|
Name |
Accession |
Description |
Interval |
E-value |
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
10-246 |
4.46e-177 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 486.07 E-value: 4.46e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGY 89
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:COG1137 83 LPQEASIFRKLTVEDNILAVLELRK-LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLGDDF 246
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGEDF 238
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
10-246 |
1.38e-152 |
|
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: 423.99 E-value: 1.38e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGY 89
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLGDDF 246
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQF 237
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
11-243 |
2.88e-144 |
|
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: 402.69 E-value: 2.88e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKDLnKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLS-KKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLG 243
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
10-246 |
9.44e-128 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 361.52 E-value: 9.44e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGY 89
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLGDDF 246
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDF 239
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
13-233 |
9.41e-71 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 216.47 E-value: 9.41e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDlaMHERARKGIGYLPQ 92
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR--DPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMAILETRkDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLY-GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 173 AGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:COG1131 160 SGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA 220
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
11-245 |
2.29e-68 |
|
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: 211.05 E-value: 2.29e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:COG0411 5 LEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIART 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMA---------ILETRKDLNKQQRQQRLN-----ELLSDFKINHIKDSLGMSVSGGERRRAEIA 156
Cdd:COG0411 85 FQNPRLFPELTVLENVLVaaharlgrgLLAALLRLPRARREEREAreraeELLERVGLADRADEPAGNLSYGQQRRLEIA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 157 RALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKD-RGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:COG0411 165 RALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADP 244
|
250
....*....|
gi 480205248 236 QVRKVYLGDD 245
Cdd:COG0411 245 RVIEAYLGEE 254
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
11-243 |
5.99e-68 |
|
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: 209.45 E-value: 5.99e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:COG0410 4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKDlnKQQRQQRLNELLSDF-KINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:COG0410 84 PEGRRIFPSLTVEENLLLGAYARRD--RAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLG 243
Cdd:COG0410 162 EPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
25-237 |
2.75e-66 |
|
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: 205.36 E-value: 2.75e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASIFRKLTIAE 104
Cdd:cd03219 15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRTFQIPRLFPELTVLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIM---------AILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGV 175
Cdd:cd03219 95 NVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 176 DPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQV 237
Cdd:cd03219 175 NPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
13-235 |
1.13e-63 |
|
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: 198.93 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmhERARKGIGYLPQ 92
Cdd:COG4555 4 VENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEP--REARRQIGVLPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMAILETRkDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:COG4555 82 ERGLYDRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 173 AGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:COG4555 161 NGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
11-234 |
1.21e-63 |
|
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: 198.04 E-value: 1.21e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKinHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRKARLERVYELFPRLK--ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
13-238 |
6.21e-60 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 189.03 E-value: 6.21e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA--RKGIGYL 90
Cdd:COG1127 8 VRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelRRRIGML 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:COG1127 88 FQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLYDE 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL--DNEQVR 238
Cdd:COG1127 168 PTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLasDDPWVR 238
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
13-222 |
2.60e-56 |
|
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily A; This family of ATP-binding proteins belongs to a multi-subunit transporter involved in drug resistance (BcrA and DrrA), nodulation, lipid transport, and lantibiotic immunity. In bacteria and archaea, these transporters usually include an ATP-binding protein and one or two integral membrane proteins. Eukaryotic systems of the ABCA subfamily display ABC domains that are quite similar to this family. The ATP-binding domain shows the highest similarity between all members of the ABC transporter family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213197 [Multi-domain] Cd Length: 173 Bit Score: 177.59 E-value: 2.60e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamHERARKGIGYLPQ 92
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKE--PEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMailetrkdlnkqqrqqrlnellsdfkinhikdslgmsVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:cd03230 81 EPSLYENLTVRENLK-------------------------------------LSGGMKQRLALAQALLHDPELLILDEPT 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 480205248 173 AGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSV 222
Cdd:cd03230 124 SGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
13-238 |
6.94e-56 |
|
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: 178.46 E-value: 6.94e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE--RARKGIGYL 90
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAElyRLRRRMGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:cd03261 83 FQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL--DNEQVR 238
Cdd:cd03261 163 PTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRasDDPLVR 233
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
11-231 |
1.72e-54 |
|
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: 174.62 E-value: 1.72e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRW--VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnlDLSDLAMHERARKGIG 88
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--GYSIRTDRKAARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAEN--IMAILetrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:cd03263 79 YCPQFDALFDELTVREHlrFYARL---KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTLKdRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
13-236 |
7.49e-54 |
|
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: 173.29 E-value: 7.49e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSK-RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYLP 91
Cdd:COG1122 3 LENLSFSYPGgTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGLVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 Q--EASIFRKlTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:COG1122 82 QnpDDQLFAP-TVEEDVAFGPENLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
11-241 |
3.83e-52 |
|
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: 169.45 E-value: 3.83e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYL 90
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMA---------ILETRKDlnkqqrQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAA 161
Cdd:COG1120 81 PQEPPAPFGLTVRELVALgryphlglfGRPSAED------REAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 162 DPKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKV 240
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEV 234
|
.
gi 480205248 241 Y 241
Cdd:COG1120 235 Y 235
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
10-245 |
4.98e-51 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 167.98 E-value: 4.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDlamheRARKGIGY 89
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-----EDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASIFRKLTIAENIMAiLETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVY-LARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLGDD 245
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNTLRLEAD 230
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
11-241 |
2.00e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 164.88 E-value: 2.00e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLsdlamhERARKGIGYL 90
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFR--KLTIAENIMAILETR----KDLNKQQRQqRLNELLSDFKINHIKD-SLGmSVSGGERRRAEIARALAADP 163
Cdd:COG1121 81 PQRAEVDWdfPITVRDVVLMGRYGRrglfRRPSRADRE-AVDEALERVGLEDLADrPIG-ELSGGQQQRVLLARALAQDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 164 KFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGsVIAEGTPQEILDNEQVRKVY 241
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAY 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
13-231 |
8.41e-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: 160.23 E-value: 8.41e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmhERARKGIGYLPQ 92
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENiMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:cd03265 81 DLSVDDELTGWEN-LYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 173 AGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
10-234 |
1.18e-48 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 163.39 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDL-SDLAMHERarkGIG 88
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRP-PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 169 DEPFAGVDpISVGdiKDI----IQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:COG1118 158 DEPFGALD-AKVR--KELrrwlRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
13-226 |
1.52e-47 |
|
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: 155.29 E-value: 1.52e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYLPQ 92
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 easifrkltiaenimailetrkdlnkqqrqqrlneLLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:cd03214 81 -----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 173 AGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03214 126 SHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
18-247 |
1.14e-46 |
|
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: 157.17 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 18 KNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmhERARKGIGYLPQEASIF 97
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREP--RKVRRSIGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 98 RKLTIAENIMAILETRkDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:TIGR01188 79 EDLTGRENLEMMGRLY-GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 178 ISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIldneqvrKVYLGDDFV 247
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL-------KRRLGKDTL 220
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
11-239 |
1.93e-46 |
|
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: 154.22 E-value: 1.93e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKDlNKQQRQQRLNEL---LSDFKinhikDSLGMSVSGGERRRAEIARALAADPKFML 167
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPR-RSRKIPDEIYELfpvLKEML-----GRRGGDLSGGQQQQLAIARALVTRPKLLL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEiLDNEQVRK 239
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEgGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDE-LDEDKVRR 226
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
11-226 |
6.32e-46 |
|
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: 152.43 E-value: 6.32e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErarkgIGYL 90
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNR-----IGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-236 |
8.43e-46 |
|
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: 159.68 E-value: 8.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRW-----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA-- 83
Cdd:COG1123 261 LEVRNLSKRYPVRGkggvrAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 84 RKGIGYLPQ--EASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKIN-HIKDSLGMSVSGGERRRAEIARALA 160
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 161 ADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQ 497
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
13-220 |
3.31e-45 |
|
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: 150.31 E-value: 3.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYL 90
Cdd:cd03225 2 LKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQ--EASIFrKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:cd03225 81 FQnpDDQFF-GPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEG 220
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
13-213 |
6.98e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 149.61 E-value: 6.98e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLsdlamhERARKGIGYLPQ 92
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------EKERKRIGYVPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRK--LTIAENIMAILETRKDLNKQQRQ---QRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFML 167
Cdd:cd03235 76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKadkAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEK 213
Cdd:cd03235 156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR 201
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
13-226 |
8.11e-45 |
|
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: 149.59 E-value: 8.11e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGYLPQ 92
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:cd03259 80 DYALFPHLTVAENIAFGLKLRG-VPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 173 AGVDPIS----VGDIKDIIqtlKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03259 159 SALDAKLreelREELKELQ---RELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
13-226 |
2.69e-44 |
|
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: 148.28 E-value: 2.69e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRW----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSdlamHE--RARKG 86
Cdd:cd03266 4 ADALTKRFRDVKktvqAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEpaEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASIFRKLTIAENImAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENL-EYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
11-234 |
3.20e-44 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 152.17 E-value: 3.20e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGYL 90
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NVGMV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:COG3842 83 FQDYALFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 171 PFAGVDP---ISV-GDIKDIiqtLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:COG3842 162 PLSALDAklrEEMrEELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-173 |
3.52e-43 |
|
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: 143.17 E-value: 3.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLaMHERARKGIGYLPQEASIFRKLTIAEN 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD-ERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 106 IMAILETrKDLNKQQRQQRLNELLSDFKINHIKDSL----GMSVSGGERRRAEIARALAADPKFMLLDEPFA 173
Cdd:pfam00005 80 LRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
13-220 |
4.75e-43 |
|
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: 143.87 E-value: 4.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDL-AMHERARKGIGYLP 91
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLeDELPPLRRRIGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEASIFRKLTIAENIMailetrkdlnkqqrqqrlnellsdfkinhikdslgMSVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:cd03229 83 QDFALFPHLTVLENIA-----------------------------------LGLSGGQQQRVALARALAMDPDVLLLDEP 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 480205248 172 FAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEG 220
Cdd:cd03229 128 TSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-241 |
6.84e-42 |
|
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: 149.92 E-value: 6.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 2 EQSVQQPQTLCIKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAm 79
Cdd:COG4987 325 PAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 80 HERARKGIGYLPQEASIFRKlTIAENI-MAiletRKDLNKQQRQQRLNEL-LSDFkINHIKDSL-------GMSVSGGER 150
Cdd:COG4987 404 EDDLRRRIAVVPQRPHLFDT-TLRENLrLA----RPDATDEELWAALERVgLGDW-LAALPDGLdtwlgegGRRLSGGER 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 151 RRAEIARALAADPKFMLLDEPFAGVDPISVGDI-KDIIQTLKDRGIgVLITdHNVREtLAICEKAYIVSEGSVIAEGTPQ 229
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGRTV-LLIT-HRLAG-LERMDRILVLEDGRIVEQGTHE 554
|
250
....*....|...
gi 480205248 230 EIL-DNEQVRKVY 241
Cdd:COG4987 555 ELLaQNGRYRQLY 567
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
13-244 |
8.36e-42 |
|
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: 142.48 E-value: 8.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGYLPQ 92
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMAILETRK---DLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:cd03296 82 HYALFRHMTVFDNVAFGLRVKPrseRPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVY--LGD 244
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYsfLGE 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
11-202 |
1.20e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 141.08 E-value: 1.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARkgIGYL 90
Cdd:COG4133 3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRkdlNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALY---GLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190
....*....|....*....|....*....|..
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
13-226 |
3.11e-41 |
|
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: 140.04 E-value: 3.11e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamhERARKGIGYLPQ 92
Cdd:cd03268 3 TNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKN---IEALRRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENiMAILETRKDLNKQQRQQRLNEL-LSDFKINHIKD-SLGMsvsggeRRRAEIARALAADPKFMLLDE 170
Cdd:cd03268 80 APGFYPNLTAREN-LRLLARLLGIRKKRIDEVLDVVgLKDSAKKKVKGfSLGM------KQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
11-225 |
2.66e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.45 E-value: 2.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRW----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLsdlamhERARKG 86
Cdd:COG1116 8 LELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPV------TGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:COG1116 82 RGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVL-ITdHNVRETLAICEKAYIVSE--GSVIAE 225
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLwQETGKTVLfVT-HDVDEAVFLADRVVVLSArpGRIVEE 222
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
13-234 |
2.76e-40 |
|
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: 138.97 E-value: 2.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY-SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMhERARKGIGYLP 91
Cdd:cd03295 3 FENVTKRYgGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDP-VELRRKIGYVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEASIFRKLTIAENImAILETRKDLNKQQRQQRLNELLS--DFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:cd03295 82 QQIGLFPHMTVEENI-ALVPKLLKWPKEKIRERADELLAlvGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKdRGIG---VLITdHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQ-QELGktiVFVT-HDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-233 |
2.83e-40 |
|
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: 138.78 E-value: 2.83e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRW----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIG 88
Cdd:COG1124 4 VRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR-VQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQ--EASIFRKLTIAEnimAILETRKDLNKQQRQQRLNELLSDFKIN-HIKDSLGMSVSGGERRRAEIARALAADPKF 165
Cdd:COG1124 83 MVFQdpYASLHPRHTVDR---ILAEPLRIHGLPDREERIAELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALILEPEL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 166 MLLDEPFAGVDPISVGDIKDIIQTLK-DRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:COG1124 160 LLLDEPTSALDVSVQAEILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
13-245 |
3.91e-40 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 140.33 E-value: 3.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARkgIGYLPQ 92
Cdd:PRK13537 10 FRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR--VGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMaILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:PRK13537 88 FDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 173 AGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNE---QVRKVYlGDD 245
Cdd:PRK13537 167 TGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcDVIEIY-GPD 241
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
12-220 |
4.22e-40 |
|
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: 135.45 E-value: 4.22e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 12 CIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERaRKGIGYLP 91
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QeasifrkltiaenimailetrkdlnkqqrqqrlnellsdfkinhikdslgmsVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 480205248 172 FAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEG 220
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
11-236 |
4.31e-40 |
|
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: 144.28 E-value: 4.31e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD---KGEIHLDNLDLSDLAMHERARK 85
Cdd:COG1123 5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 86 gIGYLPQEA-SIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPK 164
Cdd:COG1123 85 -IGMVFQDPmTQLNPVTVGDQIAEALENLG-LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
11-232 |
4.92e-40 |
|
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: 137.81 E-value: 4.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSdlamHE--RARKGIG 88
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLR----RAprAALARLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAENIM--AILEtrkDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:TIGR03864 78 VVFQQPTLDLDLSVRQNLRyhAALH---GLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVREtLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:TIGR03864 155 LLDEPTVGLDPASRAAITAHVRALaRDQGLSVLWATHLVDE-IEASDRLVVLHRGRVLADGAAAELR 220
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
13-205 |
1.53e-39 |
|
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: 136.08 E-value: 1.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYS----KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA---RK 85
Cdd:cd03255 3 LKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafrRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 86 GIGYLPQEASIFRKLTIAENIMAILETRKDLNKQQRqQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKF 165
Cdd:cd03255 83 HIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERR-ERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKI 161
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 480205248 166 MLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVR 205
Cdd:cd03255 162 ILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPE 202
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
11-226 |
3.05e-39 |
|
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: 135.01 E-value: 3.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGqIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnlDLSDLAMHERARKGIGYL 90
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRID--GQDVLKQPQKLRRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAE--NIMAILetrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:cd03264 78 PQEFGVYPNFTVREflDYIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTL-KDRgiGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELgEDR--IVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
26-245 |
4.06e-39 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 136.27 E-value: 4.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASIFRKLTIAEN 105
Cdd:PRK11300 21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRTFQHVRLFREMTVIEN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 106 ImailetrkdLNKQQRQQRLNELLSDFKI--------------NHIKDSLGM---------SVSGGERRRAEIARALAAD 162
Cdd:PRK11300 101 L---------LVAQHQQLKTGLFSGLLKTpafrraesealdraATWLERVGLlehanrqagNLAYGQQRRLEIARCMVTQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 163 PKFMLLDEPFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVY 241
Cdd:PRK11300 172 PEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNPDVIKAY 251
|
....
gi 480205248 242 LGDD 245
Cdd:PRK11300 252 LGEA 255
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
11-240 |
7.23e-39 |
|
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: 134.77 E-value: 7.23e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYsKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGYL 90
Cdd:cd03299 1 LKVENLSKDW-KEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRK-VDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKV 240
Cdd:cd03299 156 PFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
13-241 |
2.08e-38 |
|
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: 133.85 E-value: 2.08e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY-SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE--RARKGIGY 89
Cdd:cd03256 3 VENLSKTYpNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQIGM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASIFRKLTIAENI-------MAILETRKDLNKQQRQQRLNELLsdfkinhikDSLGMS---------VSGGERRRA 153
Cdd:cd03256 83 IFQQFNLIERLSVLENVlsgrlgrRSTWRSLFGLFPKEEKQRALAAL---------ERVGLLdkayqradqLSGGQQQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 154 EIARALAADPKFMLLDEPFAGVDPISVgdiKDIIQTLKD----RGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQ 229
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASS---RQVMDLLKRinreEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPA 230
|
250
....*....|..
gi 480205248 230 EiLDNEQVRKVY 241
Cdd:cd03256 231 E-LTDEVLDEIY 241
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
11-220 |
9.33e-38 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 131.09 E-value: 9.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYL 90
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPE-WRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKlTIAENIMAILETRkdlNKQQRQQRLNELLSDFKINHikDSLGMSV---SGGERRRAEIARALAADPKFML 167
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLR---ERKFDRERALELLERLGLPP--DILDKPVerlSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEG 220
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
11-243 |
1.14e-37 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 131.92 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENI-MAILETRKDlNKQQRQQRLNELLSDFKINHIKDSLGMSvsGGERRRAEIARALAADPKFMLLD 169
Cdd:PRK11614 86 PEGRRVFSRMTVEENLaMGGFFAERD-QFQERIKWVYELFPRLHERRIQRAGTMS--GGEQQMLAIGRALMSQPRLLLLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLG 243
Cdd:PRK11614 163 EPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
13-225 |
1.17e-37 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 131.32 E-value: 1.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY----SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA---RK 85
Cdd:COG1136 7 LRNLTKSYgtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELArlrRR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 86 GIGYLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKF 165
Cdd:COG1136 87 HIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRPKL 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 166 MLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNvRETLAICEKAYIVSEGSVIAE 225
Cdd:COG1136 166 ILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
11-220 |
2.32e-37 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 129.04 E-value: 2.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERaRKGIG 88
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESL-RKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFrKLTIAENIMailetrkdlnkqqrqqrlnellsdfkinhikdslgmsvSGGERRRAEIARALAADPKFMLL 168
Cdd:cd03228 80 YVPQDPFLF-SGTIRENIL--------------------------------------SGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTLKDRGIGVLITdHNVrETLAICEKAYIVSEG 220
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIA-HRL-STIRDADRIIVLDDG 170
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
13-236 |
2.38e-37 |
|
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: 130.78 E-value: 2.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRW----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHER--ARKG 86
Cdd:cd03258 4 LKNVSKVFGDTGgkvtALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkARRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:cd03258 84 IGMIFQHFNLLSSRTVFENVALPLEIAG-VPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:cd03258 163 LCDEATSALDPETTQSILALLRDInRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
13-225 |
4.02e-37 |
|
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: 129.90 E-value: 4.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRW----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSdlamheRARKGIG 88
Cdd:cd03293 3 VRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQG-VPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTL--KDRGIGVLITdHNVRETLAICEKAYIVSE--GSVIAE 225
Cdd:cd03293 156 DEPFSALDALTREQLQEELLDIwrETGKTVLLVT-HDIDEAVFLADRVVVLSArpGRIVAE 215
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
28-226 |
4.45e-37 |
|
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: 129.72 E-value: 4.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMqSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSD------LAMHERarkGIGYLPQEASIFRKLT 101
Cdd:cd03297 16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQR---KIGLVFQQYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENIMAILetrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:cd03297 92 VRENLAFGL---KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 480205248 182 DI-KDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03297 169 QLlPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-235 |
1.34e-36 |
|
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: 136.50 E-value: 1.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 21 SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERaRKGIGYLPQEASIFRKl 100
Cdd:COG2274 486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-RRQIGVVLQDVFLFSG- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIMAileTRKDLNKQQRQQRLNEL-LSDFkINHIKDSL-------GMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:COG2274 564 TIRENITL---GDPDATDEEIIEAARLAgLHDF-IEALPMGYdtvvgegGSNLSGGQRQRLAIARALLRNPRILILDEAT 639
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 173 AGVDPISVgdiKDIIQTLKD--RGIGVLITDHNvRETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:COG2274 640 SALDAETE---AIILENLRRllKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-244 |
1.47e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 131.88 E-value: 1.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 18 KNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLdnLDLSDLAMHERARKGIGYLPQEASIF 97
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITV--LGVPVPARARLARARIGVVPQFDNLD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 98 RKLTIAENIMaILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:PRK13536 127 LEFTVRENLL-VFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDP 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 178 ISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNE---QVRKVYLGD 244
Cdd:PRK13536 206 HARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHigcQVIEIYGGD 275
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
13-226 |
2.06e-36 |
|
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: 128.39 E-value: 2.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRW----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDL--AMHERARKG 86
Cdd:cd03257 4 VKNLSVSFPTGGgsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLsrRLRKIRRKE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEA--SIFRKLTIAENIMAILETRKDLNKQQRQQRLnELLSDFKINHIKDSLGM---SVSGGERRRAEIARALAA 161
Cdd:cd03257 84 IQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEA-VLLLLVGVGLPEEVLNRyphELSGGQRQRVAIARALAL 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 162 DPKFMLLDEPFAGVDPISVGDIKDIIQTLKD-RGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03257 163 NPKLLIADEPTSALDVSVQAQILDLLKKLQEeLGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
11-245 |
2.73e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.64 E-value: 2.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNY-SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE--RARKGI 87
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 88 GYLPQEASIFRKLTIAENIMA-------ILET-RKDLNKQQRQQRLnELLsdfkinhikDSLGMS---------VSGGER 150
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLAgrlgrtsTWRSlLGLFPPEDRERAL-EAL---------ERVGLAdkayqradqLSGGQQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 151 RRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQ 229
Cdd:COG3638 153 QRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPA 232
|
250
....*....|....*.
gi 480205248 230 EiLDNEQVRKVYLGDD 245
Cdd:COG3638 233 E-LTDAVLREIYGGEA 247
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
4-235 |
5.15e-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: 133.73 E-value: 5.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 4 SVQQPQTLCIKHLAKNY-SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHER 82
Cdd:COG4988 330 PAAGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 83 aRKGIGYLPQEASIFrKLTIAENI-MAiletRKDLNKQQRQQRLNEL-LSDFkINHIKDSL-------GMSVSGGERRRA 153
Cdd:COG4988 410 -RRQIAWVPQNPYLF-AGTIRENLrLG----RPDASDEELEAALEAAgLDEF-VAALPDGLdtplgegGRGLSGGQAQRL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 154 EIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITdHNVrETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:COG4988 483 ALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRL-ALLAQADRILVLDDGRIVEQGTHEELLA 560
|
..
gi 480205248 234 NE 235
Cdd:COG4988 561 KN 562
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
13-236 |
1.50e-35 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 126.26 E-value: 1.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMH-ERARKGIGYLP 91
Cdd:COG1126 4 IENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDiNKLRRKVGMVF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:COG1126 84 QQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 172 FAGVDPISVGDIKDIIQTLKDRGIGVLITDHNV---REtlaICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:COG1126 164 TSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMgfaRE---VADRVVFMDGGRIVEEGPPEEFFENPQ 228
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
13-231 |
1.91e-35 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 129.05 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSdlAMHERARKgIGYLPQ 92
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVS--RLHARDRK-VGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENI---MAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:PRK10851 82 HYALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKD--RGIGVLITdHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEelKFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
23-238 |
2.86e-35 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 126.42 E-value: 2.86e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE--RARKGIGYLPQEASIFRKL 100
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRlyTVRKRMSMLFQSGALFTDM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISV 180
Cdd:PRK11831 100 NVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITM 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 181 GDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVR 238
Cdd:PRK11831 180 GVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-243 |
2.99e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 126.00 E-value: 2.99e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASIFRKLTIAEN 105
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRKFQKPTVFEELTVFEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 106 IMAILETRKD--------LNKQQRqQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:COG4674 106 LELALKGDRGvfaslfarLTAEER-DRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTD 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 178 ISVGDIKDIIQTL-KDRgiGVLITDHN---VREtlaICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLG 243
Cdd:COG4674 185 AETERTAELLKSLaGKH--SVVVVEHDmefVRQ---IARKVTVLHQGSVLAEGSLDEVQADPRVIEVYLG 249
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
30-243 |
5.56e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 124.87 E-value: 5.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 30 SFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGYLPQEASIFRKLTIAENIMAI 109
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 110 LETRKDLNKQQRQQrLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQT 189
Cdd:COG3840 96 LRPGLKLTAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 190 L-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILD---NEQVRKvYLG 243
Cdd:COG3840 175 LcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDgepPPALAA-YLG 231
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
28-232 |
6.29e-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: 127.92 E-value: 6.29e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSD------LAMHERArkgIGYLPQEASIFRKLT 101
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRR---IGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENImaiLETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:TIGR02142 92 VRGNL---RYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 480205248 182 DIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:TIGR02142 169 EILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
13-203 |
1.15e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.62 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSK-RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA--RKGIGY 89
Cdd:COG2884 4 FENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylRRRIGV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:COG2884 84 VFQDFRLLPDRTVYENVALPLRVTG-KSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLAD 162
|
170 180 190
....*....|....*....|....*....|....
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHN 203
Cdd:COG2884 163 EPTGNLDPETSWEIMELLEEINRRGTTVLIATHD 196
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
13-202 |
1.51e-34 |
|
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: 123.02 E-value: 1.51e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA-RKGIGYLP 91
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGMVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:cd03262 83 QQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEP 162
|
170 180 190
....*....|....*....|....*....|.
gi 480205248 172 FAGVDPISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:cd03262 163 TSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
25-226 |
4.44e-34 |
|
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: 122.44 E-value: 4.44e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIgYLPQEASIFRKLTIAE 104
Cdd:cd03267 36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWWDLPVID 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NiMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIK 184
Cdd:cd03267 115 S-FYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 480205248 185 DIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03267 194 NFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
11-233 |
5.00e-34 |
|
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: 121.48 E-value: 5.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL--VRMDKGEIHLDNLDLSDLAMHERARKGIG 88
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAenimailetrkdlnkqqrqqrlnELLSDfkinhikdsLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:cd03217 81 LAFQYPPEIPGVKNA-----------------------DFLRY---------VNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAI-CEKAYIVSEGSVIAEGtPQEILD 233
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELAL 193
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
12-226 |
6.83e-34 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 121.61 E-value: 6.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 12 CIKHLAKNySKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDK---GEIHLDNLDLSDLAMheraRKGIG 88
Cdd:cd03234 10 GLKAKNWN-KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsGQILFNGQPRKPDQF----QKCVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAENI--MAILETRKDLNKQQRQQRL-NELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKF 165
Cdd:cd03234 85 YVRQDDILLPGLTVRETLtyTAILRLPRKSSDAIRKKRVeDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 166 MLLDEPFAGVDPISVgdiKDIIQTLKD---RGIGVLITDHNVR-ETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03234 165 LILDEPTSGLDSFTA---LNLVSTLSQlarRNRIVILTIHQPRsDLFRLFDRILLLSSGEIVYSG 226
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
10-234 |
7.72e-34 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.80 E-value: 7.72e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGY 89
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:COG3839 80 VFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 170 EPFAGVDPIS----VGDIKDIIQTLkdrGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:COG3839 159 EPLSNLDAKLrvemRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDR 224
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
28-232 |
2.18e-33 |
|
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: 123.67 E-value: 2.18e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSD------LAMHERArkgIGYLPQEASIFRKLT 101
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDsargifLPPHRRR---IGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENIMAileTRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:COG4148 94 VRGNLLY---GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 480205248 182 DIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:COG4148 171 EILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVL 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
13-240 |
3.51e-33 |
|
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: 120.03 E-value: 3.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGYLPQ 92
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 173 AGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKV 240
Cdd:cd03300 159 GALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFV 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
11-241 |
3.55e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 120.61 E-value: 3.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYL 90
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR-RAVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASI---FRkltiAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALA------- 160
Cdd:COG4559 81 PQHSSLafpFT----VEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 161 ADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKV 240
Cdd:COG4559 157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERV 236
|
.
gi 480205248 241 Y 241
Cdd:COG4559 237 Y 237
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
10-202 |
4.20e-33 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 119.12 E-value: 4.20e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD---KGEIHLDNLDLSDLAMHERarkG 86
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASIFRKLTIAENIMaiLETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLA--FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170 180 190
....*....|....*....|....*....|....*..
gi 480205248 167 LLDEPFAGVDPISVGDIKD-IIQTLKDRGIGVLITDH 202
Cdd:COG4136 156 LLDEPFSKLDAALRAQFREfVFEQIRQRGIPALLVTH 192
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
13-231 |
4.77e-33 |
|
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: 119.59 E-value: 4.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRM-----DKGEIHLDNLDLSDLAMH-ERARKG 86
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDvLELRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASIFRKlTIAENIMAILETRKDLNKQQRQQRLNELLSDFKI-NHIKDSL-GMSVSGGERRRAEIARALAADPK 164
Cdd:cd03260 83 VGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRKAALwDEVKDRLhALGLSGGQQQRLCLARALANEPE 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRgIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:cd03260 162 VLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
10-241 |
1.69e-32 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 119.11 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGY 89
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASI---FRkltiAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALA------ 160
Cdd:PRK13548 81 LPQHSSLsfpFT----VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 161 ADPKFMLLDEpfagvdPISVGDIKDIIQTL-------KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:PRK13548 157 GPPRWLLLDE------PTSALDLAHQHHVLrlarqlaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230
|
....*...
gi 480205248 234 NEQVRKVY 241
Cdd:PRK13548 231 PETLRRVY 238
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
13-232 |
1.69e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 118.26 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRW----VVKDVSFTMQSGQIVGLLGPNGAGKTTsfymvvgLVRM-------DKGEIHLDNLDLSDLAMHE 81
Cdd:COG1135 4 LENLSKTFPTKGgpvtALDDVSLTIEKGEIFGIIGYSGAGKST-------LIRCinllerpTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 82 --RARKGIGYLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNEL-----LSDfKINHIKDSLgmsvSGGERRRAE 154
Cdd:COG1135 77 lrAARRKIGMIFQHFNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELlelvgLSD-KADAYPSQL----SGGQKQRVG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 155 IARALAADPKFMLLDEPFAGVDPISVGDI----KDIIQTLkdrGIG-VLITD--HNVREtlaICEKAYIVSEGSVIAEGT 227
Cdd:COG1135 151 IARALANNPKVLLCDEATSALDPETTRSIldllKDINREL---GLTiVLITHemDVVRR---ICDRVAVLENGRIVEQGP 224
|
....*
gi 480205248 228 PQEIL 232
Cdd:COG1135 225 VLDVF 229
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
13-241 |
1.97e-31 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 115.95 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYLPQ 92
Cdd:COG4604 4 IKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKR-LAILRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAEnimaiL-------ETRKDLNKQQRQ------QRLNelLSDFKINHIkDSLgmsvSGGERRRAEIARAL 159
Cdd:COG4604 83 ENHINSRLTVRE-----LvafgrfpYSKGRLTAEDREiideaiAYLD--LEDLADRYL-DEL----SGGQRQRAFIAMVL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 160 AADPKFMLLDEPFAGVDPI-SVgdikDIIQTLK----DRGIGVLITDHNVreTLAICEKAYIVS--EGSVIAEGTPQEIL 232
Cdd:COG4604 151 AQDTDYVLLDEPLNNLDMKhSV----QMMKLLRrladELGKTVVIVLHDI--NFASCYADHIVAmkDGRVVAQGTPEEII 224
|
....*....
gi 480205248 233 DNEQVRKVY 241
Cdd:COG4604 225 TPEVLSDIY 233
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
25-233 |
5.55e-31 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 114.78 E-value: 5.55e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL--VRMDKGEIHLDNLDLSDLAMHERARKGIGYL---PQEasiFRK 99
Cdd:COG0396 15 ILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAfqyPVE---IPG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 100 LTIAENIMAILETR--KDLNKQQRQQRLNELLSDFKIN--HIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGV 175
Cdd:COG0396 92 VSVSNFLRTALNARrgEELSAREFLKLLKEKMKELGLDedFLDRYVNEGFSGGEKKRNEILQMLLLEPKLAILDETDSGL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 176 DPISVGDIKDIIQTLKDRGIGVLITDHNVRetlaICE-----KAYIVSEGSVIAEGTPqEILD 233
Cdd:COG0396 172 DIDALRIVAEGVNKLRSPDRGILIITHYQR----ILDyikpdFVHVLVDGRIVKSGGK-ELAL 229
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
25-242 |
1.78e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 114.02 E-value: 1.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLS-DLAMHERARKGIGYLPQ--EASIFRKlT 101
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKyDKKSLLEVRKTVGIVFQnpDDQLFAP-T 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENImAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:PRK13639 96 VEEDV-AFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 182 DIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL-DNEQVRKVYL 242
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFsDIETIRKANL 236
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-222 |
1.89e-30 |
|
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: 111.15 E-value: 1.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 22 KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERaRKGIGYLPQEASIFrKLT 101
Cdd:cd03246 14 EPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL-GDHVGYLPQDDELF-SGS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENIMailetrkdlnkqqrqqrlnellsdfkinhikdslgmsvSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:cd03246 92 IAENIL--------------------------------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGER 133
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 480205248 182 DIKDIIQTLKDRGIGVLITDHNvRETLAICEKAYIVSEGSV 222
Cdd:cd03246 134 ALNQAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
11-238 |
4.33e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 115.32 E-value: 4.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERArkgIGYL 90
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP---INMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 171 PFAGVDPisvgDIKDIIQ-----TLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVR 238
Cdd:PRK11607 176 PMGALDK----KLRDRMQlevvdILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTR 244
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
11-231 |
1.12e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.50 E-value: 1.12e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKD--LNKQQRQQRLNELLSDFKInHIK-DSLGMSVSGGERRRAEIARALAADPKFML 167
Cdd:COG1129 85 HQELNLVPNLSVAENIFLGREPRRGglIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 168 LDEPFAgvdPISVGDIK---DIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:COG1129 164 LDEPTA---SLTEREVErlfRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
28-226 |
1.23e-29 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 110.28 E-value: 1.23e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamhERARKGIGYLPQEASIFRKLTIAENIM 107
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAA---PPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 108 AILETRKDLNKQQRQqRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDII 187
Cdd:cd03298 93 LGLSPGLKLTAEDRQ-AIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 480205248 188 QTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03298 172 LDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
10-241 |
1.53e-29 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 111.26 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGY 89
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQ-----EASIFRKLtIAENIMAILETRKDLNkQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPK 164
Cdd:PRK11231 81 LPQhhltpEGITVREL-VAYGRSPWLSLWGRLS-AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVY 241
Cdd:PRK11231 159 VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
11-242 |
1.87e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 111.86 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSK-RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDN--LDLSDLAMHErARKGI 87
Cdd:PRK13636 6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLMK-LRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 88 GYLPQE-------ASIFRKLTIAENIMAiletrkdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALA 160
Cdd:PRK13636 85 GMVFQDpdnqlfsASVYQDVSFGAVNLK-------LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 161 ADPKFMLLDEPFAGVDPISVGDI-KDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL-DNEQVR 238
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFaEKEMLR 237
|
....
gi 480205248 239 KVYL 242
Cdd:PRK13636 238 KVNL 241
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
21-232 |
2.13e-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: 115.23 E-value: 2.13e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 21 SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamhERARKG--IGYLPQEASIFR 98
Cdd:COG4618 343 SKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQW---DREELGrhIGYLPQDVELFD 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 99 KlTIAENI----------------MA-----IL------ETRkdlnkqqrqqrlnellsdfkinhIKDSlGMSVSGGERR 151
Cdd:COG4618 420 G-TIAENIarfgdadpekvvaaakLAgvhemILrlpdgyDTR-----------------------IGEG-GARLSGGQRQ 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 152 RAEIARALAADPKFMLLDEPFAGVDpiSVGD--IKDIIQTLKDRGIGVLITDHNVReTLAICEKAYIVSEGSVIAEGTPQ 229
Cdd:COG4618 475 RIGLARALYGDPRLVVLDEPNSNLD--DEGEaaLAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRD 551
|
...
gi 480205248 230 EIL 232
Cdd:COG4618 552 EVL 554
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
21-233 |
2.59e-29 |
|
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: 110.01 E-value: 2.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 21 SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmHERARKGIGYLPQEASIFRKl 100
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENI-MAILE-TRKDLNKQQRQQRLNELlsdfkINHIKDSL-------GMSVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:cd03254 92 TIMENIrLGRPNaTDEEVIEAAKEAGAHDF-----IMKLPNGYdtvlgenGGNLSQGERQLLAIARAMLRDPKILILDEA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 172 FAGVDPISVGDIKDIIQTLKDrGIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:cd03254 167 TSNIDTETEKLIQEALEKLMK-GRTSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDELLA 226
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
13-229 |
2.60e-29 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 110.10 E-value: 2.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTtSFYMVVGLVRM-DKGEIHLDN--LDLSDLAMHERA---RKG 86
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKS-SLLRVLNLLETpDSGQLNIAGhqFDFSQKPSEKAIrllRQK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:COG4161 84 VGMVFQQYNLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNV---RET---LAICEKAYIVSEGSVIAEGTPQ 229
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVefaRKVasqVVYMEKGRIIEQGDASHFTQPQ 232
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
17-222 |
4.61e-29 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 107.90 E-value: 4.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 17 AKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLP---QE 93
Cdd:cd03215 7 VRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPedrKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 94 ASIFRKLTIAENIMailetrkdlnkqqrqqrLNELLsdfkinhikdslgmsvSGGERRRAEIARALAADPKFMLLDEPFA 173
Cdd:cd03215 87 EGLVLDLSVAENIA-----------------LSSLL----------------SGGNQQKVVLARWLARDPRVLILDEPTR 133
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 480205248 174 GVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSV 222
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
20-241 |
5.21e-29 |
|
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: 109.79 E-value: 5.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 20 YSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTsfymvvgLVRMDKGEIH-------------LDNLDLSDLamheraRKG 86
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKST-------LLSLITGDLPptygndvrlfgerRGGEDVWEL------RKR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYL-PQEASIFRKLTIAENIM-----AILETRKDLNKQQRQqRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALA 160
Cdd:COG1119 80 IGLVsPALQLRFPRDETVLDVVlsgffDSIGLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 161 ADPKFMLLDEPFAGVDPISVGDIKDIIQTL---KDRGIgVLITdHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQV 237
Cdd:COG1119 159 KDPELLILDEPTAGLDLGARELLLALLDKLaaeGAPTL-VLVT-HHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENL 236
|
....
gi 480205248 238 RKVY 241
Cdd:COG1119 237 SEAF 240
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
13-223 |
7.57e-29 |
|
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: 108.11 E-value: 7.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSK-RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNldlSDLAMHERaRKGIGYLP 91
Cdd:cd03226 2 IENISFSYKKgTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNG---KPIKAKER-RKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QE-------ASIFRKLTIaenimaileTRKDLNKqqRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPK 164
Cdd:cd03226 78 QDvdyqlftDSVREELLL---------GLKELDA--GNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVI 223
Cdd:cd03226 147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
17-231 |
7.79e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.19 E-value: 7.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 17 AKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLP---QE 93
Cdd:COG1129 259 VEGLSVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYVPedrKG 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 94 ASIFRKLTIAENI-MAILETRKD---LNKQQRQQRLNELLSDFKI--NHIKDSLGmSVSGGERRRAEIARALAADPKFML 167
Cdd:COG1129 339 EGLVLDLSIRENItLASLDRLSRgglLDRRRERALAEEYIKRLRIktPSPEQPVG-NLSGGNQQKVVLAKWLATDPKVLI 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 168 LDEPFAGVDpisVG---DIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:COG1129 418 LDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
13-176 |
9.03e-29 |
|
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: 108.11 E-value: 9.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGYLPQ 92
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRK-VPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPL 158
|
....
gi 480205248 173 AGVD 176
Cdd:cd03301 159 SNLD 162
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
29-241 |
9.55e-29 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 108.77 E-value: 9.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 29 VSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRmDKGEIHLDNLDLSDLAMHERARKGiGYLPQEAS------IFRKLTi 102
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDWSAAELARHR-AYLSQQQSppfampVFQYLA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 aenimaiLETRKDLNKQQRQQRLNELLSDFKINhikDSLGMSV---SGGERRRAEIARAL-----AADP--KFMLLDEPF 172
Cdd:COG4138 92 -------LHQPAGASSEAVEQLLAQLAEALGLE---DKLSRPLtqlSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 173 AGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVY 241
Cdd:COG4138 162 NSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF 230
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
27-230 |
2.31e-28 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 112.04 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 27 KDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDN--LDLSDLAMherARK-GIGYLPQEASIFRKLTIA 103
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRD---AIAlGIGMVHQHFMLVPNLTVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 104 ENIMAILETRKD--LNKQQRQQRLNELLSD--FKIN---HIKDslgMSVsgGERRRAEIARALAADPKFMLLDEPFAGVD 176
Cdd:COG3845 99 ENIVLGLEPTKGgrLDRKAARARIRELSERygLDVDpdaKVED---LSV--GEQQRVEILKALYRGARILILDEPTAVLT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 480205248 177 PISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQE 230
Cdd:COG3845 174 PQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAE 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
10-247 |
2.34e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 111.09 E-value: 2.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGY 89
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASI---FRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:PRK09536 82 VPQDTSLsfeFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVYLGDDF 246
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTA 241
|
.
gi 480205248 247 V 247
Cdd:PRK09536 242 V 242
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
23-234 |
2.75e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.18 E-value: 2.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERaRKGIGYLPQEASIFrKLTI 102
Cdd:COG1132 353 RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL-RRQIGVVPQDTFLF-SGTI 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENI-MAILE-TRKDLNKQQRQQRLNELLSDF--KINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPI 178
Cdd:COG1132 431 RENIrYGRPDaTDEEVEEAAKAAQAHEFIEALpdGYDTVVGERGVNLSGGQRQRIAIARALLKDPPILILDEATSALDTE 510
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 179 SVGDIKDIIQTL-KDRgIGVLITdHNVReTLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:COG1132 511 TEALIQEALERLmKGR-TTIVIA-HRLS-TIRNADRILVLDDGRIVEQGTHEELLAR 564
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
13-237 |
3.59e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 108.15 E-value: 3.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYL 90
Cdd:PRK13632 10 VENVSFSYpnSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-IRKKIGII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEA-SIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:PRK13632 89 FQNPdNQFIGATVEDDIAFGLENKK-VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFD 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLIT-DHNVRETLaICEKAYIVSEGSVIAEGTPQEILDNEQV 237
Cdd:PRK13632 168 ESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEI 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
14-234 |
3.90e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.10 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 14 KHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA-RKGIGYLPQ 92
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIM-AILETRKdLNKQQRQQRLNELLSDF----KINHIKDSLgmsvSGGERRRAEIARALAADPKFML 167
Cdd:PRK09493 85 QFYLFPHLTALENVMfGPLRVRG-ASKEEAEKQARELLAKVglaeRAHHYPSEL----SGGQQQRVAIARALAVKPKLML 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:PRK09493 160 FDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
22-213 |
6.42e-28 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 111.22 E-value: 6.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 22 KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERaRKGIGYLPQEASIFRKlT 101
Cdd:TIGR02857 334 RRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAWVPQHPFLFAG-T 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENI-MAILE-TRKDLNKQQRQQRLNELLSDFK--INHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:TIGR02857 412 IAENIrLARPDaSDAEIREALERAGLDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491
|
170 180 190
....*....|....*....|....*....|....*.
gi 480205248 178 ISVGDIKDIIQTLKDRGIGVLITdHNvRETLAICEK 213
Cdd:TIGR02857 492 ETEAEVLEALRALAQGRTVLLVT-HR-LALAALADR 525
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-234 |
6.58e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 108.22 E-value: 6.58e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY--SKRWV--VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVR---MDKGEIHLDNLDLSDLAMHERAR- 84
Cdd:COG0444 4 VRNLKVYFptRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPppgITSGEILFDGEDLLKLSEKELRKi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 85 --KGIGYLPQE--ASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGM---SVSGGERRRAEIAR 157
Cdd:COG0444 84 rgREIQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRVMIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 158 ALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKD-RGIGVL-ITdHN---VREtlaICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:COG0444 164 ALALEPKLLIADEPTTALDVTIQAQILNLLKDLQReLGLAILfIT-HDlgvVAE---IADRVAVMYAGRIVEEGPVEELF 239
|
..
gi 480205248 233 DN 234
Cdd:COG0444 240 EN 241
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-226 |
9.67e-28 |
|
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: 104.94 E-value: 9.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 21 SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRM--DKGEIHLDNLDLSDlamhERARKGIGYLPQEASIFR 98
Cdd:cd03213 20 SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDK----RSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 99 KLTIAENIMAILETRkdlnkqqrqqrlnellsdfkinhikdslgmSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPI 178
Cdd:cd03213 96 TLTVRETLMFAAKLR------------------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSS 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 480205248 179 SVGDIKDIIQTLKDRGIGVLITDHNVR-ETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03213 146 SALQVMSLLRRLADTGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-247 |
1.11e-27 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 106.57 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLD---LSDLAMHERARKGIGYLPQEASIFRKLTI 102
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDiaaMSRKELRELRRKKISMVFQSFALLPHRTV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENIMAILETRkDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGD 182
Cdd:cd03294 120 LENVAFGLEVQ-GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRRE 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 183 IKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQvrkvylgDDFV 247
Cdd:cd03294 199 MQDELLRLqAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPA-------NDYV 257
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-228 |
1.24e-27 |
|
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: 111.26 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSdlAMHERARKGIG 88
Cdd:TIGR01257 929 VCVKNLVKIFepSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLG 1006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAENIMAILETrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:TIGR01257 1007 MCPQHNILFHHLTVAEHILFYAQL-KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVL 1085
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 169 DEPFAGVDPISVGDIKDIIqtLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTP 228
Cdd:TIGR01257 1086 DEPTSGVDPYSRRSIWDLL--LKYRsGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
13-241 |
1.39e-27 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 106.25 E-value: 1.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKG-EIHLDNLDLS-----DLAMHER-ARK 85
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSaGSHIELLGRTvqregRLARDIRkSRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 86 GIGYLPQEASIFRKLTIAENIM--AILET---RKDLN--KQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARA 158
Cdd:PRK09984 87 NTGYIFQQFNLVNRLSVLENVLigALGSTpfwRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 159 LAADPKFMLLDEPFAGVDPISVgdiKDIIQTLKD----RGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEiLDN 234
Cdd:PRK09984 167 LMQQAKVILADEPIASLDPESA---RIVMDTLRDinqnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQ-FDN 242
|
....*..
gi 480205248 235 EQVRKVY 241
Cdd:PRK09984 243 ERFDHLY 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
11-235 |
2.30e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 109.37 E-value: 2.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILeTRKDLNKQQRQQRLNELLSDFKInhikDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK15439 92 PQEPLLFPNLSVKENILFGL-PKRQASMQKMKQLLAALGCQLDL----DSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
11-225 |
3.63e-27 |
|
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: 102.51 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYL 90
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQeasifrkltiaenimailetrkdlnkqqrqqrlnellsdfkinhikdslgmsVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:cd03216 81 YQ----------------------------------------------------LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAE 225
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
28-203 |
7.47e-27 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 103.26 E-value: 7.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamHERA----RKGIGYLPQEASIFRKLTIA 103
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDL--RGRAipylRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 104 ENIMAILETrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDI 183
Cdd:cd03292 97 ENVAFALEV-TGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180
....*....|....*....|
gi 480205248 184 KDIIQTLKDRGIGVLITDHN 203
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHA 195
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
11-231 |
9.55e-27 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 105.96 E-value: 9.55e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERarkGIGYL 90
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGLKMLG-VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
21-232 |
1.34e-26 |
|
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: 107.43 E-value: 1.34e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 21 SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmHERARKGIGYLPQEASIFrKL 100
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWD-RETFGKHIGYLPQDVELF-PG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENImaileTRKDLNKQQRQ----QRL---NELLSDFKINHikDSL----GMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:TIGR01842 407 TVAENI-----ARFGENADPEKiieaAKLagvHELILRLPDGY--DTVigpgGATLSGGQRQRIALARALYGDPKLVVLD 479
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 170 EPFAGVDpiSVGDI--KDIIQTLKDRGIGVLITDHNVReTLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:TIGR01842 480 EPNSNLD--EEGEQalANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVL 541
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
13-229 |
4.79e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 101.63 E-value: 4.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTsFYMVVGLVRM-DKGEIHLDN--LDLSDlAMHERA----RK 85
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSS-LLRVLNLLEMpRSGTLNIAGnhFDFSK-TPSDKAirelRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 86 GIGYLPQEASIFRKLTIAENI----MAILEtrkdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAA 161
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNLieapCRVLG----LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 162 DPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNV---RET---LAICEKAYIVSEGSVIAEGTPQ 229
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVevaRKTasrVVYMENGHIVEQGDASCFTQPQ 232
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
21-242 |
7.81e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 101.80 E-value: 7.81e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 21 SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYLPQ--EASIFR 98
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIRE-VRKFVGLVFQnpDDQIFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 99 klTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPI 178
Cdd:PRK13652 94 --PTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 179 SVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI-LDNEQVRKVYL 242
Cdd:PRK13652 172 GVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARVHL 237
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-235 |
9.23e-26 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 100.81 E-value: 9.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 30 SFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDlsdlamHER---ARKGIGYLPQEASIFRKLTIAENI 106
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD------HTTtppSRRPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 107 MAILETRKDLNKQQRQQrLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDI 186
Cdd:PRK10771 93 GLGLNPGLKLNAAQREK-LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 480205248 187 IQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGK 221
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
10-208 |
1.64e-25 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 100.71 E-value: 1.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYSKRW----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNldlsdlamheRARK 85
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDG----------VPVT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 86 GIGylPQEASIFRK------LTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARAL 159
Cdd:COG4525 73 GPG--ADRGVVFQKdallpwLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARAL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 480205248 160 AADPKFMLLDEPFAGVDPISvgdiKDIIQTL-----KDRGIGVLITDHNVRETL 208
Cdd:COG4525 150 AADPRFLLMDEPFGALDALT----REQMQELlldvwQRTGKGVFLITHSVEEAL 199
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-171 |
3.21e-25 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 103.22 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNldlsdlamheRARkgIGYLPQ 92
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMAILETRKDLNKQQRQ------------QRLNELLSDF----------KINHIKDSLGM------- 143
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlERLAELQEEFealggweaeaRAEEILSGLGFpeedldr 148
|
170 180 190
....*....|....*....|....*....|.
gi 480205248 144 ---SVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:COG0488 149 pvsELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-226 |
3.99e-25 |
|
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: 98.82 E-value: 3.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 21 SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERaRKGIGYLPQEASIFrKL 100
Cdd:cd03245 15 QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLF-YG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIMAILETRKDlnkqQRQQRLNEL--LSDFKINHiKDSL-------GMSVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:cd03245 93 TLRDNITLGAPLADD----ERILRAAELagVTDFVNKH-PNGLdlqigerGRGLSGGQRQAVALARALLNDPPILLLDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 172 FAGVDPISVGDIKDIIQTLKdRGIGVLITDHNVReTLAICEKAYIVSEGSVIAEG 226
Cdd:cd03245 168 TSAMDMNSEERLKERLRQLL-GDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
10-202 |
6.56e-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: 102.44 E-value: 6.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLaknySKRW-----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERAR 84
Cdd:TIGR02868 334 TLELRDL----SAGYpgappVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 85 KgIGYLPQEASIFRKlTIAENIMAILE--TRKDLNKQQRQQRLNELLSDFK--INHIKDSLGMSVSGGERRRAEIARALA 160
Cdd:TIGR02868 410 R-VSVCAQDAHLFDT-TVRENLRLARPdaTDEELWAALERVGLADWLRALPdgLDTVLGEGGARLSGGERQRLALARALL 487
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 480205248 161 ADPKFMLLDEPFAGVDPisvGDIKDIIQTLKDRGIG---VLITDH 202
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDA---ETADELLEDLLAALSGrtvVLITHH 529
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-232 |
1.12e-24 |
|
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: 101.80 E-value: 1.12e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYS--KRWVVK---DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHL----DNLDLSDLAMHERA 83
Cdd:TIGR03269 282 VRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGRG 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 84 R--KGIGYLPQEASIFRKLTIAENIM-AI-LETRKDLNKQQRQQRLNEL-LSDFKINHIKDSLGMSVSGGERRRAEIARA 158
Cdd:TIGR03269 362 RakRYIGILHQEYDLYPHRTVLDNLTeAIgLELPDELARMKAVITLKMVgFDEEKAEEILDKYPDELSEGERHRVALAQV 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 159 LAADPKFMLLDEPFAGVDPISVGDIKD-IIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:TIGR03269 442 LIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
25-225 |
1.53e-24 |
|
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: 98.34 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDL--AMHERARKGIGYLPQEA--SIFRKL 100
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrKQRRAFRRDVQLVFQDSpsAVNPRM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIMAILETRKDLNKQQRQQRLNELLSDFKI-NHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPIS 179
Cdd:TIGR02769 106 TVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 480205248 180 VGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAE 225
Cdd:TIGR02769 186 QAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEE 232
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
26-234 |
2.08e-24 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 99.01 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnldlsdlamherarkgiGYLPQEasifRKLTIAEN 105
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVL-----------------GYVPFK----RRKEFARR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 106 I-------------MAILET----RK--DLNKQQRQQRLNELLSDFKINHIKD------SLgmsvsgGERRRAEIARALA 160
Cdd:COG4586 97 IgvvfgqrsqlwwdLPAIDSfrllKAiyRIPDAEYKKRLDELVELLDLGELLDtpvrqlSL------GQRMRCELAAALL 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 161 ADPKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKER 245
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-243 |
5.04e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 97.43 E-value: 5.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHER-ARKGIGYLPQ--EASIFRKlTI 102
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSdIRKKVGLVFQypEYQLFEE-TI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENImAILETRKDLNKQQRQQRLNELLSDFKINH--IKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISV 180
Cdd:PRK13637 102 EKDI-AFGPINLGLSEEEIENRVKRAMNIVGLDYedYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGR 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 181 GDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN-EQVRKVYLG 243
Cdd:PRK13637 181 DEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvETLESIGLA 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
13-238 |
8.22e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 99.47 E-value: 8.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQ 92
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGIIYQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENI-MAILETRK-------DLNKQQRQQRLNELLSDFKINHIKDSLGMSVSggERRRAEIARALAADPK 164
Cdd:PRK09700 88 ELSVIDELTVLENLyIGRHLTKKvcgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSIS--HKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVR 238
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
11-237 |
1.72e-23 |
|
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: 98.36 E-value: 1.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD--KGEIHLDNLDLSDLAMHERARKGIG 88
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAENIM---AILETRKDLNKQQRQQRLNELLSDFKINHIKDSLG-MSVSGGERRRAEIARALAADPK 164
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIFlgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEgTPQEILDNEQV 237
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVAT-KDMSTMSEDDI 233
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
11-228 |
1.97e-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: 94.63 E-value: 1.97e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVG--LVRMDKGEIHLDNLDLSDLAMHERARKGIg 88
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDERARAGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YL----PQE-----ASIFrkLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKIN--HIKDSLGMSVSGGERRRAEIAR 157
Cdd:TIGR01978 80 FLafqyPEEipgvsNLEF--LRSALNARRSARGEEPLDLLDFEKLLKEKLALLDMDeeFLNRSVNEGFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 158 ALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAIC-EKAYIVSEGSVIAEGTP 228
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDV 229
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
29-241 |
2.69e-23 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 94.61 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 29 VSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVrMDKGEIHLDNLDLSDLAMHERARKGiGYLPQEAS------IFRKLTi 102
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTppfampVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 aenimaiLETRKDLNKQQRQQRLNELLSDFKINhikDSLGMSV---SGGERRRAEIA-------RALAADPKFMLLDEPF 172
Cdd:PRK03695 92 -------LHQPDKTRTEAVASALNEVAEALGLD---DKLGRSVnqlSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPM 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 173 AGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVY 241
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
25-205 |
2.86e-23 |
|
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: 93.96 E-value: 2.86e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERAR---KGIGYLPQEASIFRKLT 101
Cdd:TIGR02211 20 VLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnKKLGFIYQFHHLLPDFT 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENIMAILETRKdLNKQQRQQRLNELLSDF----KINHIKDSLgmsvSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:TIGR02211 100 ALENVAMPLLIGK-KSVKEAKERAYEMLEKVglehRINHRPSEL----SGGERQRVAIARALVNQPSLVLADEPTGNLDN 174
|
170 180
....*....|....*....|....*....
gi 480205248 178 ISVGDIKDIIQTL-KDRGIGVLITDHNVR 205
Cdd:TIGR02211 175 NNAKIIFDLMLELnRELNTSFLVVTHDLE 203
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
23-233 |
3.59e-23 |
|
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: 93.83 E-value: 3.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYLPQEASIFRKlTI 102
Cdd:cd03253 14 RPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQDTVLFND-TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENImailetrkdlnkqqRQQRLN----ELLSDFKINHIKDSL--------------GMSVSGGERRRAEIARALAADPK 164
Cdd:cd03253 92 GYNI--------------RYGRPDatdeEVIEAAKAAQIHDKImrfpdgydtivgerGLKLSGGEKQRVAIARAILKNPP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITdHNVReTLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:cd03253 158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLS-TIVNADKIIVLKDGRIVERGTHEELLA 224
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-245 |
3.87e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 3.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDL---SDLAMHERARKGIGYLPQEASIFRKLTI 102
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENIMAILETrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGD 182
Cdd:PRK10070 124 LDNTAFGMEL-AGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 183 IKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILD---NEQVRKVYLGDD 245
Cdd:PRK10070 203 MQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNnpaNDYVRTFFRGVD 269
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
1-241 |
6.22e-23 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 94.08 E-value: 6.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 1 MEQSVQQPQTLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMH 80
Cdd:PRK10575 2 QEYTNHSDTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 81 ERARKgIGYLPQEASIFRKLTIAEnIMAI--LETRKDLNK--QQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIA 156
Cdd:PRK10575 82 AFARK-VAYLPQQLPAAEGMTVRE-LVAIgrYPWHGALGRfgAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 157 RALAADPKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:PRK10575 160 MLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE 239
|
....*.
gi 480205248 236 QVRKVY 241
Cdd:PRK10575 240 TLEQIY 245
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
11-236 |
6.73e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 6.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSF------------YMVVGLVRMDKGEIHLDNLDLSDLa 78
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmndlnpeVTITGSIVYNGHNIYSPRTDTVDL- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 79 mheraRKGIGYLPQEASIFrKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKI-NHIKDSL---GMSVSGGERRRAE 154
Cdd:PRK14239 85 -----RKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLhdsALGLSGGQQQRVC 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 155 IARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITdHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:PRK14239 159 IARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDRTGFFLDGDLIEYNDTKQMFMN 237
|
..
gi 480205248 235 EQ 236
Cdd:PRK14239 238 PK 239
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-220 |
7.27e-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: 92.91 E-value: 7.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmHERArkgigYLPQEASIFRKLTIAEN 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG-PDRM-----VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 106 I-MAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIK 184
Cdd:TIGR01184 75 IaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 480205248 185 D-IIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEG 220
Cdd:TIGR01184 155 EeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
11-236 |
8.04e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.49 E-value: 8.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDN------------LDLSDLA 78
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGqtinlvrdkdgqLKVADKN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 79 MHERARKGIGYLPQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINH-IKDSLGMSVSGGERRRAEIAR 157
Cdd:PRK10619 86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIAR 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 158 ALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:PRK10619 166 ALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQ 244
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-202 |
8.93e-23 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 8.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 20 YSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHldnldlsdlamhERARKGIGYLPQEASIFRK 99
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR------------RAGGARVAYVPQRSEVPDS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 100 L--TIAENI-MAILETRKDLNKQQRQQRLnellsdfKINHIKDSLGM---------SVSGGERRRAEIARALAADPKFML 167
Cdd:NF040873 70 LplTVRDLVaMGRWARRGLWRRLTRDDRA-------AVDDALERVGLadlagrqlgELSGGQRQRALLAQGLAQEADLLL 142
|
170 180 190
....*....|....*....|....*....|....*
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:NF040873 143 LDEPTTGLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-203 |
9.66e-23 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.18 E-value: 9.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 1 MEQSVQQPQT-LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTT---SF---YMVVGLVRMDkGEIHLDNLD 73
Cdd:COG1117 1 MTAPASTLEPkIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLnrmNDLIPGARVE-GEILLDGED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 74 LSDLAMH-ERARKGIGYLPQEASIFRKlTIAENIMAILETRKDLNKQQRQQRLNELLSDFKI-NHIKDSL---GMSVSGG 148
Cdd:COG1117 80 IYDPDVDvVELRRRVGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELDEIVEESLRKAALwDEVKDRLkksALGLSGG 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 149 ERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRgIGVLITDHN 203
Cdd:COG1117 159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHN 212
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
11-208 |
1.20e-22 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 92.84 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmherARKGIGYl 90
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG----AERGVVF- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 pQEASIFRKLTIAENIMAILETRkDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK11248 77 -QNEGLLPWRNVQDNVAFGLQLA-GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 480205248 171 PFAGVDPISvgdiKDIIQTL-----KDRGIGVLITDHNVRETL 208
Cdd:PRK11248 155 PFGALDAFT----REQMQTLllklwQETGKQVLLITHDIEEAV 193
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
14-241 |
1.20e-22 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 93.13 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 14 KHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYLPQE 93
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLLAQN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 94 ASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSV---SGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK10253 90 ATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVdtlSGGQRQRAWIAMVLAQETAIMLLDE 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 171 PFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRKVY 241
Cdd:PRK10253 170 PTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
22-233 |
1.39e-22 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 92.29 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 22 KRWVVKDVSFTMQSGQIVGLLGPNGAGKTT------SFYMVvglvrmDKGEIHLDNLDLSDLAMHErARKGIGYLPQEAS 95
Cdd:cd03251 14 GPPVLRDISLDIPAGETVALVGPSGSGKSTlvnlipRFYDV------DSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 96 IFRKlTIAENIM--AILETRKDLNKQQRQQRLNELlsdfkINHIKDSL-------GMSVSGGERRRAEIARALAADPKFM 166
Cdd:cd03251 87 LFND-TVAENIAygRPGATREEVEEAARAANAHEF-----IMELPEGYdtvigerGVKLSGGQRQRIAIARALLKDPPIL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTL-KDRgiGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:cd03251 161 ILDEATSALDTESERLVQAALERLmKNR--TTFVIAHRL-STIENADRIVVLEDGKIVERGTHEELLA 225
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-235 |
1.71e-22 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 92.22 E-value: 1.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTsfymVVGLV-RM---DKGEIHLDNLDLSDLAMHERaRKGIGYLPQEASIFrKL 100
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLeRFydpTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEPVLF-DG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIM-----AILETRKDLNKQQrqqrlneLLSDFkINHIKDSL-------GMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:cd03249 92 TIAENIRygkpdATDEEVEEAAKKA-------NIHDF-IMSLPDGYdtlvgerGSQLSGGQKQRIAIARALLRNPKILLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTLKdRGIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:cd03249 164 DEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-248 |
1.96e-22 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 92.77 E-value: 1.96e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYL 90
Cdd:PRK13635 8 VEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWD-VRRQVGMV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEA-SIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:PRK13635 87 FQNPdNQFVGATVQDDVAFGLENIG-VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKD-RGIGVLITDHNVRETlAICEKAYIVSEGSVIAEGTPQEILD-NEQVRKVYLGDDFV 247
Cdd:PRK13635 166 EATSMLDPRGRREVLETVRQLKEqKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIFKsGHMLQEIGLDVPFS 244
|
.
gi 480205248 248 V 248
Cdd:PRK13635 245 V 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
26-239 |
4.89e-22 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 94.08 E-value: 4.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQ---EASIFRKLTI 102
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENiMAILETRKD------------LNKQQRQQRLNELLSdFKINHIKDSLGmSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK09700 359 AQN-MAISRSLKDggykgamglfheVDEQRTAENQRELLA-LKCHSVNQNIT-ELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRK 239
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMA 504
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
27-233 |
8.90e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 93.57 E-value: 8.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 27 KDVSFTMQSGQIVGLLGPNGAGKTT-----SFYMVVGLVRmdKGEIHLDNLDLSDLAMHERArkgiGYLPQEASIFRKLT 101
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKGVKG--SGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIPTLT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAE--NIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSL------GMSVSGGERRRAEIARALAADPKFMLLDEPFA 173
Cdd:TIGR00955 116 VREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRigvpgrVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 174 GVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETL-AICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
20-232 |
1.19e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 90.84 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 20 YSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEI--HLDNLDLSD---LAMHERA-------RKGI 87
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVlwQGKPLDYSKrglLALRQQVatvfqdpEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 88 GYLPQEASI---FRKLTIAENIMAiletrkdlnkqqrqQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPK 164
Cdd:PRK13638 91 FYTDIDSDIafsLRNLGVPEAEIT--------------RRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQAR 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK13638 157 YLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
11-226 |
1.35e-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: 88.14 E-value: 1.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamHERARKGIG 88
Cdd:cd03247 1 LSINNVSFSYpeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL--EKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKlTIAENimailetrkdlnkqqrqqrlnellsdfkinhikdsLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:cd03247 79 VLNQRPYLFDT-TLRNN-----------------------------------LGRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 169 DEPFAGVDPISVGDIKDII-QTLKDRGIgVLITDHNVreTLAICEKAYIVSEGSVIAEG 226
Cdd:cd03247 123 DEPTVGLDPITERQLLSLIfEVLKDKTL-IWITHHLT--GIEHMDKILFLENGKIIMQG 178
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-231 |
1.84e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.40 E-value: 1.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYS--KRWV--VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE--RARKG 86
Cdd:PRK11153 4 LKNISKVFPqgGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:PRK11153 84 IGMIFQHFNLLSSRTVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 167 LLDEPFAGVDPISVgdiKDIIQTLKD--RGIG---VLITdHN---VREtlaICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK11153 163 LCDEATSALDPATT---RSILELLKDinRELGltiVLIT-HEmdvVKR---ICDRVAVIDAGRLVEQGTVSEV 228
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
13-236 |
1.99e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 89.42 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLsDLAMHERARKG------ 86
Cdd:PRK11264 6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITI-DTARSLSQQKGlirqlr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 --IGYLPQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPK 164
Cdd:PRK11264 85 qhVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQ 236
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
13-171 |
2.72e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 2.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHL-DNLDlsdlamherarkgIGYLP 91
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVK-------------IGYFD 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEASIFR-KLTIAENImailetrKDLNKQQRQQRLNELLSDF---------KINHIkdslgmsvSGGERRRAEIARALAA 161
Cdd:COG0488 385 QHQEELDpDKTVLDEL-------RDGAPGGTEQEVRGYLGRFlfsgddafkPVGVL--------SGGEKARLALAKLLLS 449
|
170
....*....|
gi 480205248 162 DPKFMLLDEP 171
Cdd:COG0488 450 PPNVLLLDEP 459
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-243 |
3.29e-21 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 89.56 E-value: 3.29e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLdnldLSDLAMHERARKGIGYLPQEASI-FRKLTIAE 104
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI----LGQPTRQALQKNLVAYVPQSEEVdWSFPVLVE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NI--------MAILETRKDLNKQQRQQRLNEL-LSDFKINHIKDslgmsVSGGERRRAEIARALAADPKFMLLDEPFAGV 175
Cdd:PRK15056 99 DVvmmgryghMGWLRRAKKRDRQIVTAALARVdMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 176 DPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVsEGSVIAEGTPQEILDNEQVRKVYLG 243
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMV-KGTVLASGPTETTFTAENLELAFSG 240
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-202 |
3.56e-21 |
|
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: 87.80 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHerARKGIGYLPQEASIFRKLTI 102
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE--PHENILYLGHLPGLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENI---MAILetrkdlnkQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPIS 179
Cdd:TIGR01189 91 LENLhfwAAIH--------GGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|...
gi 480205248 180 VGDIKDIIQTLKDRGIGVLITDH 202
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTH 185
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
13-171 |
4.66e-21 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 89.79 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKR---------WV--VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE 81
Cdd:COG4608 10 VRDLKKHFPVRgglfgrtvgVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 82 RA--RKGIGYLPQE--ASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLsdfkinhikDSLGMS----------VSG 147
Cdd:COG4608 90 LRplRRRMQMVFQDpyASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELL---------ELVGLRpehadrypheFSG 160
|
170 180
....*....|....*....|....
gi 480205248 148 GERRRAEIARALAADPKFMLLDEP 171
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEP 184
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
25-209 |
5.00e-21 |
|
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: 87.87 E-value: 5.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDN----LDLSDLAMHE--RARKG-IGYLPQeasiF 97
Cdd:COG4778 26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQASPREilALRRRtIGYVSQ----F 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 98 rkLTI-----AENIMA--ILETRKDlnKQQRQQRLNELLSDFkinHIKDSL-GMS---VSGGERRRAEIARALAADPKFM 166
Cdd:COG4778 102 --LRViprvsALDVVAepLLERGVD--REEARARARELLARL---NLPERLwDLPpatFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTLKDRGIGVL-IT-DHNVRETLA 209
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFhDEEVREAVA 219
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
23-203 |
5.04e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 87.62 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDlamhERARKGIGYLPQEASIFRKLTI 102
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDD----PDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENimaiLETRKDLnKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGD 182
Cdd:PRK13539 91 AEN----LEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180
....*....|....*....|.
gi 480205248 183 IKDIIQTLKDRGIGVLITDHN 203
Cdd:PRK13539 166 FAELIRAHLAQGGIVIAATHI 186
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
11-231 |
5.56e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 91.24 E-value: 5.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHL-AKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGY 89
Cdd:COG3845 258 LEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEasifRK-------LTIAENimAILETRKD--------LNKQQRQQRLNELLSDFKI--NHIKDSLGmSVSGGERRR 152
Cdd:COG3845 338 IPED----RLgrglvpdMSVAEN--LILGRYRRppfsrggfLDRKAIRAFAEELIEEFDVrtPGPDTPAR-SLSGGNQQK 410
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 153 AEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:COG3845 411 VILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEA 489
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
13-239 |
7.55e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.70 E-value: 7.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY--SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD---KGEIHLDNLDLSDLAMHE-RARKG 86
Cdd:PRK13640 8 FKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDdnpNSKITVDGITLTAKTVWDiREKVG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASiFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFM 166
Cdd:PRK13640 88 IVFQNPDNQ-FVGATVGDDVAFGLENRA-VPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 167 LLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETlAICEKAYIVSEGSVIAEGTPQEILDNEQVRK 239
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-231 |
1.10e-20 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 89.62 E-value: 1.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 1 MEQSVQQPQTLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMH 80
Cdd:PRK09452 5 NKQPSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 81 ERArkgIGYLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALA 160
Cdd:PRK09452 85 NRH---VNTVFQSYALFPHMTVFENVAFGLRMQK-TPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 161 ADPKFMLLDEPFAGVD----PISVGDIKDIIQTLkdrGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK09452 161 NKPKVLLLDESLSALDyklrKQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
11-237 |
1.44e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.14 E-value: 1.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRW-----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNL----DLSDLAMHE 81
Cdd:PRK13645 7 IILDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKKIKEVK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 82 RARKGIGYLPQ--EASIFRKlTIAENImAILETRKDLNKQQRQQRLNELLSDFKI--NHIKDSlGMSVSGGERRRAEIAR 157
Cdd:PRK13645 87 RLRKEIGLVFQfpEYQLFQE-TIEKDI-AFGPVNLGENKQEAYKKVPELLKLVQLpeDYVKRS-PFELSGGQKRRVALAG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 158 ALAADPKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:PRK13645 164 IIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE 243
|
.
gi 480205248 237 V 237
Cdd:PRK13645 244 L 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
19-202 |
1.47e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 86.16 E-value: 1.47e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 19 NYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDL-SDLAMHErarKGIGYLPQEASIF 97
Cdd:PRK13540 10 DYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQ---KQLCFVGHRSGIN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 98 RKLTIAENIMAiletrkDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:PRK13540 87 PYLTLRENCLY------DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*
gi 480205248 178 ISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-227 |
1.56e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 87.43 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA--RKGIGYLPQEA-SIF--RK 99
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafRRDIQMVFQDSiSAVnpRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 100 lTIAENIMAILETRKDLNKQQRQQRLNELLSDFKIN-HIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPI 178
Cdd:PRK10419 107 -TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLDLV 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 480205248 179 SVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGT 227
Cdd:PRK10419 186 LQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETQP 235
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
23-235 |
1.85e-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: 86.77 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSdLAMHERARKGIGYLPQEASIFRKlTI 102
Cdd:cd03252 15 PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA-LADPAWLRRQVGVVLQENVLFNR-SI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENImAILETRKDLNKQQRQQRL---NELLSDFKI--NHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:cd03252 93 RDNI-ALADPGMSMERVIEAAKLagaHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 178 ISVgdiKDIIQTLKD--RGIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:cd03252 172 ESE---HAIMRNMHDicAGRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
13-247 |
2.33e-20 |
|
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: 89.48 E-value: 2.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL--VRMDKGEI--HL------------------- 69
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyHValcekcgyverpskvgepc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 70 ------------DNLDLSDlAMHERARKGIGYLPQEA-SIFRKLTIAENIMAILEtRKDLNKQQRQQRLNELLSDFKINH 136
Cdd:TIGR03269 83 pvcggtlepeevDFWNLSD-KLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 137 IKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKD-IIQTLKDRGIGVLITDH--NVRETLAicEK 213
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHwpEVIEDLS--DK 238
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 480205248 214 AYIVSEGSVIAEGTPQEIL--------DNEQVRKVYLGDDFV 247
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVavfmegvsEVEKECEVEVGEPII 280
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
18-228 |
2.37e-20 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 85.54 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 18 KNYSKRW------VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHeRARKGIGYLP 91
Cdd:cd03369 10 ENLSVRYapdlppVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-DLRSSLTIIP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEASIFrkltiaeniMAILETRKDLNKQQRQQRLNELLSdfkinhIKDSlGMSVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:cd03369 89 QDPTLF---------SGTIRSNLDPFDEYSDEEIYGALR------VSEG-GLNLSQGQRQLLCLARALLKRPRVLVLDEA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 172 FAGVDPISVGDIKDIIQTLKdRGIGVLITDHNVReTLAICEKAYIVSEGSVIAEGTP 228
Cdd:cd03369 153 TASIDYATDALIQKTIREEF-TNSTILTIAHRLR-TIIDYDKILVMDAGEVKEYDHP 207
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-243 |
3.62e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 1 MEQSVQQPQTLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDL---SDL 77
Cdd:PRK14246 1 MEAGKSAEDVFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 78 AMHE--RARKGIGYLPQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKI-NHIKDSL---GMSVSGGERR 151
Cdd:PRK14246 81 FQIDaiKLRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 152 RAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRgIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK14246 161 RLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEI 239
|
250
....*....|....*
gi 480205248 232 L---DNEQVRKVYLG 243
Cdd:PRK14246 240 FtspKNELTEKYVIG 254
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
13-228 |
5.03e-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: 85.24 E-value: 5.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSK--RWVVKDVSFTMQSGQIVGLLGPNGAGKTTsfyMVVGLVRM---DKGEIHLDNLDLSDLAMHeRARKGI 87
Cdd:cd03244 5 FKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSS---LLLALFRLvelSSGSILIDGVDISKIGLH-DLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 88 GYLPQEASIFRKlTIAENIMAILE-TRKDLNKQQRQQRLNELLSDF--KINHIKDSLGMSVSGGERRRAEIARALAADPK 164
Cdd:cd03244 81 SIIPQDPVLFSG-TIRSNLDPFGEySDEELWQALERVGLKEFVESLpgGLDTVVEEGGENLSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQT-LKDRgiGVLITDHNVrETLAICEKAYIVSEGSVIAEGTP 228
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREaFKDC--TVLTIAHRL-DTIIDSDRILVLDKGRVVEFDSP 221
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-236 |
6.90e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 85.92 E-value: 6.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 15 HLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTsfyMVVGLVRMD--------KGEIHLDNLDLSDLAMHERARKG 86
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTT---FLRTLNRMNdkvsgyrySGDVLLGGRSIFNYRDVLEFRRR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 87 IGYLPQEASIFrKLTIAENIMAILETRKDLNKQQ----RQQRLNEL-LSDFKINHIKDSlGMSVSGGERRRAEIARALAA 161
Cdd:PRK14271 103 VGMLFQRPNPF-PMSIMDNVLAGVRAHKLVPRKEfrgvAQARLTEVgLWDAVKDRLSDS-PFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 162 DPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRgIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPK 254
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
24-237 |
7.12e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.44 E-value: 7.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 24 WVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA---------------RKGIG 88
Cdd:PRK13631 40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkiknfkelRRRVS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQ--EASIFrKLTIAENIM---AILETRKDLNKQQRQQRLNELLSDFKInhiKDSLGMSVSGGERRRAEIARALAADP 163
Cdd:PRK13631 120 MVFQfpEYQLF-KDTIEKDIMfgpVALGVKKSEAKKLAKFYLNKMGLDDSY---LERSPFGLSGGQKRRVAIAGILAIQP 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 164 KFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQV 237
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQHI 269
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
13-209 |
8.44e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.17 E-value: 8.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIhldnldlsdlamhERARK-GIGYLP 91
Cdd:PRK09544 7 LENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-------------KRNGKlRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QeasifrKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:PRK09544 74 Q------KLYLDTTLPLTVNRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEP 147
|
170 180 190
....*....|....*....|....*....|....*....
gi 480205248 172 FAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLA 209
Cdd:PRK09544 148 TQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMA 186
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
33-248 |
1.08e-19 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 88.15 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 33 MQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLsdLAMHERARKGIGYLPQEASIFRKLTIAENIMAILET 112
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARL 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 113 RkDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKD 192
Cdd:TIGR01257 2040 R-GVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIR 2118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 193 RGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIldneqvrKVYLGDDFVV 248
Cdd:TIGR01257 2119 EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL-------KSKFGDGYIV 2167
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-234 |
1.12e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 84.96 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD-----KGEIHLDNLDLSDLAMHErARK 85
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIE-LRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 86 GIGYLPQEASIFRKLTIAENIMAILE-TRKDLNKQQRQQRLNELLSDFKI-NHIKDSLGM---SVSGGERRRAEIARALA 160
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKlNRLVKSKKELQERVRWALEKAQLwDEVKDRLDApagKLSGGQQQRLCIARALA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 161 ADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITdHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
13-176 |
1.22e-19 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 86.62 E-value: 1.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamhERARKGIGYLPQ 92
Cdd:PRK11000 6 LRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDV---PPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 EASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:PRK11000 83 SYALYPHLSVAENMSFGLKLAG-AKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPL 161
|
....
gi 480205248 173 AGVD 176
Cdd:PRK11000 162 SNLD 165
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
27-220 |
1.59e-19 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 87.03 E-value: 1.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 27 KDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLP---QEASIFRKLTIA 103
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 104 ENIMAILETRKDLnkQQRQQRLNELLSDF------KINHIKDSLGmSVSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:PRK15439 360 WNVCALTHNRRGF--WIKPARENAVLERYrralniKFNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDV 436
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 480205248 178 ISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEG 220
Cdd:PRK15439 437 SARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
11-233 |
1.75e-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: 87.10 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYS-KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGY 89
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHT-LRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASIFRKlTIAENImaILETRKDLNKQqrqqrlnELLSDFKINHIKDSL--------------GMSVSGGERRRAEI 155
Cdd:TIGR01193 553 LPQEPYIFSG-SILENL--LLGAKENVSQD-------EIWAACEIAEIKDDIenmplgyqtelseeGSSISGGQKQRIAL 622
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 156 ARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETlaiCEKAYIVSEGSVIAEGTPQEILD 233
Cdd:TIGR01193 623 ARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDKTIIFVAHRLSVAKQ---SDKIIVLDHGKIIEQGSHDELLD 697
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
18-233 |
2.99e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.59 E-value: 2.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 18 KNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDN-----LDLsdlamherarkGIGYLPQ 92
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGrvsalLEL-----------GAGFHPE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 easifrkLTIAENIM---AILetrkDLNKQQRQQRLNEL-----LSDFkINH-IKD-SLGMsvsggerrRAEIARALAA- 161
Cdd:COG1134 103 -------LTGRENIYlngRLL----GLSRKEIDEKFDEIvefaeLGDF-IDQpVKTySSGM--------RARLAFAVATa 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 162 -DPKFMLLDEpfagVdpISVGDI------KDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:COG1134 163 vDPDILLVDE----V--LAVGDAafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
13-236 |
4.37e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 84.37 E-value: 4.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRW-----VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA---- 83
Cdd:PRK13651 5 VKNIVKIFNKKLptelkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKekvl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 84 -------------------RKGIGYLPQ--EASIFrKLTIAENIM--AIletRKDLNKQQRQQRLNELLS--DFKINHIK 138
Cdd:PRK13651 85 eklviqktrfkkikkikeiRRRVGVVFQfaEYQLF-EQTIEKDIIfgPV---SMGVSKEEAKKRAAKYIElvGLDESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 139 DSlGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVS 218
Cdd:PRK13651 161 RS-PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250
....*....|....*...
gi 480205248 219 EGSVIAEGTPQEILDNEQ 236
Cdd:PRK13651 240 DGKIIKDGDTYDILSDNK 257
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-205 |
6.15e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.56 E-value: 6.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 1 MEQSVQQPQTLCIKHLAKNYSKRwVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMH 80
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTD-VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 81 ERAR---KGIGYLPQEASIFRKLTIAENI-MAILETRKdlNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIA 156
Cdd:PRK11629 80 AKAElrnQKLGFIYQFHHLLPDFTALENVaMPLLIGKK--KPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 480205248 157 RALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVR 205
Cdd:PRK11629 158 RALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLqGTAFLVVTHDLQ 207
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-234 |
6.64e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 82.97 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 20 YSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD-----KGEIHLDNLDLSDLAMHE-RARKGIGYLPQE 93
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPiEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 94 ASIFRKLTIAENIM------AILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGmSVSGGERRRAEIARALAADPKFML 167
Cdd:PRK14267 94 PNPFPHLTIYDNVAigvklnGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPS-NLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITdHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
25-239 |
1.11e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 82.83 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASIFRKLTIAE 104
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNPDNQIVATIVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIK 184
Cdd:PRK13633 105 EDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREVV 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 185 DIIQTL-KDRGIGVLITDHNVRETlAICEKAYIVSEGSVIAEGTPQEILDNEQVRK 239
Cdd:PRK13633 185 NTIKELnKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIFKEVEMMK 239
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-243 |
1.81e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 81.96 E-value: 1.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASI-FRKLTIAE 104
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGIVFQNPETqFVGRTVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NiMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIK 184
Cdd:PRK13644 98 D-LAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 185 DIIQTLKDRGIGVLITDHNVREtLAICEKAYIVSEGSVIAEGTPQEILDNEQVRkvYLG 243
Cdd:PRK13644 177 ERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-231 |
2.03e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 84.02 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHL--DNLDLSDLAmherARKGIGYLPQEASIFRKLTIA 103
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgQPVDAGDIA----TRRRVGYMSQAFSLYGELTVR 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 104 ENIMaiLETRK-DLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISvgd 182
Cdd:NF033858 358 QNLE--LHARLfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVA--- 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 480205248 183 iKD-----IIQTLKDRGIGVLITDHNVRETlAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:NF033858 433 -RDmfwrlLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASDTPAAL 484
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-226 |
2.14e-18 |
|
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: 80.65 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 17 AKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMherarkGIGYLPQeasi 96
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGL------GGGFNPE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 97 frkLTIAENI--MAILetrKDLNKQQRQQRLNEL-----LSDFKINHIKD-SLGMSVsggerrRAEIARALAADPKFMLL 168
Cdd:cd03220 99 ---LTGRENIylNGRL---LGLSRKEIDEKIDEIiefseLGDFIDLPVKTySSGMKA------RLAFAIATALEPDILLI 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 169 DEPFAgvdpisVGDI------KDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEG 226
Cdd:cd03220 167 DEVLA------VGDAafqekcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
7-237 |
2.16e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 83.83 E-value: 2.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 7 QPQTLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD--KGEIHLDNLDLSDLAMHERAR 84
Cdd:PRK13549 2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTER 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 85 KGIGYLPQEASIFRKLTIAENIMAILETRKD--LNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAAD 162
Cdd:PRK13549 82 AGIAIIHQELALVKELSVLENIFLGNEITPGgiMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 163 PKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEgTPQEILDNEQV 237
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGT-RPAAGMTEDDI 235
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-220 |
2.81e-18 |
|
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: 78.64 E-value: 2.81e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnldlsdlamherARKGIGYL 90
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQeasifrkltiaenimailetrkdlnkqqrqqrlnellsdfkinhikdslgmsVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:cd03221 69 EQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 480205248 171 PFAGVDPISvgdIKDIIQTLKDRGIGVLITDHNvRETL-AICEKAYIVSEG 220
Cdd:cd03221 97 PTNHLDLES---IEALEEALKEYPGTVILVSHD-RYFLdQVATKIIELEDG 143
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
11-202 |
3.04e-18 |
|
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: 79.84 E-value: 3.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLsDLAMHERARkGIGYL 90
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL-DFQRDSIAR-GLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENimaiLETRKDLNKqqrQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:cd03231 79 GHAPGIKTTLSVLEN----LRFWHADHS---DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|..
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:cd03231 152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
36-225 |
6.01e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 82.36 E-value: 6.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 36 GQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASIFRKLTIAENIMAILETRKD 115
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAENIFLGREFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 116 LNK---QQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKD 192
Cdd:PRK10762 110 FGRidwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS 189
|
170 180 190
....*....|....*....|....*....|...
gi 480205248 193 RGIGVLITDHNVRETLAICEKAYIVSEGSVIAE 225
Cdd:PRK10762 190 QGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
26-236 |
7.92e-18 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 82.04 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRmDKGEIHLDNLDLSDLAMHE--RARKGIGYLPQE--ASIFRKLT 101
Cdd:COG4172 302 VDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP-SEGEIRFDGQDLDGLSRRAlrPLRRRMQVVFQDpfGSLSPRMT 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENI---MAILETrkDLNKQQRQQRLNELLSDfkinhikdsLGMS----------VSGGERRRAEIARALAADPKFMLL 168
Cdd:COG4172 381 VGQIIaegLRVHGP--GLSAAERRARVAEALEE---------VGLDpaarhrypheFSGGQRQRIAIARALILEPKLLVL 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 169 DEPFAGVDpISVGdiKDIIQTLKD----RGIG-VLITdHN---VRetlAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:COG4172 450 DEPTSALD-VSVQ--AQILDLLRDlqreHGLAyLFIS-HDlavVR---ALAHRVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-237 |
8.09e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 80.16 E-value: 8.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE-RARKGIGYLPQEASIFrKLTIAE 104
Cdd:PRK13647 21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGLVFQDPDDQVF-SSTVWD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NImAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIK 184
Cdd:PRK13647 100 DV-AFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQETLM 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 480205248 185 DIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPqEILDNEQV 237
Cdd:PRK13647 179 EILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDK-SLLTDEDI 230
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
25-176 |
8.14e-18 |
|
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: 79.40 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERAR---KGIGYLPQEASIFRKLT 101
Cdd:COG4181 27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlraRHVGFVFQSFQLLPTLT 106
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 102 IAENIMAILETRKDLNKQQRQQRLNEL--LSDfKINHIKDSLgmsvSGGERRRAEIARALAADPKFMLLDEPFAGVD 176
Cdd:COG4181 107 ALENVMLPLELAGRRDARARARALLERvgLGH-RLDHYPAQL----SGGEQQRVALARAFATEPAILFADEPTGNLD 178
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
28-238 |
8.77e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 81.07 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSD------LAMHERarkGIGYLPQEASIFRKLT 101
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDaekgicLPPEKR---RIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENImailetRKDLNKQQRQQ--RLNELLSdfkINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPIS 179
Cdd:PRK11144 93 VRGNL------RYGMAKSMVAQfdKIVALLG---IEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 180 VGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVR 238
Cdd:PRK11144 164 KRELLPYLERLaREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
20-206 |
9.79e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 20 YSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTT---SFYMVVGLV---RMDkGEI--HLDNLDLSDLAMHErARKGIGYLP 91
Cdd:PRK14243 20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIpgfRVE-GKVtfHGKNLYAPDVDPVE-VRRRIGMVF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEASIFRKlTIAENIM---AILETRKDLNKQ-QRQQRLNELLSDFKiNHIKDSlGMSVSGGERRRAEIARALAADPKFML 167
Cdd:PRK14243 98 QKPNPFPK-SIYDNIAygaRINGYKGDMDELvERSLRQAALWDEVK-DKLKQS-GLSLSGGQQQRLCIARAIAVQPEVIL 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITdHNVRE 206
Cdd:PRK14243 175 MDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HNMQQ 212
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
26-236 |
1.07e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 79.80 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYLPQEA-SIFRKLTIAE 104
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK-LRKHIGIVFQNPdNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIK 184
Cdd:PRK13648 104 DVAFGLENHA-VPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLL 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 185 DIIQTLK-DRGIGVLITDHNVRETLaicEKAYIV--SEGSVIAEGTPQEILDNEQ 236
Cdd:PRK13648 183 DLVRKVKsEHNITIISITHDLSEAM---EADHVIvmNKGTVYKEGTPTEIFDHAE 234
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
11-206 |
1.23e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.99 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmHERARKGIGYL 90
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLK-PEIYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKlTIAENIMAILETRkdlNKQQRQQRLNELLSDFKI-NHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIR---NQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 480205248 170 EPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRE 206
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDE 200
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
23-231 |
1.33e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 80.06 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHL---------DNLDLSDLamheraRKGIGYLPQ- 92
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitagkKNKKLKPL------RKKVGIVFQf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 -EASIFRKlTIAENImAILETRKDLNKQQRQQRLNELLSDFKINHikDSLGMS---VSGGERRRAEIARALAADPKFMLL 168
Cdd:PRK13634 94 pEHQLFEE-TVEKDI-CFGPMNFGVSEEDAKQKAREMIELVGLPE--ELLARSpfeLSGGQMRRVAIAGVLAMEPEVLVL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK13634 170 DEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
25-221 |
1.83e-17 |
|
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: 77.89 E-value: 1.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLdnldlsdlamheraRKGIGYLPQEASIFRkLTIAE 104
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSV--------------PGSIAYVSQEPWIQN-GTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIMailetrkdLNKQQRQQRLNE------LLSDFKINHIKD-----SLGMSVSGGERRRAEIARALAADPKFMLLDEPFA 173
Cdd:cd03250 85 NIL--------FGKPFDEERYEKvikacaLEPDLEILPDGDlteigEKGINLSGGQKQRISLARAVYSDADIYLLDDPLS 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 480205248 174 GVDPiSVGD--IKDIIQ-TLKDRGIGVLITdHNVrETLAICEKAYIVSEGS 221
Cdd:cd03250 157 AVDA-HVGRhiFENCILgLLLNNKTRILVT-HQL-QLLPHADQIVVLDNGR 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
19-239 |
3.12e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.54 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 19 NYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYLPQEASIFR 98
Cdd:TIGR00958 490 NRPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ-VALVGQEPVLFS 568
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 99 KlTIAENIMAILE--TRKDLNKQQRQQRLNELLSDFK--INHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAG 174
Cdd:TIGR00958 569 G-SVRENIAYGLTdtPDEEIMAAAKAANAHDFIMEFPngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSA 647
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 175 VDpisvGDIKDIIQTLKDR-GIGVLITDHNvretLAICEKA---YIVSEGSVIAEGTPQEILDNEQVRK 239
Cdd:TIGR00958 648 LD----AECEQLLQESRSRaSRTVLLIAHR----LSTVERAdqiLVLKKGSVVEMGTHKQLMEDQGCYK 708
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
13-233 |
3.12e-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: 80.72 E-value: 3.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSK--RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDkGEIHLDNLDLSDLAMhERARKGIGYL 90
Cdd:TIGR01271 1220 VQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTL-QTWRKAFGVI 1297
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKlTIAENIMAILE-TRKDLNKQQRQQRLNELLSDF--KINHIKDSLGMSVSGGERRRAEIARALAADPKFML 167
Cdd:TIGR01271 1298 PQKVFIFSG-TFRKNLDPYEQwSDEEIWKVAEEVGLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKILL 1376
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 168 LDEPFAGVDPISVGDI-KDIIQTLKDrgIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:TIGR01271 1377 LDEPSAHLDPVTLQIIrKTLKQSFSN--CTVILSEHRV-EALLECQQFLVIEGSSVKQYDSIQKLLN 1440
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-232 |
3.51e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.96 E-value: 3.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 29 VSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQ---EASIFRKLTIAEN 105
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 106 I------------MAILETRKDLNKQQRQQRLNellsdfkinhIK----DSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:PRK11288 352 InisarrhhlragCLINNRWEAENADRFIRSLN----------IKtpsrEQLIMNLSGGNQQKAILGRWLSEDMKVILLD 421
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 170 EPFAGVDpisVG---DIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAE-----GTPQEIL 232
Cdd:PRK11288 422 EPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGElareqATERQAL 489
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
13-231 |
4.21e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 78.23 E-value: 4.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY---SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGY 89
Cdd:PRK13650 7 VKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEA-SIFRKLTIAENIMAILETrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:PRK13650 86 VFQNPdNQFVGATVEDDVAFGLEN-KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVREtLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-232 |
5.59e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 79.78 E-value: 5.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 20 YSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQ--EASIF 97
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPRIAYMPQglGKNLY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 98 RKLTIAENImailetrkD-------LNKQQRQQRLNELLsdfkinhikDSLGMS---------VSGGERRRAEIARALAA 161
Cdd:NF033858 91 PTLSVFENL--------DffgrlfgQDAAERRRRIDELL---------RATGLApfadrpagkLSGGMKQKLGLCCALIH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 162 DPKFMLLDEPFAGVDPISVGDIKDIIQTLKDR--GIGVLI-TdhnvretlaicekAYI-----------VSEGSVIAEGT 227
Cdd:NF033858 154 DPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVaT-------------AYMeeaerfdwlvaMDAGRVLATGT 220
|
....*
gi 480205248 228 PQEIL 232
Cdd:NF033858 221 PAELL 225
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
27-232 |
6.68e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 6.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 27 KDVSFTMQSGQIVGLLGPNGAGKTT------SFYMVvglvrmDKGEIHLDNLDLSDLAMhERARKGIGYLPQEASIFRKl 100
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTianlltRFYDI------DEGEILLDGHDLRDYTL-ASLRNQVALVSQNVHLFND- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIMAILE---TRKDLNKQQRQQRLnellSDFkINHIKDSL-------GMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK11176 432 TIANNIAYARTeqySREQIEEAARMAYA----MDF-INKMDNGLdtvigenGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 171 PFAGVDPISVGDIKDIIQTL-KDRgiGVLITDHNvretLAICEKA---YIVSEGSVIAEGTPQEIL 232
Cdd:PRK11176 507 ATSALDTESERAIQAALDELqKNR--TSLVIAHR----LSTIEKAdeiLVVEDGEIVERGTHAELL 566
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-233 |
7.21e-17 |
|
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: 79.38 E-value: 7.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYLPQEASIFRKlTI 102
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS-LRRQVALVSQDVVLFND-TI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENImAILETRKDLNKQQRQQRLNELLSDFkINHIKDSL-------GMSVSGGERRRAEIARALAADPKFMLLDEPFAGV 175
Cdd:TIGR02203 423 ANNI-AYGRTEQADRAEIERALAAAYAQDF-VDKLPLGLdtpigenGVLLSGGQRQRLAIARALLKDAPILILDEATSAL 500
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 176 DPISVGDIKDIIQTLKdRGIGVLITDHNvretLAICEKA---YIVSEGSVIAEGTPQEILD 233
Cdd:TIGR02203 501 DNESERLVQAALERLM-QGRTTLVIAHR----LSTIEKAdriVVMDDGRIVERGTHNELLA 556
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
11-222 |
8.11e-17 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 77.03 E-value: 8.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDlamherARKGIGYL 90
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------AREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMaiLETRKDLnKQQRQQRLNEL-LSDfKINHIKDSLgmsvSGGERRRAEIARALAADPKFMLLD 169
Cdd:PRK11247 87 FQDARLLPWKKVIDNVG--LGLKGQW-RDAALQALAAVgLAD-RANEWPAAL----SGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 480205248 170 EPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSV 222
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-231 |
8.68e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 8.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRmDKGEIHLDNLDLSDLAMHE----RARKGIGYLPQEASIFRKL 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLNRRQllpvRHRIQVVFQDPNSSLNPRL 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIMAILET-RKDLNKQQRQQR----LNELLSDFKINHIKDSlgmSVSGGERRRAEIARALAADPKFMLLDEPFAGV 175
Cdd:PRK15134 380 NVLQIIEEGLRVhQPTLSAAQREQQviavMEEVGLDPETRHRYPA---EFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 176 DPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK15134 457 DKTVQAQILALLKSLQQKhQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
28-242 |
1.13e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLD----NLDLSDLAMhERARKGIGYLPQ--EASIFRKlT 101
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAgyhiTPETGNKNL-KKLRKKVSLVFQfpEAQLFEN-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENIMAILETRKDLNKQQRQQRLNEL----LSDFKINHIKDSLgmsvSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALKWLkkvgLSEDLISKSPFEL----SGGQMRRVAIAGVMAYEPEILCLDEPAAGLDP 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 178 ISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL-DNEQVRKVYL 242
Cdd:PRK13641 179 EGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFsDKEWLKKHYL 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
22-193 |
1.14e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.85 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 22 KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTsfymVVGLVRM----DKGEIHLDNLDLSDLAMhERARKGIGYLPQEASIF 97
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKST----LINLLQRvfdpQSGRILIDGTDIRTVTR-ASLRRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 98 RKlTIAENIMAILETRKD---LNKQQRQQRLNELL-SDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFA 173
Cdd:PRK13657 422 NR-SIEDNIRVGRPDATDeemRAAAERAQAHDFIErKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATS 500
|
170 180
....*....|....*....|.
gi 480205248 174 GVDPISVGDIKDIIQTL-KDR 193
Cdd:PRK13657 501 ALDVETEAKVKAALDELmKGR 521
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-234 |
1.62e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 76.61 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTsfyMVVGLVRMDK--GEIHLD-NLDLSDLAMHERaRKGIGY 89
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKST---FLKCLNRMNEleSEVRVEgRVEFFNQNIYER-RVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEAS-IFRK-----LTIAENI---MAILETRKDLNKQ---QRQQRLNELLSDFKiNHIKDSlGMSVSGGERRRAEIAR 157
Cdd:PRK14258 86 LRRQVSmVHPKpnlfpMSVYDNVaygVKIVGWRPKLEIDdivESALKDADLWDEIK-HKIHKS-ALDLSGGQQQRLCIAR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 158 ALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRG-IGVLITDHNVRETLAICE-KAYIVSEGSVIAE----GTPQEI 231
Cdd:PRK14258 164 ALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDfTAFFKGNENRIGQlvefGLTKKI 243
|
...
gi 480205248 232 LDN 234
Cdd:PRK14258 244 FNS 246
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
28-232 |
2.81e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 76.31 E-value: 2.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHER---ARKGIGYLPQ--EASIFRKLTI 102
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEikpVRKKVGVVFQfpESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AEniMAILETRKDLNKQQRQQRLNELLSDFKIN-HIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:PRK13643 104 KD--VAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 480205248 182 DIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
25-236 |
4.18e-16 |
|
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: 77.03 E-value: 4.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL----VRMDKGEIHLDNLDLsdLAMHERARKG-----IGYLPQE-- 93
Cdd:COG4172 25 AVKGVSFDIAAGETLALVGESGSGKSVTALSILRLlpdpAAHPSGSILFDGQDL--LGLSERELRRirgnrIAMIFQEpm 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 94 ASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGM---SVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:COG4172 103 TSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVMIAMALANEPDLLIADE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDR-GIGVL-ITdHN---VREtlaICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:COG4172 183 PTTALDVTVQAQILDLLKDLQRElGMALLlIT-HDlgvVRR---FADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-237 |
5.65e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 76.51 E-value: 5.65e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 17 AKNYS-------KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVR-MDKGEIHLDNLDLSDLAMHERARKGIG 88
Cdd:PRK13549 262 VRNLTawdpvnpHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEasifRK-------LTIAENI-MAILET---RKDLNKQQRQQRLNELLSDFKIN--HIKDSLGmSVSGGERRRAEI 155
Cdd:PRK13549 342 MVPED----RKrdgivpvMGVGKNItLAALDRftgGSRIDDAAELKTILESIQRLKVKtaSPELAIA-RLSGGNQQKAVL 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 156 ARALAADPKFMLLDEPFAGVDpisVG---DIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEgTPQEIL 232
Cdd:PRK13549 417 AKCLLLNPKILILDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD-LINHNL 492
|
....*
gi 480205248 233 DNEQV 237
Cdd:PRK13549 493 TQEQV 497
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-171 |
5.67e-16 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 76.51 E-value: 5.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnlDLSDLAMHERARKGigyLPQ 92
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--ETVKLAYVDQSRDA---LDP 399
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 93 EASIFRKLTIAENIMAIleTRKDLNKQQRQQRLNellsdFKINHIKDSLGMsVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:TIGR03719 400 NKTVWEEISGGLDIIKL--GKREIPSRAYVGRFN-----FKGSDQQKKVGQ-LSGGERNRVHLAKTLKSGGNVLLLDEP 470
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-202 |
7.96e-16 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 7.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDL--------SDLAmherarkgigYLPQEASIFRK 99
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrrqrdeyhQDLL----------YLGHQPGIKTE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 100 LTIAENiMAILetrkdlnkqqrqQRLNELLSDFKINHIKDSLGM---------SVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK13538 89 LTALEN-LRFY------------QRLHGPGDDEALWEALAQVGLagfedvpvrQLSAGQQRRVALARLWLTRAPLWILDE 155
|
170 180 190
....*....|....*....|....*....|..
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-235 |
8.75e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 76.02 E-value: 8.75e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMvvgLVR---MDKGEIHLDNLDLSDLamHERA-RKGIGYLPQEASIF--- 97
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQL---LTRawdPQQGEILLNGQPIADY--SEAAlRQAISVVSQRVHLFsat 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 98 -RK-LTIA------ENIMAILEtRKDLNKQ-QRQQRLNELLSDfkinhikdsLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:PRK11160 430 lRDnLLLAapnasdEALIEVLQ-QVGLEKLlEDDKGLNAWLGE---------GGRQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 169 DEPFAGVDPISVGDIKDII-QTLKDRGIgVLITdHNVREtLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:PRK11160 500 DEPTEGLDAETERQILELLaEHAQNKTV-LMIT-HRLTG-LEQFDRICVMDNGQIIEQGTHQELLAQQ 564
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
25-235 |
1.09e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.17 E-value: 1.09e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYLPQEASIFRKlTIAE 104
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-LRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIMAILE-TRKDLNKQQRQQRLNELLSD--FKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPisvg 181
Cdd:PLN03232 1329 NIDPFSEhNDADLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV---- 1404
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 182 DIKDIIQ-TLKD--RGIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:PLN03232 1405 RTDSLIQrTIREefKSCTMLVIAHRL-NTIIDCDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
19-176 |
1.71e-15 |
|
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: 72.89 E-value: 1.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 19 NYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmHERARKGIGYLPQEASIFR 98
Cdd:cd03248 23 TRPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYE-HKYLHSKVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 99 KlTIAENIMAILETRKDLNKQQRQQRLN--ELLSDFKINHIKDS--LGMSVSGGERRRAEIARALAADPKFMLLDEPFAG 174
Cdd:cd03248 102 R-SLQDNIAYGLQSCSFECVKEAAQKAHahSFISELASGYDTEVgeKGSQLSGGQKQRVAIARALIRNPQVLILDEATSA 180
|
..
gi 480205248 175 VD 176
Cdd:cd03248 181 LD 182
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-225 |
1.91e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 75.04 E-value: 1.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEasifRK------ 99
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISED----RKrdglvl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 100 -LTIAENiMAILETRKDLNK--QQRQQRLNELLSDF-KINHIK----DSLGMSVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:PRK10762 344 gMSVKEN-MSLTALRYFSRAggSLKHADEQQAVSDFiRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEP 422
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 172 FAGVDpisVGDIKDI---IQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAE 225
Cdd:PRK10762 423 TRGVD---VGAKKEIyqlINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGE 476
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
32-176 |
1.95e-15 |
|
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: 73.21 E-value: 1.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 32 TMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSdlamherarkgigYLPQEASIFRKLTIAENIMAILE 111
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKPQYIKADYEGTVRDLLSSITK 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 112 trkdlNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVD 176
Cdd:cd03237 88 -----DFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD 147
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
13-233 |
2.17e-15 |
|
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: 73.74 E-value: 2.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSK--RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDkGEIHLDNLDLSDLAMHErARKGIGYL 90
Cdd:cd03289 5 VKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQK-WRKAFGVI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKlTIAENIMAILE-TRKDLNKQQRQQRLNELLSDF--KINHIKDSLGMSVSGGERRRAEIARALAADPKFML 167
Cdd:cd03289 83 PQKVFIFSG-TFRKNLDPYGKwSDEEIWKVAEEVGLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 168 LDEPFAGVDPISvgdIKDIIQTLKD--RGIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILD 233
Cdd:cd03289 162 LDEPSAHLDPIT---YQVIRKTLKQafADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLN 225
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
8-222 |
2.29e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 73.20 E-value: 2.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 8 PQTLCIKHLAKnYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL----VRMDKGEIHLDNLDLSDLAMheRA 83
Cdd:PRK10418 2 PQQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGIlpagVRQTAGRVLLDGKPVAPCAL--RG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 84 RKGIGYLPQEASIFRKL-TIAENImaiLETRKDLNKQQRQQRLNELLSDFKINHIKDSLGM---SVSGGERRRAEIARAL 159
Cdd:PRK10418 79 RKIATIMQNPRSAFNPLhTMHTHA---RETCLALGKPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 160 AADPKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNV------RETLAICEKAYIVSEGSV 222
Cdd:PRK10418 156 LCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMgvvarlADDVAVMSHGRIVEQGDV 225
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-237 |
2.43e-15 |
|
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: 74.86 E-value: 2.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 22 KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD-KGEIHLDNLDLSDLAMHERARKGIGYLPQEAS---IF 97
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 98 RKLTIAENI-MAILE---TRKDLNKQQRQQRLNELLSDFKINHIKDSLGM-SVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:TIGR02633 352 PILGVGKNItLSVLKsfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIgRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 173 AGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEiLDNEQV 237
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHA-LTQEQV 495
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
13-231 |
2.61e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 74.00 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSfYMVVGLVRMDKGEihlDNLDLSDLAMHERA-RKGIG-YL 90
Cdd:NF000106 16 VRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANRRAlRRTIG*HR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAIlETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:NF000106 92 PVR*GRRESFSGRENLYMI-GR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
31-210 |
3.11e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.19 E-value: 3.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 31 FTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDlamHERARKgIGYLPQEASIFRKLTIAENimaiL 110
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRF-MAYLGHLPGLKADLSTLEN----L 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 111 ETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTL 190
Cdd:PRK13543 104 HFLCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAH 183
|
170 180
....*....|....*....|
gi 480205248 191 KDRGIGVLITDHNVRETLAI 210
Cdd:PRK13543 184 LRGGGAALVTTHGAYAAPPV 203
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
29-232 |
3.88e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.82 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 29 VSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKgIGYLPQEA-SIFRKLTIAENIM 107
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK-IGMVFQNPdNQFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 108 AILETrKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDII 187
Cdd:PRK13642 105 FGMEN-QGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 480205248 188 QTLKDR-GIGVLITDHNVRETlAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK13642 184 HEIKEKyQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-231 |
4.16e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 4.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 29 VSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMdKGEIHLDNLDLSDLAMhERARKGIGYLPQEASIFrKLTIAENIma 108
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDP-ESWRKHLSWVGQNPQLP-HGTLRDNV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 109 iLETRKDLNKQQRQQRL-----NELLSDFK--INH-IKD-SLGMSVsgGERRRAEIARALAADPKFMLLDEPFAGVDPIS 179
Cdd:PRK11174 444 -LLGNPDASDEQLQQALenawvSEFLPLLPqgLDTpIGDqAAGLSV--GQAQRLALARALLQPCQLLLLDEPTASLDAHS 520
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 480205248 180 VgdiKDIIQTLKD--RGIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK11174 521 E---QLVMQALNAasRRQTTLMVTHQL-EDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
28-243 |
5.61e-15 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.61 E-value: 5.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASIFRKLTIAENIM 107
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMDNMW 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 108 AILETRK----DLNKQQRQQR--LNELlsDFKINHIKDSLGMSVSggERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:PRK10982 96 LGRYPTKgmfvDQDKMYRDTKaiFDEL--DIDIDPRAKVATLSVS--QMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 182 DIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEgTPQEILDNEQVRKVYLG 243
Cdd:PRK10982 172 HLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIAT-QPLAGLTMDKIIAMMVG 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
23-170 |
7.74e-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: 73.32 E-value: 7.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTT------SFYMVvglvrmDKGEIHLDNLDLSDLAmHERARKGIGYLPQEASI 96
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTlarllfRFYDV------TSGRILIDGQDIRDVT-QASLRAAIGIVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 97 FRKlTIAENIM-----AileTRKDLNKQQRQQRlnelLSDFkINHIKDSL-------GMSVSGGERRRAEIARALAADPK 164
Cdd:COG5265 444 FND-TIAYNIAygrpdA---SEEEVEAAARAAQ----IHDF-IESLPDGYdtrvgerGLKLSGGEKQRVAIARTLLKNPP 514
|
....*.
gi 480205248 165 FMLLDE 170
Cdd:COG5265 515 ILIFDE 520
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
28-236 |
9.27e-15 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 73.02 E-value: 9.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASIFRKLTIAENIM 107
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAIIYQELHLVPEMTVAENLY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 108 -------AILETRKDLNKQQRQQrLNELLSDFKINHIKDSLgmsvSGGERRRAEIARALAADPKFMLLDEPFAGVDPISV 180
Cdd:PRK11288 102 lgqlphkGGIVNRRLLNYEAREQ-LEHLGVDIDPDTPLKYL----SIGQRQMVEIAKALARNARVIAFDEPTSSLSAREI 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 181 GDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:PRK11288 177 EQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVDRDQ 232
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
25-203 |
1.40e-14 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDL---AMHERARKGIGYLPQEASIFRKLT 101
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLdadALAQLRREHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENImAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:PRK10535 103 AAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180
....*....|....*....|..
gi 480205248 182 DIKDIIQTLKDRGIGVLITDHN 203
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTHD 203
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
26-231 |
1.54e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.70 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLV----RMDKGEIHLDNLDLSDLAMHERaRKGIGylPQEASIFRK-- 99
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKER-RNLVG--AEVAMIFQDpm 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 100 ------LTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGM---SVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK11022 100 tslnpcYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIADE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK11022 180 PTTALDVTIQAQIIELLLELQQKeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
10-176 |
1.91e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.80 E-value: 1.91e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 10 TLCIKHLAKNYS-KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamhERARKGIG 88
Cdd:PRK11650 3 GLKLQAVRKSYDgKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL---EPADRDIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAENIMAILETRKdLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLL 168
Cdd:PRK11650 80 MVFQNYALYPHMSVRENMAYGLKIRG-MPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLF 158
|
....*...
gi 480205248 169 DEPFAGVD 176
Cdd:PRK11650 159 DEPLSNLD 166
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
11-236 |
2.28e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 70.34 E-value: 2.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDN-----LDLSDLAMHER--- 82
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAERrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 83 ARKGIGYLPQEASIFRKLT------IAENIMAILETrkdlNKQQRQQRLNELLSDFKINHIK-DSLGMSVSGGERRRAEI 155
Cdd:PRK11701 87 LRTEWGFVHQHPRDGLRMQvsaggnIGERLMAVGAR----HYGDIRATAGDWLERVEIDAARiDDLPTTFSGGMQQRLQI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 156 ARALAADPKFMLLDEPFAGVDpISV-GDIKDIIQTL-KDRGIGVLITDHN--VRETLAicEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK11701 163 ARNLVTHPRLVFMDEPTGGLD-VSVqARLLDLLRGLvRELGLAVVIVTHDlaVARLLA--HRLLVMKQGRVVESGLTDQV 239
|
....*
gi 480205248 232 LDNEQ 236
Cdd:PRK11701 240 LDDPQ 244
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-243 |
2.92e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 70.58 E-value: 2.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnldlsDLAMHERA--------RKGIGYLPQ--EAS 95
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVD-----DITITHKTkdkyirpvRKRIGMVFQfpESQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 96 IFRKLTIAEnimaILETRKD--LNKQQRQQRLNELLSDFKINhiKDSLGMS---VSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK13646 98 LFEDTVERE----IIFGPKNfkMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 171 PFAGVDPISVGDIKDIIQTLK-DRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL-DNEQVRKVYLG 243
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFkDKKKLADWHIG 246
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-236 |
4.93e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.04 E-value: 4.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 19 NYSKRWV--VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEI-----HLDNLDLSDLamhERARKGIGYLP 91
Cdd:PRK10261 331 NRVTREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIifngqRIDTLSPGKL---QALRRDIQFIF 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QE--ASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLS--DFKINHIKdSLGMSVSGGERRRAEIARALAADPKFML 167
Cdd:PRK10261 408 QDpyASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLErvGLLPEHAW-RYPHEFSGGQRQRICIARALALNPKVII 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:PRK10261 487 ADEAVSALDVSIRGQIINLLLDLqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQ 556
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
14-205 |
1.10e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 68.27 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 14 KHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERAR---KGIGYL 90
Cdd:PRK10584 14 KSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKlraKHVGFV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKDLNKQQRQQRLnELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK10584 94 FQSFMLIPTLNALENVELPALLRGESSRQSRNGAK-ALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172
|
170 180 190
....*....|....*....|....*....|....*.
gi 480205248 171 PFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVR 205
Cdd:PRK10584 173 PTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQ 208
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-243 |
1.28e-13 |
|
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: 69.97 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 18 KNYSKRW------VVKDVSFTMQSGQIVGLLGPNGAGKTTsfyMVVGLVRMD---KGEIHLDNLDLSDLAMHErARKGIG 88
Cdd:TIGR00957 1288 RNYCLRYredldlVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFRINesaEGEIIIDGLNIAKIGLHD-LRFKIT 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKlTIAENIMAILE-TRKDLNKQQRQQRLNELLSDF--KINHIKDSLGMSVSGGERRRAEIARALAADPKF 165
Cdd:TIGR00957 1364 IIPQDPVLFSG-SLRMNLDPFSQySDEEVWWALELAHLKTFVSALpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 166 MLLDEPFAGVDPISVGDIKDIIQTLKDrGIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILdneQVRKVYLG 243
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFE-DCTVLTIAHRL-NTIMDYTRVIVLDKGEVAEFGAPSNLL---QQRGIFYS 1515
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
11-232 |
1.60e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 68.28 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKR--W-------VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE 81
Cdd:PRK15112 5 LEVRNLSKTFRYRtgWfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 82 RARKgIGYLPQEASifRKLTIAENIMAILET----RKDLNKQQRQQRLNELLSDFKI--NHIKDSLGMsVSGGERRRAEI 155
Cdd:PRK15112 85 RSQR-IRMIFQDPS--TSLNPRQRISQILDFplrlNTDLEPEQREKQIIETLRQVGLlpDHASYYPHM-LAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 156 ARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDR-GIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVL 238
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
8-226 |
1.61e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 69.52 E-value: 1.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 8 PQTLCikHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD--KGEIHLDNLDLSDLAMherarK 85
Cdd:PLN03211 68 KPKIS--DETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQIL-----K 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 86 GIGYLPQEASIFRKLTIAENIM--AILETRKDLNKQQRQQRLNELLSDFKINH-----IKDSLGMSVSGGERRRAEIARA 158
Cdd:PLN03211 141 RTGFVTQDDILYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHE 220
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 159 LAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHN-VRETLAICEKAYIVSEGSVIAEG 226
Cdd:PLN03211 221 MLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFG 289
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
25-235 |
1.95e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 69.38 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYLPQEASIFRKlTIAE 104
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMD-LRKVLGIIPQAPVLFSG-TVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIMAILEtRKDLNKQQRQQRLnellsdfkinHIKD-----SLGM---------SVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PLN03130 1332 NLDPFNE-HNDADLWESLERA----------HLKDvirrnSLGLdaevseageNFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 171 PFAGVDpisVGDIKDIIQTLKD--RGIGVLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:PLN03130 1401 ATAAVD---VRTDALIQKTIREefKSCTMLIIAHRL-NTIIDCDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-236 |
2.54e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 68.19 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHL---DNLDLSDLAMHErARKGIGYLPQE--ASIFRKL 100
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWRA-VRSDIQMIFQDplASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIMAILET-RKDLNKQQRQQRLNE------LLSDFkINHIKDSLgmsvSGGERRRAEIARALAADPKFMLLDEPFA 173
Cdd:PRK15079 116 TIGEIIAEPLRTyHPKLSRQEVKDRVKAmmlkvgLLPNL-INRYPHEF----SGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 174 GVDpISV-GDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:PRK15079 191 ALD-VSIqAQVVNLLQQLqREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
14-204 |
2.72e-13 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 66.82 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 14 KHLAKNY-SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERA--RKGIGYL 90
Cdd:PRK10908 5 EHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENImAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK10908 85 FQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190
....*....|....*....|....*....|....
gi 480205248 171 PFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNV 204
Cdd:PRK10908 164 PTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
28-231 |
3.22e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 67.46 E-value: 3.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE---RARKGIGYLPQ--EASIFRKlTI 102
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikQIRKKVGLVFQfpESQLFEE-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENImAILETRKDLNKQQRQQRLNELLSDFKINH-IKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:PRK13649 104 LKDV-AFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRK 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 480205248 182 DIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK13649 183 ELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-204 |
3.98e-13 |
|
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: 68.27 E-value: 3.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 32 TMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnLDLSdlamherarkgigYLPQEASIFRKLTIAENIMAILE 111
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-LKIS-------------YKPQYISPDYDGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 112 TRKDLNKQQrqqrlNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVD---PISVGD-IKDII 187
Cdd:COG1245 428 DDFGSSYYK-----TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKaIRRFA 502
|
170
....*....|....*..
gi 480205248 188 qtlKDRGIGVLITDHNV 204
Cdd:COG1245 503 ---ENRGKTAMVVDHDI 516
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
18-192 |
5.42e-13 |
|
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: 65.75 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 18 KNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD---KGEIHLDNLDLSDlaMHERARKGIGYLPQEA 94
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKE--FAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 95 SIFRKLTIAEnimaILETRKDLNKqqrqqrlNELLSdfkinhikdslgmSVSGGERRRAEIARALAADPKFMLLDEPFAG 174
Cdd:cd03233 93 VHFPTLTVRE----TLDFALRCKG-------NEFVR-------------GISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170
....*....|....*...
gi 480205248 175 VDPISVGDIKDIIQTLKD 192
Cdd:cd03233 149 LDSSTALEILKCIRTMAD 166
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
14-171 |
1.27e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 14 KHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLdnldlsdlamherarkG----IGY 89
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI----------------GetvkLAY 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQE-ASIFRKLTIAENIMAILETRKdLNKQQ----------------RQQRLNELlsdfkinhikdslgmsvSGGERRR 152
Cdd:PRK11819 392 VDQSrDALDPNKTVWEEISGGLDIIK-VGNREipsrayvgrfnfkggdQQKKVGVL-----------------SGGERNR 453
|
170
....*....|....*....
gi 480205248 153 AEIARALAADPKFMLLDEP 171
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEP 472
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-180 |
1.90e-12 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 66.11 E-value: 1.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNY-SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLvrmDK---GEIhldnldlsdlamheRARKGI- 87
Cdd:TIGR03719 7 MNRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKdfnGEA--------------RPQPGIk 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 88 -GYLPQEASIFRKLTIAENIM-AILETRKDLNK------------------QQRQQRLNELLS-------DFKINHIKDS 140
Cdd:TIGR03719 70 vGYLPQEPQLDPTKTVRENVEeGVAEIKDALDRfneisakyaepdadfdklAAEQAELQEIIDaadawdlDSQLEIAMDA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 480205248 141 LGM--------SVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISV 180
Cdd:TIGR03719 150 LRCppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESV 197
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
25-232 |
3.18e-12 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 65.50 E-value: 3.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE-RARKGIgyLPQEASIFRKlTIA 103
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAV--VSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 104 ENIMAileTRKDLNKQQRQQ--RLNELLSDfkINHIKDSL-------GMSVSGGERRRAEIARALAADPKFMLLDEPFAG 174
Cdd:PRK10789 407 NNIAL---GRPDATQQEIEHvaRLASVHDD--ILRLPQGYdtevgerGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 175 VDpisvGDIK-DIIQTLKDRGIG--VLITDHNVrETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK10789 482 VD----GRTEhQILHNLRQWGEGrtVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLA 537
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
26-231 |
5.18e-12 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 64.36 E-value: 5.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMD---KGEIHLDNLDLSDLAMHE----RARkgigylpQEASIFR 98
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLPEKElnklRAE-------QISMIFQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 99 K--------LTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGM---SVSGGERRRAEIARALAADPKFML 167
Cdd:PRK09473 105 DpmtslnpyMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTLKDR---GIgVLITdHNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREfntAI-IMIT-HDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
63-232 |
6.13e-12 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 65.05 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 63 DKGEIHLDNLDLSDLAMHErARKGIGYLPQEASIFrKLTIAENIMAILE--TRKDLNKQQRQQRLNELLSDF--KINHIK 138
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLF-NMSIYENIKFGKEdaTREDVKRACKFAAIDEFIESLpnKYDTNV 1352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 139 DSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVS 218
Cdd:PTZ00265 1353 GPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFN 1432
|
170
....*....|....*....
gi 480205248 219 E----GSVI-AEGTPQEIL 232
Cdd:PTZ00265 1433 NpdrtGSFVqAHGTHEELL 1451
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
11-205 |
7.01e-12 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 63.51 E-value: 7.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVG--LVRMDKGEIHLDNLDLSDLAMHERARKGIG 88
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQEASIFRKLTIAENIMAIletrkdLNKQQRQQRLNEL--LSDFK-INHIKDSLGMS-----------VSGGERRRAE 154
Cdd:CHL00131 88 LAFQYPIEIPGVSNADFLRLA------YNSKRKFQGLPELdpLEFLEiINEKLKLVGMDpsflsrnvnegFSGGEKKRNE 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 480205248 155 IARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVR 205
Cdd:CHL00131 162 ILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQR 212
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-231 |
8.90e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 63.34 E-value: 8.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIhldnldlsdlamheRARKGIGYLPQEASIFRKlTIAE 104
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------KHSGRISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIMAILETRKDLNKQQRQQ-RLNELLSDF--KINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVG 181
Cdd:cd03291 117 NIIFGVSYDEYRYKSVVKAcQLEEDITKFpeKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEK 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 480205248 182 DIKD-IIQTLKDRGIGVLITdhNVRETLAICEKAYIVSEGSVIAEGTPQEI 231
Cdd:cd03291 197 EIFEsCVCKLMANKTRILVT--SKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-236 |
9.24e-12 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 64.55 E-value: 9.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIhldnldlsdlamheRARKGIGYLPQEASIFRKlTIAE 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------------KHSGRISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NImaILETRKDLNKQQRQQRLNELLSDFKINHIKDSL-----GMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPIS 179
Cdd:TIGR01271 506 NI--IFGLSYDEYRYTSVIKACQLEEDIALFPEKDKTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVT 583
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 180 VGDI-KDIIQTLKDRGIGVLITDHnvRETLAICEKAYIVSEGSVIAEGTPQEiLDNEQ 236
Cdd:TIGR01271 584 EKEIfESCLCKLMSNKTRILVTSK--LEHLKKADKILLLHEGVCYFYGTFSE-LQAKR 638
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
23-225 |
1.02e-11 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.04 E-value: 1.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 23 RWVVKDVSFTMQSGQIVGLLGPNGAGKTtSFYMVV----------GLVRMDKGEIHLDNLDlsdlamheRA-RKGIGYLP 91
Cdd:NF040905 273 RKVVDDVSLNVRRGEIVGIAGLMGAGRT-ELAMSVfgrsygrnisGTVFKDGKEVDVSTVS--------DAiDAGLAYVT 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEasifRKL-------TIAENI-MAILE--TRKDLNKQQRQQRLNEllsDF--KINhIK----DSLGMSVSGGERRRAEI 155
Cdd:NF040905 344 ED----RKGyglnlidDIKRNItLANLGkvSRRGVIDENEEIKVAE---EYrkKMN-IKtpsvFQKVGNLSGGNQQKVVL 415
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 156 ARALAADPKFMLLDEPFAGVDpisVG---DIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAE 225
Cdd:NF040905 416 SKWLFTDPDVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
13-232 |
1.20e-11 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 63.97 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 13 IKHLAKNYSK-RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAmHERARKGIGYLP 91
Cdd:PRK10790 343 IDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 92 QEASIfrkltIAENIMAILETRKDLNKQQRQQ-----RLNELLSDFK--INHIKDSLGMSVSGGERRRAEIARALAADPK 164
Cdd:PRK10790 422 QDPVV-----LADTFLANVTLGRDISEEQVWQaletvQLAELARSLPdgLYTPLGEQGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 165 FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITdHNVrETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRL-STIVEADTILVLHRGQAVEQGTHQQLL 562
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
36-204 |
2.01e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 63.29 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 36 GQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnLDLSdlamherarkgigYLPQEASIFRKLTIAENIMAIletRKD 115
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS-------------YKPQYIKPDYDGTVEDLLRSI---TDD 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 116 LNKQQRQqrlNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVD---PISVGD-IKDIIqtlK 191
Cdd:PRK13409 428 LGSSYYK---SEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqRLAVAKaIRRIA---E 501
|
170
....*....|...
gi 480205248 192 DRGIGVLITDHNV 204
Cdd:PRK13409 502 EREATALVVDHDI 514
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
26-232 |
4.12e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.44 E-value: 4.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQE---ASIFRKLTI 102
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEErrsTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENIMaILETRKDLNKQQrqqrlneLLSDFKINH----IKDSLGM----------SVSGGERRRAEIARALAADPKFMLL 168
Cdd:PRK10982 344 GFNSL-ISNIRNYKNKVG-------LLDNSRMKSdtqwVIDSMRVktpghrtqigSLSGGNQQKVIIGRWLLTQPEILML 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 169 DEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSV-----IAEGTPQEIL 232
Cdd:PRK10982 416 DEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVagivdTKTTTQNEIL 484
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-236 |
4.96e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 62.18 E-value: 4.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNL-------------DLSDLAMHERARKGIGYLPQ 92
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMllrrrsrqvielsEQSAAQMRHVRGADMAMIFQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 93 E--ASIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGM---SVSGGERRRAEIARALAADPKFML 167
Cdd:PRK10261 112 EpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAVLI 191
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 168 LDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQ 236
Cdd:PRK10261 192 ADEPTTALDVTIQAQILQLIKVLqKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQ 261
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-202 |
7.20e-11 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 59.56 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 21 SKRWVVKDVSFTMQSGQIVGLLGPNGAGKTT-----SFYMVVGLVrmdKGEIHLDNLDLSdlamhERARKGIGYLPQEAS 95
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTTlldvlAGRKTAGVI---TGEILINGRPLD-----KNFQRSTGYVEQQDV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 96 IFRKLTIAENImailetrkdlnkqqrqqRLNELLSdfkinhikdslGMSVSggERRRAEIARALAADPKFMLLDEPFAGV 175
Cdd:cd03232 90 HSPNLTVREAL-----------------RFSALLR-----------GLSVE--QRKRLTIGVELAAKPSILFLDEPTSGL 139
|
170 180
....*....|....*....|....*..
gi 480205248 176 DPISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:cd03232 140 DSQAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
29-176 |
9.94e-11 |
|
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: 61.50 E-value: 9.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 29 VSFTMQSGQIVGLLGPNGAGKTTSFYMVVGlvRMDKGEIHLdnldlsdlamherARKG-IGYLPQEASIfRKLTIAENIM 107
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLA--EMDKVEGHV-------------HMKGsVAYVPQQAWI-QNDSLRENIL 720
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 108 aileTRKDLNKQQRQQRLNE--LLSDFKINHIKDSL-----GMSVSGGERRRAEIARALAADPKFMLLDEPFAGVD 176
Cdd:TIGR00957 721 ----FGKALNEKYYQQVLEAcaLLPDLEILPSGDRTeigekGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
11-241 |
1.50e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 59.84 E-value: 1.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL---------VRMdKGEIHLDNLDLSDLAMHE 81
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARV-TGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 82 RARKGiGYLPQEASIFRKLTIAENIMailetrkdLNKQQRQQRLNEL-------------LSDFKINHIKDSlgMSVSGG 148
Cdd:PRK13547 81 LARLR-AVLPQAAQPAFAFSAREIVL--------LGRYPHARRAGALthrdgeiawqalaLAGATALVGRDV--TTLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 149 ERRRAEIARALA---------ADPKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVS 218
Cdd:PRK13547 150 ELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLaRDWNLGVLAIVHDPNLAARHADRIAMLA 229
|
250 260
....*....|....*....|...
gi 480205248 219 EGSVIAEGTPQEILDNEQVRKVY 241
Cdd:PRK13547 230 DGAIVAHGAPADVLTPAHIARCY 252
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
31-171 |
7.98e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 58.42 E-value: 7.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 31 FTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNldlsDLAMherARkgigyLPQ------EASIFRklTIAE 104
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ----DLIV---AR-----LQQdpprnvEGTVYD--FVAE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIMAILETRK-------DLNKQQRQQRLNEL-------------LSDFKINHIKDSLGM-------SVSGGERRRAEIAR 157
Cdd:PRK11147 90 GIEEQAEYLKryhdishLVETDPSEKNLNELaklqeqldhhnlwQLENRINEVLAQLGLdpdaalsSLSGGWLRKAALGR 169
|
170
....*....|....
gi 480205248 158 ALAADPKFMLLDEP 171
Cdd:PRK11147 170 ALVSNPDVLLLDEP 183
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
25-208 |
8.74e-10 |
|
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: 56.01 E-value: 8.74e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHldnldlsdlaMHERArkGIGYLPQeASIFRKLTIAE 104
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG----------MPEGE--DLLFLPQ-RPYLPLGTLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NI----MAILetrkdlnkqqrqqrlnellsdfkinhikdslgmsvSGGERRRAEIARALAADPKFMLLDEPFAGVDPisv 180
Cdd:cd03223 83 QLiypwDDVL-----------------------------------SGGEQQRLAFARLLLHKPKFVFLDEATSALDE--- 124
|
170 180
....*....|....*....|....*....
gi 480205248 181 gDIKD-IIQTLKDRGIGVLITDHnvRETL 208
Cdd:cd03223 125 -ESEDrLYQLLKELGITVISVGH--RPSL 150
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
28-239 |
1.17e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.45 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGlvrmdkgeiHLDNLDLSDLAMheraRKGIGYLPQEASIFRKlTIAENIM 107
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLG---------ELSHAETSSVVI----RGSVAYVPQVSWIFNA-TVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 108 --AILETR---KDLNKQQRQQRLnELLSDFKINHIKDSlGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGD 182
Cdd:PLN03232 701 fgSDFESErywRAIDVTALQHDL-DLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQ 778
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 183 IKDiiQTLKDRGIG---VLITdhNVRETLAICEKAYIVSEGSVIAEGTPQEILDNEQVRK 239
Cdd:PLN03232 779 VFD--SCMKDELKGktrVLVT--NQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
22-225 |
1.19e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 56.51 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 22 KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTsfymvvgLVRMDKGeihldnldlsdlAMHERARKGIGYLPQEaSIFRKLT 101
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKST-------LLRLLAG------------ALKGTPVAGCVDVPDN-QFGREAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENIMailetrKDLNKQQRQQRLNEL-LSD-------FKinhikdslgmSVSGGERRRAEIARALAADPKFMLLDEPFA 173
Cdd:COG2401 102 LIDAIG------RKGDFKDAVELLNAVgLSDavlwlrrFK----------ELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 480205248 174 GVDPISVGDIKDIIQTL-KDRGIGVLITDH--NVRETLaICEKAYIVSEGSVIAE 225
Cdd:COG2401 166 HLDRQTAKRVARNLQKLaRRAGITLVVATHhyDVIDDL-QPDLLIFVGYGGVPEE 219
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
26-205 |
2.15e-09 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 55.80 E-value: 2.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSD---LAMHERARKGIGYLPQEASIFRKlTI 102
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEpsfEATRSRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENIMaileTRKDLNKQQRQQRLN--ELLSDFKINHIKDSL-----GMSVSGGERRRAEIARALAADPKFMLLDEPFAGV 175
Cdd:cd03290 96 EENIT----FGSPFNKQRYKAVTDacSLQPDIDLLPFGDQTeigerGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190
....*....|....*....|....*....|...
gi 480205248 176 DpISVGD---IKDIIQTLKDRGIGVLITDHNVR 205
Cdd:cd03290 172 D-IHLSDhlmQEGILKFLQDDKRTLVLVTHKLQ 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
22-171 |
2.69e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 57.05 E-value: 2.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 22 KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLvrmDK---GEIhldnldlsdlamheRARKG--IGYLPQEASI 96
Cdd:PRK11819 19 KKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKefeGEA--------------RPAPGikVGYLPQEPQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 97 FRKLTIAENIMAILETRKDLnkqqrQQRLNEL-------LSDF------------KINHIK------------DSLGM-- 143
Cdd:PRK11819 82 DPEKTVRENVEEGVAEVKAA-----LDRFNEIyaayaepDADFdalaaeqgelqeIIDAADawdldsqleiamDALRCpp 156
|
170 180 190
....*....|....*....|....*....|....
gi 480205248 144 ------SVSGGERRRAEIARALAADPKFMLLDEP 171
Cdd:PRK11819 157 wdakvtKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-171 |
3.39e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 3.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 9 QTLCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnldlsdlamhERARkgIG 88
Cdd:PRK15064 318 NALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWS----------ENAN--IG 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 YLPQE-ASIFRK-LTIAEnIMAILETRKDlNKQQRQQRLNELLsdFKINHIKDSLGmSVSGGERRRAEIARALAADPKFM 166
Cdd:PRK15064 386 YYAQDhAYDFENdLTLFD-WMSQWRQEGD-DEQAVRGTLGRLL--FSQDDIKKSVK-VLSGGEKGRMLFGKLMMQKPNVL 460
|
....*
gi 480205248 167 LLDEP 171
Cdd:PRK15064 461 VMDEP 465
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-234 |
3.52e-09 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.07 E-value: 3.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL------VRMDKgeIHLDNLDLSDLAMHERaRKGIG---------- 88
Cdd:COG4170 22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhVTADR--FRWNGIDLLKLSPRER-RKIIGreiamifqep 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 89 --YLPQEASIFRKLtiAENIMAILETRKDLN-KQQRQQRLNELLSDFKI---NHIKDSLGMSVSGGERRRAEIARALAAD 162
Cdd:COG4170 99 ssCLDPSAKIGDQL--IEAIPSWTFKGKWWQrFKWRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIANQ 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 163 PKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:COG4170 177 PRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
22-202 |
4.54e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 22 KRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGlvRMDKGEIHLDNLDLSDLAMHERARKGIGYLPQEASIFRKLT 101
Cdd:TIGR00956 775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRPLDSSFQRSIGYVQQQDLHLPTST 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 102 IAENIM--AILETRKDLNKQQRQQRLNELLSDFKINHIKDSL------GMSVSggERRRAEIARALAADPKFML-LDEPF 172
Cdd:TIGR00956 853 VRESLRfsAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpgeGLNVE--QRKRLTIGVELVAKPKLLLfLDEPT 930
|
170 180 190
....*....|....*....|....*....|
gi 480205248 173 AGVDPISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:TIGR00956 931 SGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
28-223 |
7.17e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTT------------SFymvvglvrmdKGEIHLDN--LDLSDLAMHEraRKGIGYLPQE 93
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTlmkvlsgvyphgSY----------EGEILFDGevCRFKDIRDSE--ALGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 94 ASIFRKLTIAENIMAILETRK----DLNKQQRQQRlnELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLD 169
Cdd:NF040905 87 LALIPYLSIAENIFLGNERAKrgviDWNETNRRAR--ELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 480205248 170 EPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVI 223
Cdd:NF040905 165 EPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
26-180 |
9.30e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 54.97 E-value: 9.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTsfymvvgLVRM-------DKGEIHLDNLDLSDLAMHERA--RKGIGYLPQE--A 94
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKST-------LARLltmietpTGGELYYQGQDLLKADPEAQKllRQKIQIVFQNpyG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 95 SIFRKLTIAENIMAILETRKDLNKQQRQQRLNELLSD--FKINHIKDSLGMsVSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:PRK11308 104 SLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKvgLRPEHYDRYPHM-FSGGQRQRIAIARALMLDPDVVVADEPV 182
|
....*...
gi 480205248 173 AGVDpISV 180
Cdd:PRK11308 183 SALD-VSV 189
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
7-176 |
1.25e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 55.11 E-value: 1.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 7 QPQTLCIKHL--AKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMV----VGLVRMDKGEIHLDNLDLSDLAMH 80
Cdd:TIGR00956 56 KILTRGFRKLkkFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGITPEEIKKH 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 81 ERARkgIGYLPQEASIFRKLTIAENI-----MAILETR-KDLNKQQRQQRLNEL-LSDFKINHIKDS-----LGMSVSGG 148
Cdd:TIGR00956 136 YRGD--VVYNAETDVHFPHLTVGETLdfaarCKTPQNRpDGVSREEYAKHIADVyMATYGLSHTRNTkvgndFVRGVSGG 213
|
170 180
....*....|....*....|....*...
gi 480205248 149 ERRRAEIARALAADPKFMLLDEPFAGVD 176
Cdd:TIGR00956 214 ERKRVSIAEASLGGAKIQCWDNATRGLD 241
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
11-205 |
1.32e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL--VRMDKGEIHLDNLDLSDLAMHERARKGI- 87
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 88 ---GYLPQEASIFRKLTIAENIMAILETRKdlnkQQRQQRLNelLSDF---KINHIK---DSLGMSV----SGGERRRAE 154
Cdd:PRK09580 82 mafQYPVEIPGVSNQFFLQTALNAVRSYRG----QEPLDRFD--FQDLmeeKIALLKmpeDLLTRSVnvgfSGGEKKRND 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 480205248 155 IARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVR 205
Cdd:PRK09580 156 ILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQR 206
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
25-191 |
1.88e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHL-DNLDLSDLAMhERARKGIGYLPQEASIFRKlTIA 103
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINL-KWWRSKIGVVSQDPLLFSN-SIK 477
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 104 ENIMAILETRKDL----------------NKQQRQQRLNELLSDFKI-----------------NHIKDSLGMSV----- 145
Cdd:PTZ00265 478 NNIKYSLYSLKDLealsnyynedgndsqeNKNKRNSCRAKCAGDLNDmsnttdsneliemrknyQTIKDSEVVDVskkvl 557
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 146 -----------------------SGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLK 191
Cdd:PTZ00265 558 ihdfvsalpdkyetlvgsnasklSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-203 |
1.98e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 1.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 34 QSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEiHLDNLDLSDLAMHERARKGIGYL-------------PQEASIFRKl 100
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFRGSELQNYFtkllegdvkvivkPQYVDLIPK- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAENIMAILETRKDLNKqqrqqrLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEpfagvdPISV 180
Cdd:cd03236 102 AVKGKVGELLKKKDERGK------LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDE------PSSY 169
|
170 180
....*....|....*....|....*....
gi 480205248 181 GDIKD------IIQTLKDRGIGVLITDHN 203
Cdd:cd03236 170 LDIKQrlnaarLIRELAEDDNYVLVVEHD 198
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-202 |
2.04e-08 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 2.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGlvRMDKGEIHLDnLDLSDLAMHERARKGI-GYLPQEASIFRKLTIA 103
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIEGD-IRISGFPKKQETFARIsGYCEQNDIHSPQVTVR 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 104 ENIM--AILETRKDLNKQQRQQRLNELLSDFKINHIKDSL-------GMSVSggERRRAEIARALAADPKFMLLDEPFAG 174
Cdd:PLN03140 972 ESLIysAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIvglpgvtGLSTE--QRKRLTIAVELVANPSIIFMDEPTSG 1049
|
170 180
....*....|....*....|....*...
gi 480205248 175 VDPISVGDIKDIIQTLKDRGIGVLITDH 202
Cdd:PLN03140 1050 LDARAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
25-232 |
3.21e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.27 E-value: 3.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLV----RMDKGEIHLDNLDLSDLAMHERaRKGIGY----------- 89
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRER-RKLVGHnvsmifqepqs 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 -LPQEASIFRKLtiaenIMAILE-TRKDLNKQQ---RQQRLNELLSDFKINHIKD---SLGMSVSGGERRRAEIARALAA 161
Cdd:PRK15093 101 cLDPSERVGRQL-----MQNIPGwTYKGRWWQRfgwRKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIALAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 480205248 162 DPKFMLLDEPFAGVDPISVGDIKDIIQTL-KDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK15093 176 QPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELV 247
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-232 |
3.51e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 3.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 30 SFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGE--------IHLDNLDLSDLAMHERARKGIGYL-PQEASIFRkl 100
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshiTRLSFEQLQKLVSDEWQRNNTDMLsPGEDDTGR-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 101 TIAEnimAILETRKDlnkqqrQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISV 180
Cdd:PRK10938 101 TTAE---IIQDEVKD------PARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 480205248 181 GDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK10938 172 QQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEIL 223
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
222-245 |
3.69e-08 |
|
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: 48.02 E-value: 3.69e-08
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
28-234 |
5.18e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 28 DVSFTMQSGQIVGLLGPNGAGKTTSFYMVVG-LVRMDKGEIHLdnldlsdlamheraRKGIGYLPQEASIFRKlTIAENI 106
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI--------------RGTVAYVPQVSWIFNA-TVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 107 MAILETrkDLNKQQRQQRLNELLSDFKINHIKD-----SLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPiSVG 181
Cdd:PLN03130 700 LFGSPF--DPERYERAIDVTALQHDLDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA-HVG 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 182 D------IKDIIQTlKDRgigVLITdhNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:PLN03130 777 RqvfdkcIKDELRG-KTR---VLVT--NQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-176 |
9.52e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 52.47 E-value: 9.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHldnldlsdlamherARKGIGYLPQEASIFRKlTIAE 104
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVW--------------AERSIAYVPQQAWIMNA-TVRG 739
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 480205248 105 NIMAILETRK-DLNKQQRQQRLN---ELLSDFKINHIKDSlGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVD 176
Cdd:PTZ00243 740 NILFFDEEDAaRLADAVRVSQLEadlAQLGGGLETEIGEK-GVNLSGGQKARVSLARAVYANRDVYLLDDPLSALD 814
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
85-231 |
1.63e-07 |
|
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: 51.55 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 85 KGIGYLPQEASIFRK-LTIAENI-MAILETRKDLNKQQRQQRLNELLSDFKINHIKdsLGMSV---SGGERRRAEIARAL 159
Cdd:TIGR00630 767 KGKRYNRETLEVKYKgKNIADVLdMTVEEAYEFFEAVPSISRKLQTLCDVGLGYIR--LGQPAttlSGGEAQRIKLAKEL 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 160 ---AADPKFMLLDEPFAGvdpISVGDIK---DIIQTLKDRGIGVLITDHNvretLAICEKA-YIV--------SEGSVIA 224
Cdd:TIGR00630 845 skrSTGRTLYILDEPTTG---LHFDDIKkllEVLQRLVDKGNTVVVIEHN----LDVIKTAdYIIdlgpeggdGGGTVVA 917
|
....*..
gi 480205248 225 EGTPQEI 231
Cdd:TIGR00630 918 SGTPEEV 924
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
25-208 |
2.15e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 51.29 E-value: 2.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 25 VVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnldlsdlamherARKGIGYLPQEASIFRKlTIAE 104
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------AKGKLFYVPQRPYMTLG-TLRD 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NI---MAILETRKdlnKQQRQQRLNELLSDFKINHI-KDSLGMS--------VSGGERRRAEIARALAADPKFMLLDEPF 172
Cdd:TIGR00954 534 QIiypDSSEDMKR---RGLSDKDLEQILDNVQLTHIlEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|....*..
gi 480205248 173 AGVDPisvgDIKD-IIQTLKDRGIGVLITDHnvRETL 208
Cdd:TIGR00954 611 SAVSV----DVEGyMYRLCREFGITLFSVSH--RKSL 641
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-234 |
5.96e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 50.21 E-value: 5.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 144 SVSGGERRRAEIARALAADPKFM--LLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVR------ETLAICEKAY 215
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQmisladRIIDIGPGAG 555
|
90
....*....|....*....
gi 480205248 216 IVSeGSVIAEGTPQEILDN 234
Cdd:PRK00635 556 IFG-GEVLFNGSPREFLAK 573
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
9-235 |
6.64e-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: 49.14 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 9 QTLCIKHlakNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHE-RARKGI 87
Cdd:cd03288 23 HDLCVRY---ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 88 gyLPQEASIFRKlTIAENImailetrkDLNKQQRQQRLNELLSDFKINHIKDSL-----------GMSVSGGERRRAEIA 156
Cdd:cd03288 100 --ILQDPILFSG-SIRFNL--------DPECKCTDDRLWEALEIAQLKNMVKSLpggldavvtegGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 157 RALAADPKFMLLDEPFAGVDPISVGDIKDIIQT-LKDRgiGVLITDHNVRETLAiCEKAYIVSEGSVIAEGTPQEILDNE 235
Cdd:cd03288 169 RAFVRKSSILIMDEATASIDMATENILQKVVMTaFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-205 |
6.90e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 49.70 E-value: 6.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSK----RWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGL-----VRMDKGEIHLDNLDLsdLAMHE 81
Cdd:PRK15134 6 LAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESL--LHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 82 RARKGI-GylPQEASIFRKLTIAENIMAILEtrKDLNK-------QQRQQRLNELLSDFK---INHIKDSLG---MSVSG 147
Cdd:PRK15134 84 QTLRGVrG--NKIAMIFQEPMVSLNPLHTLE--KQLYEvlslhrgMRREAARGEILNCLDrvgIRQAAKRLTdypHQLSG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 148 GERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQTLK-DRGIGVLITDHNVR 205
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQqELNMGLLFITHNLS 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-177 |
6.98e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 49.59 E-value: 6.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLAMHErARKGIGYLPQEASIFRKLTIAEN 105
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED-YRKLFSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 480205248 106 IMAILE-TRKDLNKQQRQQRLNelLSDFKINHIKdslgmsVSGGERRRAEIARALAADPKFMLLDEPFAGVDP 177
Cdd:PRK10522 418 KPANPAlVEKWLERLKMAHKLE--LEDGRISNLK------LSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-201 |
1.83e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 1.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 20 YSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGlvrmDKGEIHLDnldlsDLAMHERAR----------KGIGY 89
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DHPQGYSN-----DLTLFGRRRgsgetiwdikKHIGY 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 90 LPQEASI-FRKLTIAENIM--------AILETRKDLNKQQRQQRLNELLSDfkiNHIKDSLGMSVSGGERRRAEIARALA 160
Cdd:PRK10938 341 VSSSLHLdYRVSTSVRNVIlsgffdsiGIYQAVSDRQQKLAQQWLDILGID---KRTADAPFHSLSWGQQRLALIVRALV 417
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 480205248 161 ADPKFMLLDEPFAGVDPISvgdikdiiQTLKDRGIGVLITD 201
Cdd:PRK10938 418 KHPTLLILDEPLQGLDPLN--------RQLVRRFVDVLISE 450
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
24-234 |
1.84e-06 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 48.35 E-value: 1.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 24 WVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLdnldlsdlamherarKGIGYL-PQEASIFRKLTI 102
Cdd:PRK13545 38 YALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI---------------KGSAALiAISSGLNGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 103 AENImAILETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGD 182
Cdd:PRK13545 103 IENI-ELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 480205248 183 IKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEILDN 234
Cdd:PRK13545 182 CLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
5-209 |
7.42e-06 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 46.34 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 5 VQQPQTLCIKHLA-KNYSKRWVVKDVSFTMQSGQivGLL--GPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSdLAMHE 81
Cdd:COG4178 357 TSEDGALALEDLTlRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARV-LFLPQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 82 RArkgigYLPQEasifrklTIAEnimAIL--ETRKDLNKQQrqqrLNELLSDFKINHIKDSLGMSV------SGGERRRA 153
Cdd:COG4178 434 RP-----YLPLG-------TLRE---ALLypATAEAFSDAE----LREALEAVGLGHLAERLDEEAdwdqvlSLGEQQRL 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 480205248 154 EIARALAADPKFMLLDEPFAGVDPISVgdiKDIIQTLKDR--GIGVLITDHnvRETLA 209
Cdd:COG4178 495 AFARLLLHKPDWLFLDEATSALDEENE---AALYQLLREElpGTTVISVGH--RSTLA 547
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-171 |
9.06e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 46.32 E-value: 9.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 4 SVQQPQTL-----CIKHLAKNYSKRWVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHL-DNLDLSDL 77
Cdd:PRK10636 301 SFRAPESLpnpllKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLaKGIKLGYF 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 78 AMHErarkgIGYLPQEASIFRKLTiaenimailetrkDLNKQQRQQRLNELLSD--FKINHIKDSLGmSVSGGERRRAEI 155
Cdd:PRK10636 381 AQHQ-----LEFLRADESPLQHLA-------------RLAPQELEQKLRDYLGGfgFQGDKVTEETR-RFSGGEKARLVL 441
|
170
....*....|....*.
gi 480205248 156 ARALAADPKFMLLDEP 171
Cdd:PRK10636 442 ALIVWQRPNLLLLDEP 457
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
24-232 |
1.03e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 45.58 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 24 WVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNlDLSDLAMHerarkgigylpqeASIFRKLTIA 103
Cdd:PRK13546 38 FALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAIS-------------AGLSGQLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 104 ENI----MAILETRKDLNKQQRQQRLNELLSDFKINHIKdslgmSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPIS 179
Cdd:PRK13546 104 ENIefkmLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVK-----KYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 480205248 180 VGDIKDIIQTLKDRGIGVLITDHNVRETLAICEKAYIVSEGSVIAEGTPQEIL 232
Cdd:PRK13546 179 AQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
34-210 |
1.71e-05 |
|
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: 45.55 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 34 QSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIH--------LDNLDLSDLAMH-ERARKGigylpqEASIFRKLTIAE 104
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevLKRFRGTELQDYfKKLANG------EIKVAHKPQYVD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 105 NIMAIL--ETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFagvdpiSVGD 182
Cdd:COG1245 171 LIPKVFkgTVRELLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPS------SYLD 244
|
170 180 190
....*....|....*....|....*....|....
gi 480205248 183 IK------DIIQTLKDRGIGVLITDHNvretLAI 210
Cdd:COG1245 245 IYqrlnvaRLIRELAEEGKYVLVVEHD----LAI 274
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
85-228 |
1.87e-05 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 44.53 E-value: 1.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 85 KGIGYLPQEASI-FRKLTIAENI-MAILETRKDLNKQQRQQRLNELLSDFKINHIKdsLGMSV---SGGERRRAEIARAL 159
Cdd:cd03271 107 KGKRYNRETLEVrYKGKSIADVLdMTVEEALEFFENIPKIARKLQTLCDVGLGYIK--LGQPAttlSGGEAQRIKLAKEL 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 160 ---AADPKFMLLDEPFAGvdpISVGDIK---DIIQTLKDRGIGVLITDHNVrETLAICEkaYIVS--------EGSVIAE 225
Cdd:cd03271 185 skrSTGKTLYILDEPTTG---LHFHDVKkllEVLQRLVDKGNTVVVIEHNL-DVIKCAD--WIIDlgpeggdgGGQVVAS 258
|
...
gi 480205248 226 GTP 228
Cdd:cd03271 259 GTP 261
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
32-171 |
6.21e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 43.64 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 32 TMQSGQIVGLLGPNGAGKTTSfymvvglVRMDKGEIhLDNLdlsdlamherarkgiGYLPQEASI--------------- 96
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTA-------VKILSGEL-IPNL---------------GDYEEEPSWdevlkrfrgtelqny 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 97 FRKLtIAENIMAIL--------------ETRKDLNKQQRQQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAAD 162
Cdd:PRK13409 152 FKKL-YNGEIKVVHkpqyvdlipkvfkgKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRD 230
|
....*....
gi 480205248 163 PKFMLLDEP 171
Cdd:PRK13409 231 ADFYFFDEP 239
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
26-68 |
7.00e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 7.00e-05
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 480205248 26 VKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIH 68
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIH 377
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
144-220 |
7.70e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.92 E-value: 7.70e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 480205248 144 SVSGGERRRAEIARALAADPK--FMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVRetlAICEKAYIVSEG 220
Cdd:cd03238 87 TLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHNLD---VLSSADWIIDFG 162
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
11-170 |
1.11e-04 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 41.78 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 11 LCIKHLAKNYSKRwVVKDVSFTMQSGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDLSDLamherARKGIGYL 90
Cdd:PRK13541 2 LSLHQLQFNIEQK-NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-----AKPYCTYI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 91 PQEASIFRKLTIAENIMAILETRKDLnkqqrqQRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDE 170
Cdd:PRK13541 76 GHNLGLKLEMTVFENLKFWSEIYNSA------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
36-176 |
3.31e-04 |
|
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: 40.25 E-value: 3.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 36 GQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDnldlsdlamheraRKGIGYLPQEasifrkltiaenimailetrkd 115
Cdd:cd03222 25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-------------GITPVYKPQY---------------------- 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 480205248 116 lnkqqrqqrlnellsdfkinhikdslgMSVSGGERRRAEIARALAADPKFMLLDEPFAGVD 176
Cdd:cd03222 70 ---------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLD 103
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
144-232 |
4.10e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 144 SVSGGERRRAEIARALAA---DPKFMLLDEPFAGVDPISVGDIKDIIQTLKDRGIGVLITDHNVrETLAICEkaYIVS-- 218
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNM-HVVKVAD--YVLElg 885
|
90 100
....*....|....*....|
gi 480205248 219 ------EGSVIAEGTPQEIL 232
Cdd:PRK00635 886 peggnlGGYLLASCSPEELI 905
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
144-217 |
4.13e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.43 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 144 SVSGGERR------RAEIARALAADPKFMLLDEPFAGVDPISVGDIKDIIQ-TLKDRGI---GVLITDHnvRETLAICEK 213
Cdd:PRK01156 801 SLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEySLKDSSDipqVIMISHH--RELLSVADV 878
|
....
gi 480205248 214 AYIV 217
Cdd:PRK01156 879 AYEV 882
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
144-236 |
1.89e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 39.23 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 144 SVSGGERRRAEIARALAADPKFML--LDEPFAGVDPisvGDIKDIIQTLK---DRGIGVLITDHNvRETlaICEKAYIVS 218
Cdd:TIGR00630 488 TLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHQ---RDNRRLINTLKrlrDLGNTLIVVEHD-EDT--IRAADYVID 561
|
90 100
....*....|....*....|....*.
gi 480205248 219 --------EGSVIAEGTPQEILDNEQ 236
Cdd:TIGR00630 562 igpgagehGGEVVASGTPEEILANPD 587
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-208 |
5.09e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 36.58 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 35 SGQIVGLLGPNGAGKTTSFYMVVGLVRMDKGEIHLDNLDlsdlamherarkgigylpqeasifrkltiaenimailetrk 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGE----------------------------------------- 39
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 480205248 115 dlnkqqrqqRLNELLSDFKINHIKDSLGMSVSGGERRRAEIARALAADPKFMLLDEPFAGVDPISVGDIKDII------Q 188
Cdd:smart00382 40 ---------DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllL 110
|
170 180
....*....|....*....|
gi 480205248 189 TLKDRGIGVLITDHNVRETL 208
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLG 130
|
|
| |
