLQIRddltseQRQDRAnelMEEFHIEHLRDSLGQALSGGERRRVEIARALAAN 155
Cdd:PRK13644 84 QNPETQFVGRTVEEDlafgpeNLcLPPIEIR------KRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTME 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 156 PKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVREtLAVCERAYIVSQGNLIAHGTPQQILEDDHVKrvYL 235
Cdd:PRK13644 155 PECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TL 231
|
.
6MIT_B 236 G 236
Cdd:PRK13644 232 G 232
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-226 |
1.32e-19 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 86.91 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-RDAGNIIIDDEDISLL-PLHArARRGIGYLPQEAS---I 89
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRnPQQA-IAQGIAMVPEDRKrdgI 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 90 FRRLSVFDNL-MAVLqirDDLTSEQRQDRANELME-EFHIEHLR---DSLGQA---LSGGERRRVEIARALAANPKFILL 161
Cdd:PRK13549 353 VPVMGVGKNItLAAL---DRFTGGSRIDDAAELKTiLESIQRLKvktASPELAiarLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 162 DEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG----NLIAHG-TPQQILE 226
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGklkgDLINHNlTQEQVME 499
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-217 |
2.01e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 86.32 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE 86
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ASIFRRLSVFDNLMAVLQIRDDLTSEQRQ--DRANELMEEFHIE-HLRDSLGQaLSGGERRRVEIARALAANPKFILLDE 163
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMFVDQDKmyRDTKAIFDELDIDiDPRAKVAT-LSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIA 217
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-234 |
2.20e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 84.49 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP--------RDAGNIIIDDEDISLLPLHAR 75
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggaprgaRVTGDVTLNGEPLAAIDAPRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 76 ARRGiGYLPQEAsifRRLSVFDNLMAVL------QIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIA 149
Cdd:PRK13547 82 ARLR-AVLPQAA---QPAFAFSAREIVLlgryphARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 150 RALA---------ANPKFILLDEPFAGVDPI---SVIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIA 217
Cdd:PRK13547 158 RVLAqlwpphdaaQPPRYLLLDEPTAALDLAhqhRLLDTVRRLA--RDWNLGVLAIVHDPNLAARHADRIAMLADGAIVA 235
|
250
....*....|....*..
6MIT_B 218 HGTPQQILEDDHVKRVY 234
Cdd:PRK13547 236 HGAPADVLTPAHIARCY 252
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
2.53e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 83.74 E-value: 2.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVP--RDAGNIIIDDEDISLLPLHA- 74
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLELNEeaRVEGEVRLFGRNIYSPDVDPi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 75 RARRGIGYLPQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANE-------LMEEFHiEHLRDSLGQaLSGGERRRVE 147
Cdd:PRK14267 82 EVRREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDERVEwalkkaaLWDEVK-DRLNDYPSN-LSGGQRQRLV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK14267 160 IARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-225 |
2.54e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 83.94 E-value: 2.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 8 NLAKAY---KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDI----SLLPLHA-RARRG 79
Cdd:PRK14246 12 NISRLYlyiNDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgkDIFQIDAiKLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRLSVFDNLMAVLQIRDdlTSEQRQDRanELMEEF--------HIEHLRDSLGQALSGGERRRVEIARA 151
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHG--IKEKREIK--KIVEEClrkvglwkEVYDRLNSPASQLSGGQQQRLTIARA 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 152 LAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:PRK14246 168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIF 240
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
16-184 |
2.85e-19 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 86.17 E-value: 2.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRlSV 95
Cdd:PRK13657 348 RQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR-ASLRRNIAVVFQDAGLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 FDNLmavlQI-RDDLTSEQRQD---RANELmeEFhIEHLRDSL-------GQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:PRK13657 426 EDNI----RVgRPDATDEEMRAaaeRAQAH--DF-IERKPDGYdtvvgerGRQLSGGERQRLAIARALLKDPPILILDEA 498
|
170 180
....*....|....*....|
6MIT_B 165 FAGVDPISVIDIKRIIEHLR 184
Cdd:PRK13657 499 TSALDVETEAKVKAALDELM 518
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-227 |
2.90e-19 |
|
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: 85.89 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKG----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA----GNIIIDDEDISLLPL 72
Cdd:COG4172 4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPAahpsGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 73 HA-RARRG--IGYLPQE--ASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQ---ALSGGERR 144
Cdd:COG4172 84 RElRRIRGnrIAMIFQEpmTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 145 RVEIARALAANPKFILLDEPFAGVDpisVIDIKRIIEHLRD----SGLGVL-ITdHN---VREtlaVCERAYIVSQGNLI 216
Cdd:COG4172 164 RVMIAMALANEPDLLIADEPTTALD---VTVQAQILDLLKDlqreLGMALLlIT-HDlgvVRR---FADRVAVMRQGEIV 236
|
250
....*....|.
6MIT_B 217 AHGTPQQILED 227
Cdd:COG4172 237 EQGPTAELFAA 247
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-227 |
3.40e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.93 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYL 83
Cdd:TIGR00958 482 QDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYD-HHYLHRQVALV 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRlSVFDNLMAVLQI--RDDLTSEQRQDRANELMEEFH--IEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:TIGR00958 561 GQEPVLFSG-SVRENIAYGLTDtpDEEIMAAAKAANAHDFIMEFPngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVL 639
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
6MIT_B 160 LLDEPFAGVDpisvIDIKRIIEHLRDS-GLGVLITDHNvretLAVCERA---YIVSQGNLIAHGTPQQILED 227
Cdd:TIGR00958 640 ILDEATSALD----AECEQLLQESRSRaSRTVLLIAHR----LSTVERAdqiLVLKKGSVVEMGTHKQLMED 703
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
15-225 |
3.49e-19 |
|
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: 85.95 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArARRGIGYLPQEASIFRRlS 94
Cdd:TIGR01193 486 GSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT-LRQFINYLPQEPYIFSG-S 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLMavLQIRDDLTsEQRQDRANELME-EFHIEHLRDSL-------GQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:TIGR01193 564 ILENLL--LGAKENVS-QDEIWAACEIAEiKDDIENMPLGYqtelseeGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 167 GVDpisVIDIKRIIEHLrdsglgVLITDHNV-----RETLA-VCERAYIVSQGNLIAHGTPQQIL 225
Cdd:TIGR01193 641 NLD---TITEKKIVNNL------LNLQDKTIifvahRLSVAkQSDKIIVLDHGKIIEQGSHDELL 696
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
7-230 |
6.74e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 82.86 E-value: 6.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYK-GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH-ARARRGIGYLP 84
Cdd:PRK13647 8 EDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwVRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QEASIFRrLSVFDNLmAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:PRK13647 88 PDDQVFS-STVWDDV-AFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHV 230
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIV 231
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-224 |
6.90e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 83.24 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKG---RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRAR 77
Cdd:PRK13650 2 SNIIEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVW-DIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 RGIGYLPQEAsifrrlsvfDNLMAVLQIRDD---------LTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEI 148
Cdd:PRK13650 81 HKIGMVFQNP---------DNQFVGATVEDDvafglenkgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVREtLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-226 |
7.92e-19 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 84.88 E-value: 7.92e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP-RDAGNIIIDDEDISLLPLHARARRGIGYLPQEAS---IFR 91
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 92 RLSVFDNL-MAVLQ---IRDDLTSEQRQDRANELMEEFHIEHLRDSLGQA-LSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:TIGR02633 353 ILGVGKNItLSVLKsfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIGrLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 167 GVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG----NLIAHG-TPQQILE 226
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGklkgDFVNHAlTQEQVLA 497
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-219 |
9.60e-19 |
|
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: 81.42 E-value: 9.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 10 AKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhararrGIGYLPQeasi 89
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL------GGGFNPE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 90 frrLSVFDNLMAVLQIRdDLTSEQRQDRANELME-----EFHIEHLRdslgqALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:cd03220 99 ---LTGRENIYLNGRLL-GLSRKEIDEKIDEIIEfselgDFIDLPVK-----TYSSGMKARLAFAIATALEPDILLIDEV 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHG 219
Cdd:cd03220 170 LAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
19-237 |
9.65e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 82.95 E-value: 9.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA---RARRGIGYLPQ--EASIFRRL 93
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkKLRKKVSLVFQfpEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 SVFDNLMAVLQIrdDLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
Cdd:PRK13641 103 VLKDVEFGPKNF--GFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 173 VIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED-DHVKRVYLGE 237
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDkEWLKKHYLDE 246
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-198 |
1.16e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 81.79 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR-- 77
Cdd:PRK11629 6 LQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElr 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 -RGIGYLPQEASIFRRLSVFDNLMAVLQIrDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANP 156
Cdd:PRK11629 86 nQKLGFIYQFHHLLPDFTALENVAMPLLI-GKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
6MIT_B 157 KFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVR 198
Cdd:PRK11629 165 RLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-232 |
1.83e-18 |
|
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: 81.82 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLHaRARRGIG 81
Cdd:cd03289 3 MTVKDLTAKYTegGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQ-KWRKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRlSVFDNLMAVLQIRDdltsEQRQDRANELMEEFHIEHLRDSL-------GQALSGGERRRVEIARALAA 154
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLDPYGKWSD----EEIWKVAEEVGLKSVIEQFPGQLdfvlvdgGCVLSHGHKQLMCLARSVLS 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQIL-EDDHVKR 232
Cdd:cd03289 156 KAKILLLDEPSAHLDPITYQVIRKTLKQAF-ADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLnEKSHFKQ 232
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
18-230 |
3.02e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 81.82 E-value: 3.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddEDISLLPLHARARRGIGYLPQEASIFRRLS--- 94
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHELITNPYSKKIKNFKELRrrv 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 --VFDnlMAVLQIRDDlTSE-----------QRQDRANELmEEFHIEHL--------RDSLGqaLSGGERRRVEIARALA 153
Cdd:PRK13631 119 smVFQ--FPEYQLFKD-TIEkdimfgpvalgVKKSEAKKL-AKFYLNKMglddsyleRSPFG--LSGGQKRRVAIAGILA 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDDHV 230
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
7-215 |
3.98e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 79.92 E-value: 3.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL-----PLharARRGI 80
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPF---LRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLmAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFIL 160
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNL 215
Cdd:PRK10908 161 ADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-226 |
4.81e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 82.45 E-value: 4.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR-----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVpRDAGNIIIDDEdisllPL 72
Cdd:PRK15134 276 LDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQ-----PL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 73 HARARRGIgyLPqeasiFRRL---------SVFDNLMAVLQI--------RDDLTSEQRQDRANELMEEFHIE-HLRDSL 134
Cdd:PRK15134 350 HNLNRRQL--LP-----VRHRiqvvfqdpnSSLNPRLNVLQIieeglrvhQPTLSAAQREQQVIAVMEEVGLDpETRHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 135 GQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETLAVCERAYIVSQG 213
Cdd:PRK15134 423 PAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQG 502
|
250
....*....|...
6MIT_B 214 NLIAHGTPQQILE 226
Cdd:PRK15134 503 EVVEQGDCERVFA 515
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
21-197 |
5.79e-18 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 82.16 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEI-----VGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIdDEDISllplhararrgigYLPQEASIFRRLSV 95
Cdd:PRK13409 352 DFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKIS-------------YKPQYIKPDYDGTV 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 FDNLMavlQIRDDLTSEQRQdraNELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVD---PIS 172
Cdd:PRK13409 418 EDLLR---SITDDLGSSYYK---SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLA 491
|
170 180
....*....|....*....|....*.
6MIT_B 173 VID-IKRIIEhlrDSGLGVLITDHNV 197
Cdd:PRK13409 492 VAKaIRRIAE---EREATALVVDHDI 514
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-218 |
8.84e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 81.88 E-value: 8.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEASIFRRLSVFDNLM--AVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKF 158
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYlgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAH 218
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAT 221
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
7-169 |
9.00e-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: 79.05 E-value: 9.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGR---RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYL 83
Cdd:cd03248 15 QNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRlSVFDNLMAVLQIRDDLTSEQRQDRAN------ELMEEFHIEhlRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:cd03248 94 GQEPVLFAR-SLQDNIAYGLQSCSFECVKEAAQKAHahsfisELASGYDTE--VGEKGSQLSGGQKQRVAIARALIRNPQ 170
|
170
....*....|..
6MIT_B 158 FILLDEPFAGVD 169
Cdd:cd03248 171 VLILDEATSALD 182
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
4-227 |
1.04e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.75 E-value: 1.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAY------KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTT-TFYMVVGIVPRDaGNIIIDDEDISLLPLHARA 76
Cdd:PRK13633 5 IKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTiAKHMNALLIPSE-GKVYVDGLDTSDEENLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 77 RRGIGYLPQEAsifrrlsvfDNLMAVLQIRDDLT---------SEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVE 147
Cdd:PRK13633 84 RNKAGMVFQNP---------DNQIVATIVEEDVAfgpenlgipPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 148 IARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETlAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFK 233
|
.
6MIT_B 227 D 227
Cdd:PRK13633 234 E 234
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-227 |
1.24e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 81.44 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIGYLPQE--ASIFRRLS 94
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqALRRDIQFIFQDpyASLDPRQT 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLMAVLQIRDDLTSEQRQDRANELMEEFHI--EHLRdSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVD-PI 171
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLlpEHAW-RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDvSI 498
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 172 SVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
20-197 |
1.35e-17 |
|
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: 81.37 E-value: 1.35e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 20 EDVSLTVNSG-----EIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiidDEDISllplhararrgIGYLPQEASIFRRLS 94
Cdd:COG1245 352 GGFSLEVEGGeiregEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV---DEDLK-----------ISYKPQYISPDYDGT 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLMAVlqIRDDLTSEQRQdraNELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVD---PI 171
Cdd:COG1245 418 VEEFLRSA--NTDDFGSSYYK---TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRL 492
|
170 180
....*....|....*....|....*..
6MIT_B 172 SVID-IKRIIEhlrDSGLGVLITDHNV 197
Cdd:COG1245 493 AVAKaIRRFAE---NRGKTAMVVDHDI 516
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-234 |
1.59e-17 |
|
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: 81.50 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYK--GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLHaRARRGIG 81
Cdd:TIGR01271 1218 MDVQGLTAKYTeaGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQ-TWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRlSVFDNLMAVLQIRDdltsEQRQDRANELMEEFHIEHLRDSL-------GQALSGGERRRVEIARALAA 154
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLDPYEQWSD----EEIWKVAEEVGLKSVIEQFPDKLdfvlvdgGYVLSNGHKQLMCLARSILS 1370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRdSGLGVLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQIL-EDDHVKRV 233
Cdd:TIGR01271 1371 KAKILLLDEPSAHLDPVTLQIIRKTLKQSF-SNCTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLnETSLFKQA 1448
|
.
6MIT_B 234 Y 234
Cdd:TIGR01271 1449 M 1449
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-228 |
1.75e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.18 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRLSVFd 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGL-TDLRRVLSIIPQSPVLFSGTVRF- 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 98 NLmavlqirdDLTSEQRQdraNELMEEFHIEHLRDSL--------------GQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:PLN03232 1329 NI--------DPFSEHND---ADLWEALERAHIKDVIdrnpfgldaevsegGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 164 PFAGVDPISVIDIKRII-EHLRDSGLgvLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIrEEFKSCTM--LVIAHRL-NTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-169 |
1.77e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 79.92 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-------EDISLLPlharARRGIGYLPQEASIFRRL 93
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGICLPP----EKRRIGYVFQDARLFPHY 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 94 SVFDNL---MAvlqirddltsEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVD 169
Cdd:PRK11144 92 KVRGNLrygMA----------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
18-222 |
1.77e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 80.92 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL---PLHARARRGIGYLPQEASIFRRLS 94
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLmAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVI 174
Cdd:PRK10535 103 AAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
6MIT_B 175 DIKRIIEHLRDSGLGVLITDHNvRETLAVCERAYIVSQGNLIAHGTPQ 222
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTHD-PQVAAQAERVIEIRDGEIVRNPPAQ 228
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-227 |
2.43e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 78.90 E-value: 2.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD----EDISLLPLHARARRGIGYLPQ--EASIF 90
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDyaipANLKKIKEVKRLRKEIGLVFQfpEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 91 RRLSVFDNLMAVLQIRDDltSEQRQDRANELMEEFHI--EHLRDSLGQaLSGGERRRVEIARALAANPKFILLDEPFAGV 168
Cdd:PRK13645 105 QETIEKDIAFGPVNLGEN--KQEAYKKVPELLKLVQLpeDYVKRSPFE-LSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 169 DPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK13645 182 DPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
16-236 |
2.51e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 78.63 E-value: 2.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA---RARRGIGYLPQ--EASIF 90
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQfpESQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 91 RRLSVFDnlMAVLQIRDDLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVD 169
Cdd:PRK13649 100 EETVLKD--VAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 170 PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED-DHVKRVYLG 236
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvDFLEEKQLG 245
|
|
| 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
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDIS-------LLPLhaRARRGIGYLPQEAS 88
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkkLKPL--RKKVGIVFQFPEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 89 IFRRLSVFDnlMAVLQIRDDLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAG 167
Cdd:PRK13634 98 LFEETVEKD--ICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 168 VDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-228 |
3.98e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.28 E-value: 3.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD-------EDISLLPLhaRARRGIGYLPQEASIFR 91
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDitithktKDKYIRPV--RKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 92 RLSVFDNLMAVLQIRDDLtsEQRQDRANELMEEFHIEhlRDSLGQA---LSGGERRRVEIARALAANPKFILLDEPFAGV 168
Cdd:PRK13646 101 DTVEREIIFGPKNFKMNL--DEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPTAGL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 169 DPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:PRK13646 177 DPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-225 |
4.54e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.57 E-value: 4.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLakayKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYL 83
Cdd:PRK11288 258 LRLDGL----KGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLC 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQ---EASIFRRLSVFDNLmAVLQIRDDLTS----EQRQDRANelmEEFHIEHL------RDSLGQALSGGERRRVEIAR 150
Cdd:PRK11288 334 PEdrkAEGIIPVHSVADNI-NISARRHHLRAgcliNNRWEAEN---ADRFIRSLniktpsREQLIMNLSGGNQQKAILGR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 151 ALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLI-----AHGTPQQIL 225
Cdd:PRK11288 410 WLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAgelarEQATERQAL 489
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-228 |
6.28e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 6.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 2 ATLTAKNLAKAYKGR--RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRG 79
Cdd:PRK11160 337 VSLTLNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAALRQA 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRlSVFDNL-MAVLQIRDDltseqrqdRANELMEEFHIEHLRDS----------LGQALSGGERRRVEI 148
Cdd:PRK11160 416 ISVVSQRVHLFSA-TLRDNLlLAAPNASDE--------ALIEVLQQVGLEKLLEDdkglnawlgeGGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 149 ARALAANPKFILLDEPFAGVDPISVIDIKRII-EHLRDSGLgVLITdHNVREtLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLaEHAQNKTV-LMIT-HRLTG-LEQFDRICVMDNGQIIEQGTHQELLAQ 563
|
.
6MIT_B 228 D 228
Cdd:PRK11160 564 Q 564
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-193 |
8.67e-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: 78.82 E-value: 8.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 5 TAKNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprdagniiidDEDISllpLHARARRGI--G 81
Cdd:TIGR03719 6 TMNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKDFN---GEARPQPGIkvG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLM-AVLQIRDDLtseqrqDRANELMEEF-------------------HIEH------------ 129
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEeGVAEIKDAL------DRFNEISAKYaepdadfdklaaeqaelqeIIDAadawdldsqlei 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 130 ----LR----DSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRiieHLRD-SGLGVLIT 193
Cdd:TIGR03719 146 amdaLRcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEyPGTVVAVT 215
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-227 |
1.31e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 76.76 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKG--RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIV-PRDAGNIIIDDEDISLLP---LHARAR 77
Cdd:PRK13640 6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlPDDNPNSKITVDGITLTAktvWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 78 RGIGYLPQEASiFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:PRK13640 86 VGIVFQNPDNQ-FVGATVGDDVAFGLENRA-VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETlAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK13640 164 IIILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-169 |
1.92e-16 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 76.37 E-value: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGR---------RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA 74
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 75 RARRgIGYLPQEA--SIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIehLRDSLG---QALSGGERRRVEIA 149
Cdd:PRK15112 85 RSQR-IRMIFQDPstSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGL--LPDHASyypHMLAPGQKQRLGLA 161
|
170 180
....*....|....*....|
6MIT_B 150 RALAANPKFILLDEPFAGVD 169
Cdd:PRK15112 162 RALILRPKVIIADEALASLD 181
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-173 |
1.94e-16 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 76.93 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR----------VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLH 73
Cdd:PRK11308 6 LQAIDLKKHYPVKRglfkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 74 ARA--RRGIGYLPQE--ASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHI--EHLrDSLGQALSGGERRRVE 147
Cdd:PRK11308 86 AQKllRQKIQIVFQNpyGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLrpEHY-DRYPHMFSGGQRQRIA 164
|
170 180
....*....|....*....|....*.
6MIT_B 148 IARALAANPKFILLDEPFAGVDpISV 173
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALD-VSV 189
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-206 |
2.30e-16 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 74.89 E-value: 2.30e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRGIGYL 83
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT----RGDRSRFMAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNL--MAVLQIRddltsEQRQDRANELMEEFHIEHlRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:PRK13543 88 GHLPGLKADLSTLENLhfLCGLHGR-----RAKQMPGSALAIVGLAGY-EDTLVRQLSAGQKKRLALARLWLSPAPLWLL 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
6MIT_B 162 DEPFAGVDPISVIDIKRIIE-HLRDSGlGVLITDHNVRETLAVCER 206
Cdd:PRK13543 162 DEPYANLDLEGITLVNRMISaHLRGGG-AALVTTHGAYAAPPVRTR 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-202 |
3.79e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 77.15 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII-DDEDISLLPLHArarrgigYLPQeasifrrl 93
Cdd:COG4178 375 GRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLPQRP-------YLPL-------- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 svfDNLMAVL---QIRDDLTSEQrqdrANELMEEFHIEHLRDSL------GQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:COG4178 440 ---GTLREALlypATAEAFSDAE----LREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEA 512
|
170 180 190
....*....|....*....|....*....|....*....
6MIT_B 165 FAGVDPISVIDI-KRIIEHLRDSGLgVLITdHnvRETLA 202
Cdd:COG4178 513 TSALDEENEAALyQLLREELPGTTV-ISVG-H--RSTLA 547
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
4-195 |
6.51e-16 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 73.45 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplharaRRGIGYL 83
Cdd:PRK13540 2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--------KDLCTYQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:PRK13540 74 KQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153
|
170 180 190
....*....|....*....|....*....|..
6MIT_B 164 PFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
Cdd:PRK13540 154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
4-225 |
7.90e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 74.74 E-value: 7.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVED---VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGI 80
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVW-NLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 GYLPQEA-SIFRRLSVFDNLMAVLQiRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:PRK13642 84 GMVFQNPdNQFVGATVEDDVAFGME-NQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 160 LLDEPFAGVDPISVIDIKRIIEHLRDS-GLGVLITDHNVRETlAVCERAYIVSQGNLIAHGTPQQIL 225
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-215 |
1.06e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.81 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQEasifRR------ 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISED----RKrdglvl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 93 -LSVFDNlMAVLQIRD------DLTSEQRQDRANELMEEFHIEhlRDSLGQA---LSGGERRRVEIARALAANPKFILLD 162
Cdd:PRK10762 344 gMSVKEN-MSLTALRYfsraggSLKHADEQQAVSDFIRLFNIK--TPSMEQAiglLSGGNQQKVAIARGLMTRPKVLILD 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
6MIT_B 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNL 215
Cdd:PRK10762 421 EPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-164 |
1.30e-15 |
|
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: 75.36 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplhararrgigylpq 85
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE--------------------- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 easifrrlSVfdNLMAVLQIRDDLTS-----EQRQDRANELMEEFHIEHLRDSLGQ-------------ALSGGERRRVE 147
Cdd:TIGR03719 384 --------TV--KLAYVDQSRDALDPnktvwEEISGGLDIIKLGKREIPSRAYVGRfnfkgsdqqkkvgQLSGGERNRVH 453
|
170
....*....|....*..
6MIT_B 148 IARALAANPKFILLDEP 164
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEP 470
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-229 |
1.99e-15 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 74.17 E-value: 1.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLA---KAYKGR-RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAgnIIIDD----EDISLLPL 72
Cdd:COG4170 1 MPLLDIRNLTieiDTPQGRvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNW--HVTADrfrwNGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 73 HARARRGIgyLPQE-ASIFRR--------LSVFDNLMAVLQiRDDLTS------EQRQDRANELMEEFHI---EHLRDSL 134
Cdd:COG4170 79 SPRERRKI--IGREiAMIFQEpsscldpsAKIGDQLIEAIP-SWTFKGkwwqrfKWRKKRAIELLHRVGIkdhKDIMNSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 135 GQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQG 213
Cdd:COG4170 156 PHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCG 235
|
250
....*....|....*.
6MIT_B 214 NLIAHGTPQQILEDDH 229
Cdd:COG4170 236 QTVESGPTEQILKSPH 251
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-229 |
2.51e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 74.77 E-value: 2.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQEASIFRRLSVFd 97
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGL-MDLRKVLGIIPQAPVLFSGTVRF- 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 98 NLmavlqirdDLTSEQRQDRANELMEEFHIEHL--RDSL---------GQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:PLN03130 1332 NL--------DPFNEHNDADLWESLERAHLKDVirRNSLgldaevseaGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 167 GVDPISVIDI-KRIIEHLRDSGLgvLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQILEDDH 229
Cdd:PLN03130 1404 AVDVRTDALIqKTIREEFKSCTM--LIIAHRL-NTIIDCDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-227 |
2.81e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 72.86 E-value: 2.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhARARRGIGYLPQE------ASIFRRLS 94
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNF-EKLRKHIGIVFQNpdnqfvGSIVKYDV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VF--DNLMavlqirddLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPIS 172
Cdd:PRK13648 106 AFglENHA--------VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 173 VIDIKRIIEHLR-DSGLGVLITDHNVRETLavcERAYIV--SQGNLIAHGTPQQILED 227
Cdd:PRK13648 178 RQNLLDLVRKVKsEHNITIISITHDLSEAM---EADHVIvmNKGTVYKEGTPTEIFDH 232
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-195 |
3.43e-15 |
|
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: 71.51 E-value: 3.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDISLLPLHARARRGIGYLPQEasifrrlsv 95
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG---RKTAGVITGEILINGRPLDKNFQRSTGYVEQQ--------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 fDNLMAVLQIRDDLtseqrqdranelmeEFHiEHLRdslgqALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
Cdd:cd03232 88 -DVHSPNLTVREAL--------------RFS-ALLR-----GLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|
6MIT_B 176 IKRIIEHLRDSGLGVLITDH 195
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIH 166
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-195 |
3.84e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.37 E-value: 3.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDIS-LLPLHARARRGIGYLPQEASIFRRLS 94
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE---RVTTGVITGGDRLVnGRPLDSSFQRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLM--AVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSL----GQALSGGERRRVEIARALAANPKFIL-LDEPFAG 167
Cdd:TIGR00956 853 VRESLRfsAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSG 932
|
170 180
....*....|....*....|....*...
6MIT_B 168 VDPISVIDIKRIIEHLRDSGLGVLITDH 195
Cdd:TIGR00956 933 LDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-163 |
8.18e-15 |
|
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: 72.93 E-value: 8.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 12 AYKGRR-VVEDVSLTVNSGEIVGLLGPNGAGKTTT------FYMVvgivprDAGNIIIDDEDISLLPLHArARRGIGYLP 84
Cdd:COG5265 366 GYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLarllfrFYDV------TSGRILIDGQDIRDVTQAS-LRAAIGIVP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QEASIFRRlSVFDNlmavlqI---RDDLTSEQRQD--RANELmEEFhIEHLRDSL-------GQALSGGERRRVEIARAL 152
Cdd:COG5265 439 QDTVLFND-TIAYN------IaygRPDASEEEVEAaaRAAQI-HDF-IESLPDGYdtrvgerGLKLSGGEKQRVAIARTL 509
|
170
....*....|.
6MIT_B 153 AANPKFILLDE 163
Cdd:COG5265 510 LKNPPILIFDE 520
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-226 |
9.93e-15 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 70.88 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 11 KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLhararrGIGYLPQeasif 90
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLEL------GAGFHPE----- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 91 rrLSVFDNLMAVLQIRdDLTSEQRQDRANElMEEFhiehlrdS-LGQAL-------SGGERRRVEIARALAANPKFILLD 162
Cdd:COG1134 103 --LTGRENIYLNGRLL-GLSRKEIDEKFDE-IVEF-------AeLGDFIdqpvktySSGMRARLAFAVATAVDPDILLVD 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 163 EpfagVdpISVIDI------KRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:COG1134 172 E----V--LAVGDAafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-164 |
1.48e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.46 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplhararrgigylpq 85
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE--------------------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 easifrrlSVfdNLMAVLQIRDDLtseqrqDRANELMEEF-----HIEhlrdsLGQA----------------------- 137
Cdd:PRK11819 386 --------TV--KLAYVDQSRDAL------DPNKTVWEEIsggldIIK-----VGNReipsrayvgrfnfkggdqqkkvg 444
|
170 180
....*....|....*....|....*...
6MIT_B 138 -LSGGERRRVEIARALAANPKFILLDEP 164
Cdd:PRK11819 445 vLSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-224 |
1.49e-14 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 71.69 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtfymvvGIVPRDagniiIDDEDISLLP-------LHARA-RR 78
Cdd:NF000106 17 RGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAH-----V*GPDAGRRPwrf*twcANRRAlRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 79 GIG-YLPQEASIFRRLSVFDNLMAVLQIRDdLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPK 157
Cdd:NF000106 86 TIG*HRPVR*GRRESFSGRENLYMIGR*LD-LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
6MIT_B 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
5-164 |
2.06e-14 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 72.07 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 5 TAKNLAKAYKGRRVV-EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIvprdagniiidDEDISllpLHARARRG--IG 81
Cdd:PRK11819 8 TMNRVSKVVPPKKQIlKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV-----------DKEFE---GEARPAPGikVG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLM-AVLQIRDDLtseqrqDRANELMEEF-------------------HIEH------------ 129
Cdd:PRK11819 74 YLPQEPQLDPEKTVRENVEeGVAEVKAAL------DRFNEIYAAYaepdadfdalaaeqgelqeIIDAadawdldsqlei 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
6MIT_B 130 ----LR----DSLGQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:PRK11819 148 amdaLRcppwDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
1-185 |
4.00e-14 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 68.44 E-value: 4.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNL----AKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDA---GNIIIDDEDIslLPLH 73
Cdd:cd03233 1 ASTLSWRNIsfttGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPY--KEFA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 74 ARARRGIGYLPQEASIFRRLSVFDNLMAVLQIRDDltseqrqdranelmeefhiEHLRdslgqALSGGERRRVEIARALA 153
Cdd:cd03233 79 EKYPGEIIYVSEEDVHFPTLTVRETLDFALRCKGN-------------------EFVR-----GISGGERKRVSIAEALV 134
|
170 180 190
....*....|....*....|....*....|..
6MIT_B 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHLRD 185
Cdd:cd03233 135 SRASVLCWDNSTRGLDSSTALEILKCIRTMAD 166
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
16-195 |
4.82e-14 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 71.06 E-value: 4.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD--AGNIIIDDEDISllplhARARRGIGYLPQEASIFRRL 93
Cdd:PLN03211 81 RTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT-----KQILKRTGFVTQDDILYPHL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 SVFDNLM--AVLQIRDDLTSEQRQDRANELMEEFHIEH-----LRDSLGQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:PLN03211 156 TVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTS 235
|
170 180
....*....|....*....|....*....
6MIT_B 167 GVDPISVIDIKRIIEHLRDSGLGVLITDH 195
Cdd:PLN03211 236 GLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-228 |
5.91e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 70.64 E-value: 5.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLA-KAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDaGNIIIDDEDISLLPLhARARRGIG 81
Cdd:PRK11174 349 TIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQ-GSLKINGIELRELDP-ESWRKHLS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRlSVFDNlmaVLQIRDDLTSEQRQ---DRANelMEEFhIEHLRDSL-------GQALSGGERRRVEIARA 151
Cdd:PRK11174 427 WVGQNPQLPHG-TLRDN---VLLGNPDASDEQLQqalENAW--VSEF-LPLLPQGLdtpigdqAAGLSVGQAQRLALARA 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 152 LAANPKFILLDEPFAGVDPISVidiKRIIEHLRDSGLG---VLITdHNVrETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:PRK11174 500 LLQPCQLLLLDEPTASLDAHSE---QLVMQALNAASRRqttLMVT-HQL-EDLAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-225 |
9.58e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.12 E-value: 9.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKG----RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD-----AGNIIIDDEDIsllp 71
Cdd:PRK15134 3 QPLLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESL---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 72 LHA-----RARRGigylPQEASIFRRLSVFDN--------LMAVLQIRDDLTSEQRQDRANELMEEFHIEH----LRDSL 134
Cdd:PRK15134 79 LHAseqtlRGVRG----NKIAMIFQEPMVSLNplhtlekqLYEVLSLHRGMRREAARGEILNCLDRVGIRQaakrLTDYP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 135 GQaLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQG 213
Cdd:PRK15134 155 HQ-LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
250
....*....|..
6MIT_B 214 NLIAHGTPQQIL 225
Cdd:PRK15134 234 RCVEQNRAATLF 245
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-201 |
1.27e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 66.41 E-value: 1.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII-DDEDISLLPLHararrgiGYLPQeasifrrl 93
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLPQR-------PYLPL-------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 svfdnlmavlqirddLTseqrqdranelmeefhiehLRDSL----GQALSGGERRRVEIARALAANPKFILLDEPFAGVD 169
Cdd:cd03223 78 ---------------GT-------------------LREQLiypwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALD 123
|
170 180 190
....*....|....*....|....*....|..
6MIT_B 170 PISVidiKRIIEHLRDSGLGVLITDHnvRETL 201
Cdd:cd03223 124 EESE---DRLYQLLKELGITVISVGH--RPSL 150
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-195 |
2.37e-13 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 69.10 E-value: 2.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDISLLPLHARARRGI-GYLPQEASIFRRLSV 95
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFARIsGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 FDNLM--AVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLG-----QALSGGERRRVEIARALAANPKFILLDEPFAGV 168
Cdd:PLN03140 971 RESLIysAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180
....*....|....*....|....*..
6MIT_B 169 DPISVIDIKRIIEHLRDSGLGVLITDH 195
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
7-183 |
3.09e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 68.50 E-value: 3.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllpLHARaRRG------- 79
Cdd:PRK10938 264 NNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYSNDLT---------LFGR-RRGsgetiwd 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 ----IGYLPQEASIFRRLSV----------FDNLmAVLQIrddlTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERR 144
Cdd:PRK10938 334 ikkhIGYVSSSLHLDYRVSTsvrnvilsgfFDSI-GIYQA----VSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQR 408
|
170 180 190
....*....|....*....|....*....|....*....
6MIT_B 145 RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL 183
Cdd:PRK10938 409 LALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVL 447
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-226 |
6.84e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 67.46 E-value: 6.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllplHARARRG----IGYLPQ--E 86
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA----DARHRRAvcprIAYMPQglG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ASIFRRLSVFDNLmavlqirdD-------LTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFI 159
Cdd:NF033858 87 KNLYPTLSVFENL--------DffgrlfgQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 160 LLDEPFAGVDPISvidikR-----IIEHLRDS--GLGVLI-TdhnvretlavcerAYI-----------VSQGNLIAHGT 220
Cdd:NF033858 159 ILDEPTTGVDPLS-----RrqfweLIDRIRAErpGMSVLVaT-------------AYMeeaerfdwlvaMDAGRVLATGT 220
|
....*.
6MIT_B 221 PQQILE 226
Cdd:NF033858 221 PAELLA 226
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-226 |
8.29e-13 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.05 E-value: 8.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIGYLPQ 85
Cdd:PRK10790 344 DNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 EASIFRRlSVFDNLMAVLQIRDD-----LTSEQRQDRANELMEEFHiEHLRDSlGQALSGGERRRVEIARALAANPKFIL 160
Cdd:PRK10790 423 DPVVLAD-TFLANVTLGRDISEEqvwqaLETVQLAELARSLPDGLY-TPLGEQ-GNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdHNVR-----ETLAVCERAYIVSQGNliaHgtpQQILE 226
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLStiveaDTILVLHRGQAVEQGT---H---QQLLA 563
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-197 |
1.68e-12 |
|
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: 64.03 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIddedisllplharaRRGIGYLPQEASIFRRlSVFD 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--------------PGSIAYVSQEPWIQNG-TIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 98 NLMAVLQIRddltsEQRQD---RANELMEEFHIEHLRD-----SLGQALSGGERRRVEIARALAANPKFILLDEPFAGVD 169
Cdd:cd03250 85 NILFGKPFD-----EERYEkviKACALEPDLEILPDGDlteigEKGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVD 159
|
170 180 190
....*....|....*....|....*....|
6MIT_B 170 PISVIDI--KRIIEHLRDSGLGVLITdHNV 197
Cdd:cd03250 160 AHVGRHIfeNCILGLLLNNKTRILVT-HQL 188
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-164 |
1.82e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 66.07 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplHARarrgIGYL 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE--------NAN----IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASifrrlSVFDNLMAVLqirdDLTSEQRQDRANELMeefhiehLRDSLG-------------QALSGGERRRVEIAR 150
Cdd:PRK15064 388 AQDHA-----YDFENDLTLF----DWMSQWRQEGDDEQA-------VRGTLGrllfsqddikksvKVLSGGEKGRMLFGK 451
|
170
....*....|....
6MIT_B 151 ALAANPKFILLDEP 164
Cdd:PRK15064 452 LMMQKPNVLVMDEP 465
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
22-215 |
2.41e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 64.03 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEASIFRRLSVFDN 98
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlraKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 99 LMAVLQIRDDlTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
Cdd:PRK10584 109 VELPALLRGE-SSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIAD 187
|
170 180 190
....*....|....*....|....*....|....*...
6MIT_B 179 IIEHL-RDSGLGVLITDHNVReTLAVCERAYIVSQGNL 215
Cdd:PRK10584 188 LLFSLnREHGTTLILVTHDLQ-LAARCDRRLRLVNGQL 224
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
17-229 |
3.59e-12 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 64.82 E-value: 3.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGiVPRDAGNIIIDD---EDISLLPLHARARR-----GIGYLPQE-- 86
Cdd:PRK15093 21 KAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTADRmrfDDIDLLRLSPRERRklvghNVSMIFQEpq 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 87 ------ASIFRRLsvfdnlmavLQIRDDLTSEQ--------RQDRANELMEEFHIEHLRDSLGQ---ALSGGERRRVEIA 149
Cdd:PRK15093 100 scldpsERVGRQL---------MQNIPGWTYKGrwwqrfgwRKRRAIELLHRVGIKDHKDAMRSfpyELTEGECQKVMIA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILEDD 228
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250
|
.
6MIT_B 229 H 229
Cdd:PRK15093 251 H 251
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-198 |
5.72e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.51 E-value: 5.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG-----IVprdAGNIIIDDEDISLLPLHARARR 78
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpaykIL---EGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 79 GIGYLPQEASIFRRLSVFDNLMAVLQirddltSEQRQDRANELMEEFHIEHLRDSL--------------GQALSGGERR 144
Cdd:CHL00131 85 GIFLAFQYPIEIPGVSNADFLRLAYN------SKRKFQGLPELDPLEFLEIINEKLklvgmdpsflsrnvNEGFSGGEKK 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 145 RVEIARALAANPKFILLDEPFAGVDpisvIDIKRIIEH----LRDSGLGVLITDHNVR 198
Cdd:CHL00131 159 RNEILQMALLDSELAILDETDSGLD----IDALKIIAEginkLMTSENSIILITHYQR 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
7-218 |
7.74e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 64.27 E-value: 7.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTT------FYMVvgivprDAGNIIIDDEDISLLPLhARARR 78
Cdd:PRK11176 345 RNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIanlltrFYDI------DEGEILLDGHDLRDYTL-ASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 79 GIGYLPQEASIFRRlSVFDNLMAVlqiRDDLTSEQRQDRANEL---MEefHIEHLRDSL-------GQALSGGERRRVEI 148
Cdd:PRK11176 418 QVALVSQNVHLFND-TIANNIAYA---RTEQYSREQIEEAARMayaMD--FINKMDNGLdtvigenGVLLSGGQRQRIAI 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 149 ARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLI-----TDHNVRETLaVCERAYIVSQGN---LIAH 218
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKNRTSLVIahrlsTIEKADEIL-VVEDGEIVERGThaeLLAQ 568
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
19-227 |
7.88e-12 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 63.96 E-value: 7.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDisLLPLHAR----ARRGIGYLPQE--ASIFRR 92
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKD--LLGMKDDewraVRSDIQMIFQDplASLNPR 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 93 LSVFDNLMAVLQI-RDDLTSEQRQDRANELMEEFHI-EHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDp 170
Cdd:PRK15079 115 MTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD- 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 171 IS----VIDIKRIIEhlRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK15079 194 VSiqaqVVNLLQQLQ--REMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-213 |
9.06e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 62.79 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVP----RDAGNIIIDDEdisllPLHARARRGIgylpQEASIFR 91
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPagvrQTAGRVLLDGK-----PVAPCALRGR----KIATIMQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 92 R-LSVFDNL--MAVlQIRDDLTSEQRQDRANELMEEFHIEHLRDSLGQA------LSGGERRRVEIARALAANPKFILLD 162
Cdd:PRK10418 87 NpRSAFNPLhtMHT-HARETCLALGKPADDATLTAALEAVGLENAARVLklypfeMSGGMLQRMMIALALLCEAPFIIAD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 163 EPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNV------RETLAVCERAYIVSQG 213
Cdd:PRK10418 166 EPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMgvvarlADDVAVMSHGRIVEQG 223
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-169 |
9.91e-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: 64.20 E-value: 9.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRrlsvfd 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLH-DLRFKITIIPQDPVLFS------ 1373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 98 nlmAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSL-----------GQALSGGERRRVEIARALAANPKFILLDEPFA 166
Cdd:TIGR00957 1374 ---GSLRMNLDPFSQYSDEEVWWALELAHLKTFVSALpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLDEATA 1450
|
...
6MIT_B 167 GVD 169
Cdd:TIGR00957 1451 AVD 1453
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-224 |
2.17e-11 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 62.43 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD---AGNIIIDDEDISLLPLHA----RARrgigylpQEASIFR 91
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnklRAE-------QISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 92 R--------LSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSLG---QALSGGERRRVEIARALAANPKFIL 160
Cdd:PRK09473 105 DpmtslnpyMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKmypHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 161 LDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGTPQQI 224
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELkREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-213 |
3.37e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 3.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGYLPQE---ASIFRRLSV 95
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEErrsTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 -FDNLMAvlQIRDDLTSEQRQDraNELME---EFHIEHLR-------DSLGqALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:PRK10982 344 gFNSLIS--NIRNYKNKVGLLD--NSRMKsdtQWVIDSMRvktpghrTQIG-SLSGGNQQKVIIGRWLLTQPEILMLDEP 418
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
6MIT_B 165 FAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQG 213
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNG 467
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-201 |
6.14e-11 |
|
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: 61.69 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDdedisllplharARRGIGYLPQEAsifrrls 94
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------AKGKLFYVPQRP------- 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 vfdnLMAVLQIRDDL----TSEQRQDRA------NELMEEFHIEHLRDSLG---------QALSGGERRRVEIARALAAN 155
Cdd:TIGR00954 525 ----YMTLGTLRDQIiypdSSEDMKRRGlsdkdlEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHK 600
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
6MIT_B 156 PKFILLDEPFAGVDPisviDIK-RIIEHLRDSGLGVLITDHnvRETL 201
Cdd:TIGR00954 601 PQFAILDECTSAVSV----DVEgYMYRLCREFGITLFSVSH--RKSL 641
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
4-224 |
9.89e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 9.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedislLPLHARARRG 79
Cdd:PRK10261 13 LAVENLNIAFMQEQqkiaAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK-----MLLRRRSRQV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRLS------VFDNLMAVL--------QIRDDLTSEQRQDR------ANELMEEFHIEHLRDSLGQ--- 136
Cdd:PRK10261 88 IELSEQSAAQMRHVRgadmamIFQEPMTSLnpvftvgeQIAESIRLHQGASReeamveAKRMLDQVRIPEAQTILSRyph 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 137 ALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGNL 215
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
|
....*....
6MIT_B 216 IAHGTPQQI 224
Cdd:PRK10261 248 VETGSVEQI 256
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-217 |
2.37e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.80 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 15 GRRVVEDVSLTVNSGEIVGLLGPNGAGKTTtFYMVV-------GIvprdAGNIIIDDEDISLLPLHARARRGIGY----- 82
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMSVfgrsygrNI----SGTVFKDGKEVDVSTVSDAIDAGLAYvtedr 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 83 ----LPQEASIFRRLSVfDNLMAVlqIRDDLTSEQRQDR-ANELMEEFHIEhlRDSLGQA---LSGGERRRVEIARALAA 154
Cdd:NF040905 347 kgygLNLIDDIKRNITL-ANLGKV--SRRGVIDENEEIKvAEEYRKKMNIK--TPSVFQKvgnLSGGNQQKVVLSKWLFT 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 155 NPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIA 217
Cdd:NF040905 422 DPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITG 484
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-224 |
3.34e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 58.98 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 1 MATLTAKNLAKAYKGR----RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD----AGNIIIDDEDisLLPL 72
Cdd:PRK11022 1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPgrvmAEKLEFNGQD--LQRI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 73 HARARRGIgYLPQEASIFRR--------LSVFDNLMAVLQIRDDLTSEQRQDRANELMEEFHI---EHLRDSLGQALSGG 141
Cdd:PRK11022 79 SEKERRNL-VGAEVAMIFQDpmtslnpcYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 142 ERRRVEIARALAANPKFILLDEPFAGVD-PISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLIAHGT 220
Cdd:PRK11022 158 MSQRVMIAMAIACRPKLLIADEPTTALDvTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGK 237
|
....
6MIT_B 221 PQQI 224
Cdd:PRK11022 238 AHDI 241
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-164 |
4.16e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 59.19 E-value: 4.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 24 LTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID-DEDISLL----PLHARAR------RGIGYLPQEASIFRR 92
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqDLIVARLqqdpPRNVEGTvydfvaEGIEEQAEYLKRYHD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 93 LSV---FD------NLMAVLQ-IRDDLTSEQRQDRANELMEEFHIEhlRDSLGQALSGGERRRVEIARALAANPKFILLD 162
Cdd:PRK11147 104 ISHlveTDpseknlNELAKLQeQLDHHNLWQLENRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLD 181
|
..
6MIT_B 163 EP 164
Cdd:PRK11147 182 EP 183
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-196 |
4.80e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 58.15 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 25 TVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplhaRARRGI---GYLPQ----EASIFRRLSVFD 97
Cdd:cd03236 22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEIL----DEFRGSelqNYFTKllegDVKVIVKPQYVD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 98 NLMAVLQ--IRDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
Cdd:cd03236 98 LIPKAVKgkVGELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN 177
|
170 180
....*....|....*....|.
6MIT_B 176 IKRIIEHLRDSGLGVLITDHN 196
Cdd:cd03236 178 AARLIRELAEDDNYVLVVEHD 198
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
7-216 |
5.03e-10 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 59.03 E-value: 5.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD--AGNIIIDDEDISLLPLHARARRGIGYLP 84
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIVIIH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 85 QEASIFRRLSVFDNLMavlqirddLTSEQRQ----------DRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAA 154
Cdd:NF040905 85 QELALIPYLSIAENIF--------LGNERAKrgvidwnetnRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
6MIT_B 155 NPKFILLDEPFAGV---DPISVIDikrIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGNLI 216
Cdd:NF040905 157 DVKLLILDEPTAALneeDSAALLD---LLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
116-227 |
5.38e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 58.87 E-value: 5.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 116 DRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDH 195
Cdd:PRK10938 114 ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLN 193
|
90 100 110
....*....|....*....|....*....|..
6MIT_B 196 NVRETLAVCERAYIVSQGNLIAHGTPQQILED 227
Cdd:PRK10938 194 RFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
55-235 |
1.93e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.35 E-value: 1.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 55 RDAGNIIIDDEDISLLPLHaRARRGIGYLPQEASIFRrLSVFDNLMAVlqiRDDLTSEQRQdRANEL--MEEFhIEHLRD 132
Cdd:PTZ00265 1274 KNSGKILLDGVDICDYNLK-DLRNLFSIVSQEPMLFN-MSIYENIKFG---KEDATREDVK-RACKFaaIDEF-IESLPN 1346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 133 SL-------GQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITdhnVRETLAVCE 205
Cdd:PTZ00265 1347 KYdtnvgpyGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT---IAHRIASIK 1423
|
170 180 190
....*....|....*....|....*....|....*....
6MIT_B 206 RA-YIVSQGN-------LIAHGTPQQILE-DDHVKRVYL 235
Cdd:PTZ00265 1424 RSdKIVVFNNpdrtgsfVQAHGTHEELLSvQDGVYKKYV 1462
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-198 |
3.89e-09 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 55.18 E-value: 3.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGI--VPRDAGNIIIDDEDISLLPLHARARRGI- 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 81 ---GYLPQEASIFRRLSVFDNLMAVLQIRdDLTSEQRQDRANELMEEFHI-----EHLRDSLGQALSGGERRRVEIARAL 152
Cdd:PRK09580 82 mafQYPVEIPGVSNQFFLQTALNAVRSYR-GQEPLDRFDFQDLMEEKIALlkmpeDLLTRSVNVGFSGGEKKRNDILQMA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
6MIT_B 153 AANPKFILLDEPFAGVDpisvIDIKRIIEH----LRDSGLGVLITDHNVR 198
Cdd:PRK09580 161 VLEPELCILDESDSGLD----IDALKIVADgvnsLRDGKRSFIIVTHYQR 206
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-195 |
8.15e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 8.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPR--DAGNIIIDDEDIsllplhararrgigylPQEASIFRRL 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtpVAGCVDVPDNQF----------------GREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 94 SVFDNLMAVLQIrddLTSEQRQDRANeLMEEFHiehlrdslgqALSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
Cdd:COG2401 107 GRKGDFKDAVEL---LNAVGLSDAVL-WLRRFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTA 172
|
170 180
....*....|....*....|...
6MIT_B 174 IDIKRIIEHL-RDSGLGVLITDH 195
Cdd:COG2401 173 KRVARNLQKLaRRAGITLVVATH 195
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
18-226 |
8.32e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 55.49 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA-RARRGIgyLPQEASIFRRlSVF 96
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAV--VSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 97 DNLMAVlqiRDDLTSEQRQDRANelMEEFHIEHLR---------DSLGQALSGGERRRVEIARALAANPKFILLDEPFAG 167
Cdd:PRK10789 407 NNIALG---RPDATQQEIEHVAR--LASVHDDILRlpqgydtevGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 168 VDPISVidiKRIIEHLRDSGLG--VLITDHNVrETLAVCERAYIVSQGNLIAHGTPQQILE 226
Cdd:PRK10789 482 VDGRTE---HQILHNLRQWGEGrtVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
18-176 |
9.57e-09 |
|
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: 55.30 E-value: 9.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG-IVPRD-----AGNIIIDDEDISLLPLHARARRGIGYLPQEasiFR 91
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEgkikhSGRISFSPQTSWIMPGTIKDNIIFGLSYDE---YR 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 92 RLSVfdnlMAVLQIRDDLTSEQRQDRAnELMEEfhiehlrdslGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPI 171
Cdd:TIGR01271 518 YTSV----IKACQLEEDIALFPEKDKT-VLGEG----------GITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582
|
....*
6MIT_B 172 SVIDI 176
Cdd:TIGR01271 583 TEKEI 587
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
7-184 |
1.06e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 7 KNLAKAYKGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD----EDISLlplhARARRG 79
Cdd:PTZ00265 386 KNVRFHYDTRKDVEiykDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDshnlKDINL----KWWRSK 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 80 IGYLPQEASIFRRlSVFDNLMAVLQIRDDL-------------TSEQRQDR-------------------ANELME---E 124
Cdd:PTZ00265 462 IGVVSQDPLLFSN-SIKNNIKYSLYSLKDLealsnyynedgndSQENKNKRnscrakcagdlndmsnttdSNELIEmrkN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 125 FHI--------------------------EHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKR 178
Cdd:PTZ00265 541 YQTikdsevvdvskkvlihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQK 620
|
....*.
6MIT_B 179 IIEHLR 184
Cdd:PTZ00265 621 TINNLK 626
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-197 |
4.16e-08 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 51.42 E-value: 4.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 26 VNSGEIVGLLGPNGAGKTTTFYMVvgivprdAGNIIIDDEDISLlplharARRGIGYLPQEASifrrlsvfdnlmavlqi 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKIL-------AGQLIPNGDNDEW------DGITPVYKPQYID----------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 106 rddltseqrqdranelmeefhiehlrdslgqaLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRD 185
Cdd:cd03222 72 --------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170
....*....|...
6MIT_B 186 SGL-GVLITDHNV 197
Cdd:cd03222 120 EGKkTALVVEHDL 132
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-163 |
4.19e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 53.26 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEdisllPLHARARRgiGYLPQEASIFRRLSVFDNLMA 101
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ-----PVTADNRE--AYRQLFSAVFSDFHLFDRLLG 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
6MIT_B 102 VLQIRDDltseqrqDRANELMEEFHIEH---LRDslGQ----ALSGGERRRVEIARALAANPKFILLDE 163
Cdd:COG4615 424 LDGEADP-------ARARELLERLELDHkvsVED--GRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
16-163 |
4.37e-08 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 51.80 E-value: 4.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLplharARRGIGYLPQEASIFRRLSV 95
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-----AKPYCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
6MIT_B 96 FDNLMAVLQIRDDLTSEQRQdranelMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:PRK13541 88 FENLKFWSEIYNSAETLYAA------IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
18-220 |
4.55e-08 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 52.55 E-value: 4.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplhaRARRGIGYLPQEASI-------- 89
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------KHSGRISFSSQFSWImpgtiken 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 90 ---------FRRLSVfdnlMAVLQIRDDLTSEQRQDraNELMEEFhiehlrdslGQALSGGERRRVEIARALAANPKFIL 160
Cdd:cd03291 118 iifgvsydeYRYKSV----VKACQLEEDITKFPEKD--NTVLGEG---------GITLSGGQRARISLARAVYKDADLYL 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 161 LDEPFAGVDpisVIDIKRIIE----HLRDSGLGVLITdhNVRETLAVCERAYIVSQGNLIAHGT 220
Cdd:cd03291 183 LDSPFGYLD---VFTEKEIFEscvcKLMANKTRILVT--SKMEHLKKADKILILHEGSSYFYGT 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-169 |
4.81e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 4.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivpRDAGNIIIDDEDISL--LPLH---ARARRGIGYLPQEASIF 90
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAS---NTDGFHIGVEGVITYdgITPEeikKHYRGDVVYNAETDVHF 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 91 RRLSVFDNL-----MAVLQIRDDLTSeqRQDRANEL----MEEFHIEHLRDS-----LGQALSGGERRRVEIARALAANP 156
Cdd:TIGR00956 151 PHLTVGETLdfaarCKTPQNRPDGVS--REEYAKHIadvyMATYGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGGA 228
|
170
....*....|...
6MIT_B 157 KFILLDEPFAGVD 169
Cdd:TIGR00956 229 KIQCWDNATRGLD 241
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-169 |
4.88e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 4.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG-IVPRDAGNIIIddedisllplharaRRGIGYLPQEASIFRRlS 94
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI--------------RGTVAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VFDNLMavlqirddLTSEQRQDRANELMEEFHIEHLRDSL-----------GQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:PLN03130 695 VRDNIL--------FGSPFDPERYERAIDVTALQHDLDLLpggdlteigerGVNISGGQKQRVSMARAVYSNSDVYIFDD 766
|
....*.
6MIT_B 164 PFAGVD 169
Cdd:PLN03130 767 PLSALD 772
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-195 |
1.01e-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: 1.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 28 SGEIVGLLGPNGAGKTTtfymVVGIVprdAGNII-----IDDE----DISllplhaRARRGIG---YlpqeasiFRRLSV 95
Cdd:COG1245 98 KGKVTGILGPNGIGKST----ALKIL---SGELKpnlgdYDEEpswdEVL------KRFRGTElqdY-------FKKLAN 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 fDNLMAVLQI--------------RDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILL 161
Cdd:COG1245 158 -GEIKVAHKPqyvdlipkvfkgtvRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFF 236
|
170 180 190 200
....*....|....*....|....*....|....*....|
6MIT_B 162 DEPFagvdpiSVIDIK------RIIEHLRDSGLGVLITDH 195
Cdd:COG1245 237 DEPS------SYLDIYqrlnvaRLIRELAEEGKYVLVVEH 270
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
133-198 |
1.12e-07 |
|
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: 50.40 E-value: 1.12e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
6MIT_B 133 SLGQA---LSGGERRRVEIARALAANPK--FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVR 198
Cdd:cd03238 80 TLGQKlstLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD 150
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-225 |
1.33e-07 |
|
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: 51.06 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 18 VVEDVSLTVNSGEIVGLLGPNGAGKTT---TFYMVVGIVPrdaGNIIIDDEDISLLPLHararrgigylpqeaSIFRRLS 94
Cdd:cd03288 36 VLKHVKAYIKPGQKVGICGRTGSGKSSlslAFFRMVDIFD---GKIVIDGIDISKLPLH--------------TLRSRLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 95 VF--DNLMAVLQIRDDLTSEQR--QDRANELMEEFHIEHLRDSL-----------GQALSGGERRRVEIARALAANPKFI 159
Cdd:cd03288 99 IIlqDPILFSGSIRFNLDPECKctDDRLWEALEIAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLARAFVRKSSIL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 160 LLDEPFAGVDpISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVcERAYIVSQGNLIAHGTPQQIL 225
Cdd:cd03288 179 IMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILDA-DLVLVLSRGILVECDTPENLL 242
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-220 |
1.46e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 51.90 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVG-IVPRDAGNIIIddedisllplharaRRGIGYLPQEASIFRRlSVFDNL 99
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVI--------------RGSVAYVPQVSWIFNA-TVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 100 MavlqIRDDLTSEQ--RQDRANELMEEFHIEHLRD-----SLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDP-I 171
Cdd:PLN03232 700 L----FGSDFESERywRAIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAhV 775
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
6MIT_B 172 SVIDIKRIIEHLRDSGLGVLITdhNVRETLAVCERAYIVSQGNLIAHGT 220
Cdd:PLN03232 776 AHQVFDSCMKDELKGKTRVLVT--NQLHFLPLMDRIILVSEGMIKEEGT 822
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
3-170 |
1.59e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.51 E-value: 1.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 3 TLTAKNLAKAYKGRRV-VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHArarrgig 81
Cdd:PRK10522 322 TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED------- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 82 YLPQEASIFRRLSVFDNLMavlqirddltSEQRQDRANELMEEF----------HIEHLRDSLGQaLSGGERRRVEIARA 151
Cdd:PRK10522 395 YRKLFSAVFTDFHLFDQLL----------GPEGKPANPALVEKWlerlkmahklELEDGRISNLK-LSKGQKKRLALLLA 463
|
170
....*....|....*....
6MIT_B 152 LAANPKFILLDEPFAGVDP 170
Cdd:PRK10522 464 LAEERDILLLDEWAADQDP 482
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-169 |
1.74e-07 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 51.70 E-value: 1.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGivprdagniiidDEDISllplHAR--ARRGIGYLPQEASIFRRlSVFDN 98
Cdd:PTZ00243 678 DVSVSVPRGKLTVVLGATGSGKSTLLQSLLS------------QFEIS----EGRvwAERSIAYVPQQAWIMNA-TVRGN 740
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 99 LMavlqIRDDLTSEQRQD--RANELmeEFHIEHLRDSL-------GQALSGGERRRVEIARALAANPKFILLDEPFAGVD 169
Cdd:PTZ00243 741 IL----FFDEEDAARLADavRVSQL--EADLAQLGGGLeteigekGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-164 |
1.14e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.04 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 25 TVNSGEIVGLLGPNGAGKTTTFYMVVG-IVPrdagNIIIDDEDIS---LLplhaRARRGIG---YlpqeasiFRRLSVfD 97
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKILSGeLIP----NLGDYEEEPSwdeVL----KRFRGTElqnY-------FKKLYN-G 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 98 NLMAVLQI--------------RDDLTSEQRQDRANELMEEFHIEHLRDSLGQALSGGERRRVEIARALAANPKFILLDE 163
Cdd:PRK13409 159 EIKVVHKPqyvdlipkvfkgkvRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE 238
|
.
6MIT_B 164 P 164
Cdd:PRK13409 239 P 239
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
138-196 |
2.03e-06 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 46.58 E-value: 2.03e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 138 LSGGERRRVEIARALA-ANPK---FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN 196
Cdd:cd03227 78 LSGGEKELSALALILAlASLKprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-169 |
2.06e-06 |
|
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: 48.40 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 22 VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddedisllplHARARRGIGYLPQEASIfRRLSVFDNLMA 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEG--------------HVHMKGSVAYVPQQAWI-QNDSLRENILF 721
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
6MIT_B 102 VLQIRDDLTSEQRQdrANELMEEFHIEHLRDSL-----GQALSGGERRRVEIARALAANPKFILLDEPFAGVD 169
Cdd:TIGR00957 722 GKALNEKYYQQVLE--ACALLPDLEILPSGDRTeigekGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
138-229 |
2.42e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 48.29 E-value: 2.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 138 LSGGERRRVEIARALAANPKFI--LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvRETLAVCERAYIVSQ--- 212
Cdd:PRK00635 477 LSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIIDIGPgag 555
|
90 100
....*....|....*....|
6MIT_B 213 ---GNLIAHGTPQQILEDDH 229
Cdd:PRK00635 556 ifgGEVLFNGSPREFLAKSD 575
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
20-164 |
2.45e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.96 E-value: 2.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 20 EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDedisllplHARarrgIGYLPQEASIFRRLSVFDNL 99
Cdd:PRK15064 18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDP--------NER----LGKLRQDQFAFEEFTVLDTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 100 M-------AVLQIRD-----------------DLTSE-------QRQDRANELM------EEFHiehlrDSLGQALSGGE 142
Cdd:PRK15064 86 ImghtelwEVKQERDriyalpemseedgmkvaDLEVKfaemdgyTAEARAGELLlgvgipEEQH-----YGLMSEVAPGW 160
|
170 180
....*....|....*....|..
6MIT_B 143 RRRVEIARALAANPKFILLDEP 164
Cdd:PRK15064 161 KLRVLLAQALFSNPDILLLDEP 182
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-185 |
3.35e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 14 KGRRVVED-VSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---------IDDEDISLlplharARRGIGYL 83
Cdd:PRK10636 11 RGVRVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTfpgnwqlawVNQETPAL------PQPALEYV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 84 PQEASIFRRLSVF---------DNLMAVLQIR-DDLTSEQRQDRANELME--EFHIEHLRDSLgQALSGGERRRVEIARA 151
Cdd:PRK10636 85 IDGDREYRQLEAQlhdanerndGHAIATIHGKlDAIDAWTIRSRAASLLHglGFSNEQLERPV-SDFSGGWRMRLNLAQA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
6MIT_B 152 LAANPKFILLDEPFAGVDPISVIDIKR----------IIEHLRD 185
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDLDAVIWLEKwlksyqgtliLISHDRD 207
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
19-198 |
4.22e-06 |
|
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: 46.17 E-value: 4.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNII---IDDEDISLLPLHARARRGIGYLPQEASIfrrlsv 95
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFEATRSRNRYSVAYAAQKPWL------ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 96 fdnLMAVLQIRDDLTSEQRQDRANELMEEFHIEHLRDSL-----------GQALSGGERRRVEIARALAANPKFILLDEP 164
Cdd:cd03290 91 ---LNATVEENITFGSPFNKQRYKAVTDACSLQPDIDLLpfgdqteigerGINLSGGQRQRICVARALYQNTNIVFLDDP 167
|
170 180 190
....*....|....*....|....*....|....*..
6MIT_B 165 FAGVDpISVID---IKRIIEHLRDSGLGVLITDHNVR 198
Cdd:cd03290 168 FSALD-IHLSDhlmQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-164 |
5.22e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 6 AKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIiiddedisllplHARARRGIGYLPQ 85
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI------------HCGTKLEVAYFDQ 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 86 -EASIFRRLSVFDNLmavlqirddltSEQRQdranELM---EEFHI-EHLRDSLG---------QALSGGERRRVEIARA 151
Cdd:PRK11147 390 hRAELDPEKTVMDNL-----------AEGKQ----EVMvngRPRHVlGYLQDFLFhpkramtpvKALSGGERNRLLLARL 454
|
170
....*....|...
6MIT_B 152 LAANPKFILLDEP 164
Cdd:PRK11147 455 FLKPSNLLILDEP 467
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
123-214 |
6.59e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.82 E-value: 6.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 123 EEFHIEHLRDSLGQ---ALSGGERR------RVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIEH-LRDSGL---G 189
Cdd:PRK01156 784 QDFNITVSRGGMVEgidSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYsLKDSSDipqV 863
|
90 100
....*....|....*....|....*
6MIT_B 190 VLITDHnvRETLAVCERAYIVSQGN 214
Cdd:PRK01156 864 IMISHH--RELLSVADVAYEVKKSS 886
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
134-224 |
9.01e-06 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 46.16 E-value: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 134 LGQ---ALSGGERRRVEIARAL---AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNvretLAVCERA 207
Cdd:TIGR00630 823 LGQpatTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHN----LDVIKTA 898
|
90 100
....*....|....*....|....*.
6MIT_B 208 -YIV--------SQGNLIAHGTPQQI 224
Cdd:TIGR00630 899 dYIIdlgpeggdGGGTVVASGTPEEV 924
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
19-74 |
3.95e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 43.65 E-value: 3.95e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 19 VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNiIIDDEDISLLPLHA 74
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK-VDRNGEVSVIAISA 94
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
138-229 |
4.30e-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: 4.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 138 LSGGERRRVEIARALAANPKFIL--LDEPFAGVDPisvIDIKRIIE---HLRDSGLGVLITDHNvRETLAVCEraYIVS- 211
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQ---RDNRRLINtlkRLRDLGNTLIVVEHD-EDTIRAAD--YVIDi 562
|
90 100
....*....|....*....|....*
6MIT_B 212 -------QGNLIAHGTPQQILEDDH 229
Cdd:TIGR00630 563 gpgagehGGEVVASGTPEEILANPD 587
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
215-238 |
5.11e-05 |
|
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: 39.16 E-value: 5.11e-05
10 20
....*....|....*....|....
6MIT_B 215 LIAHGTPQQILEDDHVKRVYLGED 238
Cdd:pfam12399 2 VIAEGTPAEVRADPRVIEAYLGEE 25
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
13-164 |
8.62e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 8.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 13 YKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGniiiddeDISL---LPLHARARRGIGYLPQEASI 89
Cdd:PRK10636 322 YGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-------EIGLakgIKLGYFAQHQLEFLRADESP 394
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
6MIT_B 90 FRRLSVFDNLMAVLQIRDDLTSEQRQ-DRANELMEEFhiehlrdslgqalSGGERRRVEIARALAANPKFILLDEP 164
Cdd:PRK10636 395 LQHLARLAPQELEQKLRDYLGGFGFQgDKVTEETRRF-------------SGGEKARLVLALIVWQRPNLLLLDEP 457
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
36-195 |
1.59e-04 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 41.44 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 36 GPNGAGKTTT----FYMVVGIVPRDAGNIIIDDEDIS------LLPLHARARRGIGYLpqeasIFRRLSVFDNLMAVlqi 105
Cdd:cd03240 29 GQNGAGKTTIiealKYALTGELPPNSKGGAHDPKLIRegevraQVKLAFENANGKKYT-----ITRSLAILENVIFC--- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 106 rddltseqRQDRANELMEEfHIEhlrdslgqALSGGERR------RVEIARALAANPKFILLDEPFAGVDP----ISVID 175
Cdd:cd03240 101 --------HQGESNWPLLD-MRG--------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEenieESLAE 163
|
170 180
....*....|....*....|
6MIT_B 176 IKRIIEHLRDSGLGVlITDH 195
Cdd:cd03240 164 IIEERKSQKNFQLIV-ITHD 182
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-62 |
6.28e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 40.64 E-value: 6.28e-04
10 20 30 40
....*....|....*....|....*....|....*....|..
6MIT_B 21 DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIII 62
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI 83
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-181 |
1.14e-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: 38.12 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 28 SGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgigylpqeasifrrlsvfdnlmavlqird 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLL------------------------------ 50
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
6MIT_B 108 dltseqrqdranelmeefhiEHLRDSLGQALSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIKRIIE 181
Cdd:smart00382 51 --------------------LIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
13-195 |
1.74e-03 |
|
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: 38.38 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 13 YKGRRVVEdVSLTVNSGEIVGLL-GPNGAGKTTTFymvvgivprdagniiiddEDISLLPLHARArrGIgYLPQEASifR 91
Cdd:cd03280 12 LQGEKVVP-LDIQLGENKRVLVItGPNAGGKTVTL------------------KTLGLLTLMAQS--GL-PIPAAEG--S 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 92 RLSVFDNLMAvlqirdDLTSEQrqdranelmeefhiehlrdSLGQALSGGERRRVEIARAL--AANPKFILLDEPFAGVD 169
Cdd:cd03280 68 SLPVFENIFA------DIGDEQ-------------------SIEQSLSTFSSHMKNIARILqhADPDSLVLLDELGSGTD 122
|
170 180
....*....|....*....|....*...
6MIT_B 170 PI--SVIDIKrIIEHLRDSGLGVLITDH 195
Cdd:cd03280 123 PVegAALAIA-ILEELLERGALVIATTH 149
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-228 |
4.13e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.27 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
6MIT_B 137 ALSGGERRRVEIARALAA---NPKFILLDEPFAGvdpISVIDIKRIIE---HLRDSGLGVLITDHNVrETLAVCEraYIV 210
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTG---LHTHDIKALIYvlqSLTHQGHTVVIIEHNM-HVVKVAD--YVL 882
|
90 100
....*....|....*....|....*.
6MIT_B 211 S--------QGNLIAHGTPQQILEDD 228
Cdd:PRK00635 883 ElgpeggnlGGYLLASCSPEELIHLH 908
|
|
| |
