|
Name |
Accession |
Description |
Interval |
E-value |
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-241 |
0e+00 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 499.17 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGI 80
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNILAVLELRK-LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFIL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYLGHEFR 240
Cdd:COG1137 160 LDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGEDFR 239
|
.
gi 820872358 241 L 241
Cdd:COG1137 240 L 240
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
3-241 |
4.64e-165 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 455.20 E-value: 4.64e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGY 82
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYLGHEFRL 241
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQFRL 239
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-236 |
3.57e-153 |
|
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: 425.03 E-value: 3.57e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYL 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRG-LSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820872358 164 PFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYLG 236
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-241 |
3.47e-132 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 372.30 E-value: 3.47e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGI 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYLGHEFR 240
Cdd:PRK10895 161 LDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFR 240
|
.
gi 820872358 241 L 241
Cdd:PRK10895 241 L 241
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-238 |
4.62e-75 |
|
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: 228.00 E-value: 4.62e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGI 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIM-------------AILETRKELDREGR-RKELESLLQEFHISHIRDNLGMSLSGGERRRV 146
Cdd:COG0411 82 ARTFQNPRLFPELTVLENVLvaaharlgrgllaALLRLPRARREEREaRERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTIL 225
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
250
....*....|...
gi 820872358 226 ANELVKEVYLGHE 238
Cdd:COG0411 242 ADPRVIEAYLGEE 254
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-235 |
4.05e-72 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 219.94 E-value: 4.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARagIGYL 83
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYG-LPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 164 PFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELvKEVYL 235
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL-EDVFL 228
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-230 |
3.51e-70 |
|
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: 214.99 E-value: 3.51e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYL 83
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIM---------AILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALAT 154
Cdd:cd03219 81 FQIPRLFPELTVLENVMvaaqartgsGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELV 230
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
4.76e-69 |
|
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: 211.76 E-value: 4.76e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGI 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAILETRKelDREGRRKELESL------LQEFhishiRDNLGMSLSGGERRRVEIARALAT 154
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARR--DRAEVRADLERVyelfprLKER-----RRQRAGTLSGGEQQMLAIGRALMS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVY 234
Cdd:COG0410 154 RPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAY 233
|
..
gi 820872358 235 LG 236
Cdd:COG0410 234 LG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-227 |
2.02e-67 |
|
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: 207.29 E-value: 2.02e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYL 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKeldREGRRKELESLLQEFHISH-IRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARR---RAKRKARLERVYELFPRLKeRRKQLAGTLSGGEQQMLAIARALMSRPKLLLLD 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:cd03224 158 EPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-228 |
1.34e-64 |
|
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: 200.85 E-value: 1.34e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMhgRARAGIGYL 83
Cdd:COG4555 2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPR--EARRQIGVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKELDREgRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:COG4555 80 PDERGLYDRLTVRENIRYFAELYGLFDEE-LKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 164 PFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEI 223
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-215 |
1.31e-59 |
|
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: 185.68 E-value: 1.31e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMhgRARAGIGYL 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE--EVKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMailetrkeldregrrkelesllqefhishirdnlgmsLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03230 79 PEEPSLYENLTVRENLK-------------------------------------LSGGMKQRLALAQALLHDPELLILDE 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 820872358 164 PFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:cd03230 122 PTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-228 |
4.88e-57 |
|
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: 180.99 E-value: 4.88e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGY 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLR-ELRRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQ--EASIFRKlSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG1122 80 VFQnpDDQLFAP-TVEEDVAFGPENLG-LPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:COG1122 158 LDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
4-232 |
3.68e-56 |
|
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: 179.40 E-value: 3.68e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA--RAGIG 81
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:COG1127 86 MLFQGGALFDSLTVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILLY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA--NELVKE 232
Cdd:COG1127 166 DEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLAsdDPWVRQ 239
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-241 |
6.96e-55 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 177.61 E-value: 6.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNldvshQPMHGRARAGIGY 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDG-----EPLDPEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAiLETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVY-LARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTIlanelvKEVYLGHEFRL 241
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI------RRQFGRNTLRL 227
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-241 |
1.94e-54 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 174.89 E-value: 1.94e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVshqpmhGRARAGI 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFR--KLSVADNIMAILETRKELDREGRRKELE---SLLQEFHISHIRD-NLGmSLSGGERRRVEIARALAT 154
Cdd:COG1121 78 GYVPQRAEVDWdfPITVRDVVLMGRYGRRGLFRRPSRADREavdEALERVGLEDLADrPIG-ELSGGQQQRVLLARALAQ 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGqLIAEGDAQTILANELVKEVY 234
Cdd:COG1121 157 DPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPENLSRAY 235
|
....*..
gi 820872358 235 lGHEFRL 241
Cdd:COG1121 236 -GGPVAL 241
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
4-240 |
1.08e-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: 170.61 E-value: 1.08e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIGYL 83
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIM-------AILETRKELDREgrrkELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAP 156
Cdd:COG1120 81 PQEPPAPFGLTVRELVAlgryphlGLFGRPSAEDRE----AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 157 KFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYl 235
Cdd:COG1120 157 PLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY- 235
|
....*
gi 820872358 236 GHEFR 240
Cdd:COG1120 236 GVEAR 240
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-232 |
8.53e-52 |
|
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: 168.06 E-value: 8.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSH--QPMHGRARAGIGYLP 84
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlsEAELYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 85 QEASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 165 FAGVDPISVGDIKQIIHHLK-AKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA--NELVKE 232
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKkELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAsdDPLVRQ 234
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-219 |
2.30e-50 |
|
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213236 [Multi-domain] Cd Length: 210 Bit Score: 163.61 E-value: 2.30e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNldvshQPMHGRARAGIGYL 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG-----KPLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETrKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQL-KGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 164 PFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-219 |
5.88e-50 |
|
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: 162.30 E-value: 5.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGIGYL 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKELDREGRRKELEsLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRE-LLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 164 PFAGVDPIS----VGDIKQIIHHLkakGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03259 157 PLSALDAKLreelREELKELQREL---GITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-219 |
4.85e-49 |
|
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: 160.36 E-value: 4.85e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQ--VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgrARAGIG 81
Cdd:cd03263 1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADN--IMAILetrKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:cd03263 79 YCPQFDALFDELTVREHlrFYARL---KGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 160 LLDEPFAGVDPISVGDIKQIIHHLKaKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-219 |
8.53e-49 |
|
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: 159.62 E-value: 8.53e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 5 KAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVshqpmhGRARAGIGYLP 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL------EKERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 85 QEASIFRK--LSVADNIMAILETRKEL----DREGRRKELEsLLQEFHISHIRD-NLGmSLSGGERRRVEIARALATAPK 157
Cdd:cd03235 75 QRRSIDRDfpISVRDVVLMGLYGHKGLfrrlSKADKAKVDE-ALERVGLSELADrQIG-ELSGGQQQRVLLARALVQDPD 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 158 FILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNdGQLIAEG 219
Cdd:cd03235 153 LLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
8-214 |
1.13e-48 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 159.17 E-value: 1.13e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 8 HLAKSYKG--RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARaGIGYLPQ 85
Cdd:cd03225 4 NLSFSYPDgaRPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR-KVGLVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 86 --EASIFrKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03225 83 npDDQFF-GPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 820872358 164 PFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQ 214
Cdd:cd03225 161 PTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-224 |
8.14e-48 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 161.03 E-value: 8.14e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGI 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG3842 80 GMVFQDYALFPHLTVAENVAFGLRMRG-VPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 161 LDEPFAGVDP---ISV-GDIKQIihhLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:COG3842 159 LDEPLSALDAklrEEMrEELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEI 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
3-227 |
1.97e-47 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 159.93 E-value: 1.97e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDV-SHQPMHGRaraGIG 81
Cdd:COG1118 2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:COG1118 79 FVFQHYALFPHMTVAENIAFGLRVRP-PSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 162 DEPFAGVDPISVGDI-KQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG1118 158 DEPFGALDAKVRKELrRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
4-219 |
2.27e-47 |
|
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: 155.99 E-value: 2.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY----KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMhgRARAG 79
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPA--EARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQEASIFRKLSVADNI--MAILETRKELDREGRRKELESLLQefhISHIRDNLGMSLSGGERRRVEIARALATAPK 157
Cdd:cd03266 80 LGFVSDSTGLYDRLTARENLeyFAGLYGLKGDELTARLEELADRLG---MEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 158 FILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03266 157 VLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
7.95e-47 |
|
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: 161.99 E-value: 7.95e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGR-----QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA-- 76
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRel 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 RAGIGYLPQ--EASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHIS-HIRDNLGMSLSGGERRRVEIARALA 153
Cdd:COG1123 341 RRRVQMVFQdpYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPpDLADRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
4-220 |
1.43e-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: 1.43e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYL 83
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKEldreGRRKELESLLQEFHISH-IRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLAALPR----RSRKIPDEIYELFPVLKeMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKA-KGIGVLITDHNVRETLDICETAYIVNDGQLIAEGD 220
Cdd:TIGR03410 157 EPTEGIQPSIIKDIGRVIRRLRAeGGMAILLVEQYLDFARELADRYYVMERGRVVASGA 215
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-219 |
8.29e-46 |
|
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: 151.60 E-value: 8.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmhgRARAGIGYL 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNI---EALRRIGAL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAIletRKELDRegRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03268 78 IEAPGFYPNLTARENLRLL---ARLLGI--RKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 164 PFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-199 |
2.56e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 152.17 E-value: 2.56e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSY----KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVShqpmhgRA 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT------GP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 RAGIGYLPQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAP 156
Cdd:COG1116 79 GPDRGVVFQEPALLPWLTVLDNVALGLELRG-VPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 820872358 157 KFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRE 199
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDE 201
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-219 |
8.66e-45 |
|
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: 149.44 E-value: 8.66e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 6 AQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmhGRARAGIGYLPQ 85
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREP--REVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 86 EASIFRKLSVADNiMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:cd03265 81 DLSVDDELTGWEN-LYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 166 AGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-219 |
2.77e-44 |
|
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: 146.81 E-value: 2.77e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 5 KAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIGYLP 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 85 QeasifrklsvadnimailetrkeldregrrkelesLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd03214 80 Q-----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 165 FAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
2-195 |
3.90e-44 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 147.24 E-value: 3.90e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARagIG 81
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR--LA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMAILETRKeldREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:COG4133 79 YLGHADGLKPELTVRENLRFWAALYG---LRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190
....*....|....*....|....*....|....
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDH 195
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-166 |
3.99e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 145.48 E-value: 3.99e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYLPQEASIFRKLSVADN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERK-SLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 99 IMAILETrKELDREGRRKELESLLQEFHISHIRDNL----GMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:pfam00005 80 LRLGLLL-KGLSKREKDARAEEALEKLGLGDLADRPvgerPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-199 |
4.28e-44 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 147.62 E-value: 4.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQ----VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNldvshQPMHGRARAg 79
Cdd:cd03293 1 LEVRNVSKTYGGGGgavtALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG-----EPVTGPGPD- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQEASIFRKLSVADNIMAILETRKELDREgRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAE-ARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 820872358 160 LLDEPFAGVDPISVG----DIKQIIHHLKaKGIgVLITdHNVRE 199
Cdd:cd03293 154 LLDEPFSALDALTREqlqeELLDIWRETG-KTV-LLVT-HDIDE 194
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-214 |
8.97e-44 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 145.41 E-value: 8.97e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDV-SHQPMHGRARAGIGY 82
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtDLEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMailetrkeldregrrkelesllqefhishirdnlgMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03229 81 VFQDFALFPHLTVLENIA-----------------------------------LGLSGGQQQRVALARALAMDPDVLLLD 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQ 214
Cdd:cd03229 126 EPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-214 |
1.48e-43 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 144.31 E-value: 1.48e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 5 KAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYLP 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLE-ELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 85 QeasifrklsvadnimailetrkeldregrrkelesllqefhishirdnlgmsLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd00267 80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 820872358 165 FAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQ 214
Cdd:cd00267 108 TSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-218 |
2.57e-43 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 145.96 E-value: 2.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MAT-LKAQHLAKSYK----GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGR 75
Cdd:COG1136 1 MSPlLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 76 A---RAGIGYLPQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARAL 152
Cdd:COG1136 81 ArlrRRHIGFVFQFFNLLPELTALENVALPLLLAG-VSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 153 ATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNvRETLDICETAYIVNDGQLIAE 218
Cdd:COG1136 160 VNRPKLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRIVSD 225
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-226 |
7.46e-43 |
|
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: 145.33 E-value: 7.46e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY----KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAg 79
Cdd:COG1124 2 LEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQ--EASIFRKLSVADnimAILETRKELDREGRRKELESLLQEFHI-SHIRDNLGMSLSGGERRRVEIARALATAP 156
Cdd:COG1124 81 VQMVFQdpYASLHPRHTVDR---ILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 157 KFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLA 228
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
11-222 |
1.54e-42 |
|
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: 146.00 E-value: 1.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 11 KSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARagIGYLPQEASIF 90
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRS--IGIVPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLSVADNIMAILETRkELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDP 170
Cdd:TIGR01188 79 EDLTGRENLEMMGRLY-GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 820872358 171 ISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQ 222
Cdd:TIGR01188 158 RTRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPE 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-219 |
9.87e-42 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 141.18 E-value: 9.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGqIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARagIGYL 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVAD--NIMAILetrKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03264 78 PQEFGVYPNFTVREflDYIAWL---KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAKGIgVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03264 155 DEPTAGLDPEERIRFRNLLSELGEDRI-VILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-215 |
2.12e-41 |
|
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: 140.70 E-value: 2.12e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKG----RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA--- 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAafr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 RAGIGYLPQEASIFRKLSVADNIMAILETRKELDREgRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAP 156
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKE-RRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 157 KFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNvRETLDICETAYIVNDGQL 215
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
7.75e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 138.80 E-value: 7.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYL 83
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP-EWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKlSVADNIMAILETRKeldREGRRKELESLLQEFHISHirDNLGMS---LSGGERRRVEIARALATAPKFIL 160
Cdd:COG4619 80 PQEPALWGG-TVRDNLPFPFQLRE---RKFDRERALELLERLGLPP--DILDKPverLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
4-226 |
1.87e-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: 138.96 E-value: 1.87e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmhGRARAGIGYL 83
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAP--RAALARLGVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIM--AILETrkeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:TIGR03864 80 FQQPTLDLDLSVRQNLRyhAALHG---LSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVREtLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:TIGR03864 157 DEPTVGLDPASRAAITAHVRALARDqGLSVLWATHLVDE-IEASDRLVVLHRGRVLADGAAAELRG 221
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-232 |
2.14e-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: 2.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQ-VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGY 82
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAI--LETRKELDREGRRKELESLLqEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVpkLLKWPKEKIRERADELLALV-GLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHLKaKGIG---VLITdHNVRETLDICETAYIVNDGQLIAEGDAQTIL---ANELVKE 232
Cdd:cd03295 159 MDEPFGALDPITRDQLQEEFKRLQ-QELGktiVFVT-HDIDEAFRLADRIAIMKNGEIVQVGTPDEILrspANDFVAE 234
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
3-224 |
2.46e-40 |
|
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: 138.63 E-value: 2.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGIGY 82
Cdd:cd03296 2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAILETRKELDREGR---RKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:cd03296 79 VFQHYALFRHMTVFDNVAFGLRVKPRSERPPEaeiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 160 LLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:cd03296 159 LLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
4-196 |
2.19e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 135.57 E-value: 2.19e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYK-GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpMHGRA----RA 78
Cdd:COG2884 2 IRFENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSR--LKRREipylRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 79 GIGYLPQEASIFRKLSVADNIMAILETRkELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKF 158
Cdd:COG2884 80 RIGVVFQDFRLLPDRTVYENVALPLRVT-GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPEL 158
|
170 180 190
....*....|....*....|....*....|....*...
gi 820872358 159 ILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHN 196
Cdd:COG2884 159 LLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHD 196
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-234 |
3.51e-39 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 135.95 E-value: 3.51e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYK-GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG--RARAGI 80
Cdd:COG3638 3 LELRNLSKRYPgGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAiletrkelDREGRRKELESLLQEFHISHIR------DNLGMS---------LSGGERRR 145
Cdd:COG3638 83 GMIFQQFNLVPRLSVLTNVLA--------GRLGRTSTWRSLLGLFPPEDREralealERVGLAdkayqradqLSGGQQQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 146 VEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTi 224
Cdd:COG3638 155 VAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE- 233
|
250
....*....|
gi 820872358 225 LANELVKEVY 234
Cdd:COG3638 234 LTDAVLREIY 243
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-224 |
4.58e-39 |
|
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of fundamental importance in the cell physiology of bacteria because phosphate is required as a nutrient. The Pst system of E. coli comprises four distinct subunits encoded by the pstS, pstA, pstB, and pstC genes. The PstS protein is a phosphate-binding protein located in the periplasmic space. PstA and PstC are hydrophobic and they form the transmembrane portion of the Pst system. PstB is the catalytic subunit, which couples the energy of ATP hydrolysis to the import of phosphate across cellular membranes through the Pst system, often referred as ABC-protein. PstB belongs to one of the largest superfamilies of proteins characterized by a highly conserved adenosine triphosphate (ATP) binding cassette (ABC), which is also a nucleotide binding domain (NBD).
Pssm-ID: 213227 [Multi-domain] Cd Length: 227 Bit Score: 135.00 E-value: 4.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQA-----DQGRVLIDNLDVSHQPMHGRA-R 77
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 78 AGIGYLPQEASIFRKlSVADNIMAILETRKELDREGRRKELESLLQEFHIS-HIRDNL-GMSLSGGERRRVEIARALATA 155
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWdEVKDRLhALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 156 PKFILLDEPFAGVDPISVGDIKQIIHHLKAKgIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-231 |
5.85e-39 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 140.92 E-value: 5.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQ-PMHGRaRAGIGY 82
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRsPRDAQ-AAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAILETRKE--LDREGRRKELESLLQEFHIsHIR-DNLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRGglIDWRAMRRRARELLARLGL-DIDpDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 160 LLDEPFAgvdPISVGDIKQ---IIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVK 231
Cdd:COG1129 163 ILDEPTA---SLTEREVERlfrIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVR 234
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-234 |
6.15e-39 |
|
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: 135.00 E-value: 6.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYK-GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG--RARAGI 80
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAiletrkelDREGRRKELESLLQEFHISHIR------DNLGMS---------LSGGERRR 145
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLS--------GRLGRRSTWRSLFGLFPKEEKQralaalERVGLLdkayqradqLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 146 VEIARALATAPKFILLDEPFAGVDPISVgdiKQIIHHLKA----KGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDA 221
Cdd:cd03256 153 VAIARALMQQPKLILADEPVASLDPASS---RQVMDLLKRinreEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPP 229
|
250
....*....|...
gi 820872358 222 QTiLANELVKEVY 234
Cdd:cd03256 230 AE-LTDEVLDEIY 241
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-237 |
4.66e-38 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 132.93 E-value: 4.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYL 83
Cdd:COG4674 11 LYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKE--------LDREGRRKeLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATA 155
Cdd:COG4674 91 FQKPTVFEELTVFENLELALKGDRGvfaslfarLTAEERDR-IEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 156 PKFILLDEPFAGvdpISVGDIKQIIHHLK--AKGIGVLITDHN---VRetlDICETAYIVNDGQLIAEGDAQTILANELV 230
Cdd:COG4674 170 PKLLLLDEPVAG---MTDAETERTAELLKslAGKHSVVVVEHDmefVR---QIARKVTVLHQGSVLAEGSLDEVQADPRV 243
|
....*..
gi 820872358 231 KEVYLGH 237
Cdd:COG4674 244 IEVYLGR 250
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
8-169 |
5.24e-38 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 135.60 E-value: 5.24e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 8 HLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpMHGRARAgIGYLPQEA 87
Cdd:PRK10851 7 NIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR--LHARDRK-VGFVFQHY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 88 SIFRKLSVADNI---MAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK10851 84 ALFRHMTVFDNIafgLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEP 163
|
....*
gi 820872358 165 FAGVD 169
Cdd:PRK10851 164 FGALD 168
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-214 |
6.42e-38 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 130.20 E-value: 6.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGR--QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIG 81
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFrKLSVADNImailetrkeldregrrkelesllqefhishirdnlgmsLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI--------------------------------------LSGGQRQRIAIARALLRDPPILIL 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVrETLDICETAYIVNDGQ 214
Cdd:cd03228 121 DEATSALDPETEALILEALRALAKGKTVIVIA-HRL-STIRDADRIIVLDDGR 171
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
4-219 |
7.33e-38 |
|
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: 131.86 E-value: 7.33e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGR----QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSH--QPMHGRAR 77
Cdd:cd03257 2 LEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 78 AGIGYLPQEA--SIFRKLSVADNIMAILETRKELDREGRRKELESLLQEfHISHIRDNLGM---SLSGGERRRVEIARAL 152
Cdd:cd03257 82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLV-GVGLPEEVLNRyphELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 153 ATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-170 |
9.67e-38 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 134.82 E-value: 9.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGI 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRK-VPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170
....*....|
gi 820872358 161 LDEPFAGVDP 170
Cdd:COG3839 157 LDEPLSNLDA 166
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-238 |
1.68e-37 |
|
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: 131.30 E-value: 1.68e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVvRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGIGYL 83
Cdd:cd03299 1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKElDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKV-DKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 164 PFAGVDPISVG----DIKQIIHHLkakGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTIL---ANELVKEvYLG 236
Cdd:cd03299 156 PFSALDVRTKEklreELKKIRKEF---GVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFkkpKNEFVAE-FLG 231
|
..
gi 820872358 237 HE 238
Cdd:cd03299 232 FN 233
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-227 |
3.05e-37 |
|
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: 136.57 E-value: 3.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKG--RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD---QGRVLIDNLDVSHQPMHGRARA 78
Cdd:COG1123 5 LEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 79 gIGYLPQEA-SIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPK 157
Cdd:COG1123 85 -IGMVFQDPmTQLNPVTVGDQIAEALENLG-LSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 158 FILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-228 |
5.45e-37 |
|
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: 136.43 E-value: 5.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaRAGI 80
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFrKLSVADNimaILETRKELDREgrrkELESLLQEFHISHIRDNL-----------GMSLSGGERRRVEIA 149
Cdd:COG4988 414 AWVPQNPYLF-AGTIREN---LRLGRPDASDE----ELEAALEAAGLDEFVAALpdgldtplgegGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 150 RALATAPKFILLDEPFAGVDPISVGDIKQIIHHLkAKGIGVLITDHNVrETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRL-ALLAQADRILVLDDGRIVEQGTHEELLAKN 562
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
4-227 |
7.42e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 129.34 E-value: 7.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA-RAGIGY 82
Cdd:COG1126 2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlRRKVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:COG1126 82 VFQQFNLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLFD 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG1126 162 EPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-228 |
1.05e-36 |
|
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: 135.66 E-value: 1.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKG--RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmHGRARAG 79
Cdd:COG4987 332 PSLELEDVSFRYPGagRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLD-EDDLRRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQEASIFRKlSVADNI------------MAILEtRKELDR--EGRRKELESLLQEfhishirdnLGMSLSGGERRR 145
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLrlarpdatdeelWAALE-RVGLGDwlAALPDGLDTWLGE---------GGRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 146 VEIARALATAPKFILLDEPFAGVDPISVGDI-KQIIHHLKAKGIgVLITDHnvRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGRTV-LLITHR--LAGLERMDRILVLEDGRIVEQGTHEEL 556
|
....
gi 820872358 225 LANE 228
Cdd:COG4987 557 LAQN 560
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-218 |
4.01e-36 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 125.23 E-value: 4.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVS-HQPMHGRaRAGIGY 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDAR-RAGIAM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQeasifrklsvadnimailetrkeldregrrkelesllqefhishirdnlgmsLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03216 80 VYQ----------------------------------------------------LSVGERQMVEIARALARNARLLILD 107
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:cd03216 108 EPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-231 |
6.82e-36 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 132.46 E-value: 6.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVS-HQPMHGRArAGIGY 82
Cdd:COG3845 6 LELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIA-LGIGM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAILETRKE--LDREGRRKELESLLQEFHIS-----HIRDnlgmsLSGGERRRVEIARALATA 155
Cdd:COG3845 85 VHQHFMLVPNLTVAENIVLGLEPTKGgrLDRKAARARIRELSERYGLDvdpdaKVED-----LSVGEQQRVEILKALYRG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 156 PKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVK 231
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAE 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
15-228 |
1.57e-35 |
|
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: 133.04 E-value: 1.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaRAGIGYLPQEASIFRKlS 94
Cdd:COG2274 487 SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL-RRQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIMAileTRKELDREgrrkELESLLQEFHI------------SHIRDNlGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:COG2274 565 IRENITL---GDPDATDE----EIIEAARLAGLhdfiealpmgydTVVGEG-GSNLSGGQRQRLAIARALLRNPRILILD 636
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 163 EPFAGVDPISVgdiKQIIHHLK--AKGIGVLITDHNvRETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:COG2274 637 EATSALDAETE---AIILENLRrlLKGRTVIIIAHR-LSTIRLADRIIVLDKGRIVEDGTHEELLARK 700
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
3.66e-35 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 125.38 E-value: 3.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGI 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMA---ILETRKELDREGRRKELESLLQEFhishiRDNLGMSLSGGERRRVEIARALATAPK 157
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMggfFAERDQFQERIKWVYELFPRLHER-----RIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 158 FILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYLG 236
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-195 |
9.26e-35 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 123.41 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA-RAGIGY 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190
....*....|....*....|....*....|...
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDH 195
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH 193
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-236 |
1.19e-34 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 123.71 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 23 SLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGIGYLPQEASIFRKLSVADNIMAI 102
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 103 LETRKELDREGRRKeLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHH 182
Cdd:COG3840 96 LRPGLKLTAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDE 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 183 L-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEV--YLG 236
Cdd:COG3840 175 LcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALaaYLG 231
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-219 |
1.46e-34 |
|
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: 122.79 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSID---SGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDN--LDVSHQ----PMHGRaraGIGYLPQEASIFR 91
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvLFDSRKkinlPPQQR---KIGLVFQQYALFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KLSVADNIMAILetrKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPI 171
Cdd:cd03297 89 HLNVRENLAFGL---KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 820872358 172 SVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03297 166 LRLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-227 |
4.54e-34 |
|
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: 125.21 E-value: 4.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDN---LDVSHQ---PMHGRAragIGYLPQEASIFRKLS 94
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARGiflPPHRRR---IGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIMAileTRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:COG4148 94 VRGNLLY---GRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 175 DI----KQIIHHLkakGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG4148 171 EIlpylERLRDEL---DIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
16-228 |
1.01e-33 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 122.18 E-value: 1.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVshqPMHGR-----ARAGIGYLPQEASIF 90
Cdd:PRK11831 20 RCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENI---PAMSRsrlytVRKRMSMLFQSGALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDP 170
Cdd:PRK11831 97 TDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDP 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 171 ISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:PRK11831 177 ITMGVLVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANP 235
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-234 |
1.48e-33 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 119.94 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGL--VQADQGRVLIDNLDVSHQPMHGRARAGIG 81
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADnimailetrkeldregrrkelesllqefhisHIRdNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03217 81 LAFQYPPEIPGVKNAD-------------------------------FLR-YVNEGFSGGEKKRNEILQLLLLEPDLAIL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNvRETLD--ICETAYIVNDGQLIAEGDAQtiLANELVKEVY 234
Cdd:cd03217 129 DEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY-QRLLDyiKPDRVHVLYDGRIVKSGDKE--LALEIEKKGY 200
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
7-227 |
1.50e-33 |
|
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: 120.76 E-value: 1.50e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKGR----QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGR--ARAGI 80
Cdd:cd03258 5 KNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkARRRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAILETRKElDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:cd03258 85 GMIFQHFNLLSSRTVFENVALPLEIAGV-PKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:cd03258 164 CDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-169 |
1.79e-33 |
|
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: 120.05 E-value: 1.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGIGYL 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKELDREGRRKeLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDER-VREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
....*.
gi 820872358 164 PFAGVD 169
Cdd:cd03301 157 PLSNLD 162
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-234 |
8.25e-33 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 120.68 E-value: 8.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIg 81
Cdd:PRK13537 6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 yLPQEASIFRKLSVADNIMaILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:PRK13537 85 -VPQFDNLDPDFTVRENLL-VFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANEL---VKEVY 234
Cdd:PRK13537 163 DEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEIY 238
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
11-241 |
1.22e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 121.09 E-value: 1.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 11 KSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVshqPMHGR-ARAGIGYLPQEASI 89
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARlARARIGVVPQFDNL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 90 FRKLSVADNIMAI-----LETRKeldregRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK13536 126 DLEFTVRENLLVFgryfgMSTRE------IEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 165 FAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANEL---VKEVYLG--HEF 239
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIgcqVIEIYGGdpHEL 279
|
..
gi 820872358 240 RL 241
Cdd:PRK13536 280 SS 281
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-198 |
1.78e-32 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 117.76 E-value: 1.78e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 14 KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD---QGRVLIDNLDVSHQPMHGRaragIGYLPQEASIF 90
Cdd:cd03234 18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKC----VAYVRQDDILL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLSVADNI--MAILETRKELDREGRRKELE-SLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:cd03234 94 PGLTVRETLtyTAILRLPRKSSDAIRKKRVEdVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSG 173
|
170 180 190
....*....|....*....|....*....|.
gi 820872358 168 VDPISVGDIKQIIHHLKAKGIGVLITDHNVR 198
Cdd:cd03234 174 LDSFTALNLVSTLSQLARRNRIVILTIHQPR 204
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-234 |
2.17e-32 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 118.25 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGL--VQADQGRVLIDNLDVSHQPMHGRARAGIG 81
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YL---PQEasiFRKLSVADNIMAILETR--KELDREGRRKELESLLQEFHI--SHIRDNLGMSLSGGERRRVEIARALAT 154
Cdd:COG0396 81 LAfqyPVE---IPGVSVSNFLRTALNARrgEELSAREFLKLLKEKMKELGLdeDFLDRYVNEGFSGGEKKRNEILQMLLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVReTLDICE--TAYIVNDGQLIAEGDAQtiLANELVKE 232
Cdd:COG0396 158 EPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHYQR-ILDYIKpdFVHVLVDGRIVKSGGKE--LALELEEE 234
|
..
gi 820872358 233 VY 234
Cdd:COG0396 235 GY 236
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-226 |
2.75e-32 |
|
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: 120.60 E-value: 2.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDN--LDVSHQ----PMHGRAragIGYLPQEASIFRKLS 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtLFDSRKgiflPPEKRR---IGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNImaiLETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:TIGR02142 92 VRGNL---RYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 820872358 175 DIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:TIGR02142 169 EILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWA 221
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-238 |
4.82e-32 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 117.40 E-value: 4.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYL 83
Cdd:PRK11300 6 LSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIM-------------AILETRKEldregRRKELESL------LQEFHISHIRDNLGMSLSGGERR 144
Cdd:PRK11300 86 FQHVRLFREMTVIENLLvaqhqqlktglfsGLLKTPAF-----RRAESEALdraatwLERVGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 145 RVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQT 223
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240
|
250
....*....|....*
gi 820872358 224 ILANELVKEVYLGHE 238
Cdd:PRK11300 241 IRNNPDVIKAYLGEA 255
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-201 |
1.26e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 116.50 E-value: 1.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKG----RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDnldvsHQPMHGRA 76
Cdd:COG4525 1 MSMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLD-----GVPVTGPG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 rAGIGYLPQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAP 156
Cdd:COG4525 76 -ADRGVVFQKDALLPWLNVLDNVAFGLRLRG-VPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 820872358 157 KFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETL 201
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEAL 199
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-170 |
1.75e-31 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 114.89 E-value: 1.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD---QGRVLIDNLDVSHQPMHGRaraG 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR---R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQEASIFRKLSVADNIMaiLETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:COG4136 78 IGILFQDDLLFPHLSVGENLA--FALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155
|
170
....*....|.
gi 820872358 160 LLDEPFAGVDP 170
Cdd:COG4136 156 LLDEPFSKLDA 166
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-215 |
5.30e-31 |
|
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: 114.26 E-value: 5.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGIGYL 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKK-LPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 164 PFAGVD-----PISVgDIKQIIHHLkakGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:cd03300 157 PLGALDlklrkDMQL-ELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-234 |
1.30e-30 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 113.67 E-value: 1.30e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmhGRARAGI-GY 82
Cdd:COG4559 2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWS--PWELARRrAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADnIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALA-------TA 155
Cdd:COG4559 80 LPQHSSLAFPFTVEE-VVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGG 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 156 PKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVY 234
Cdd:COG4559 159 PRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-224 |
1.56e-30 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 116.09 E-value: 1.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRAragIGYL 83
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP---INMM 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK11607 97 FQSYALFPHMTVEQNIAFGLKQDK-LPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 164 PFAGVDP-------ISVGDIkqiihhLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:PRK11607 176 PMGALDKklrdrmqLEVVDI------LERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-228 |
1.85e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 113.93 E-value: 1.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKG--RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAG 79
Cdd:PRK13632 6 VMIKVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLK-EIRKK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQEA-SIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK13632 85 IGIIFQNPdNQFIGATVEDDIAFGLENKK-VPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 159 ILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLIT-DHNVRETLdICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNK 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
2-238 |
2.02e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.33 E-value: 2.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIG 81
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMAILETRKELDREGRRkELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALA------TA 155
Cdd:PRK13548 80 VLPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDA-LVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 156 PKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVY 234
Cdd:PRK13548 159 PRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
|
....
gi 820872358 235 lGHE 238
Cdd:PRK13548 239 -GAD 241
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-216 |
2.42e-30 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 111.58 E-value: 2.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 6 AQHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpmhGRARAGIGYLP 84
Cdd:cd03226 2 IENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA----KERRKSIGYVM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 85 QEAS--IFRKlSVADNImaiLETRKELDREGRRKEleSLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03226 78 QDVDyqLFTD-SVREEL---LLGLKELDAGNEQAE--TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLI 216
Cdd:cd03226 152 EPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-219 |
3.80e-30 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 112.04 E-value: 3.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 13 YKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIgYLPQEASIFRK 92
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGV-VFGQKTQLWWD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 LSVADN---IMAILETRKELDREgRRKELESLLQefhISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVD 169
Cdd:cd03267 110 LPVIDSfylLAAIYDLPPARFKK-RLDELSELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 820872358 170 PISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03267 186 VVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-218 |
4.23e-30 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 116.66 E-value: 4.23e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAksykGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYL 83
Cdd:COG1129 257 LEVEGLS----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIAYV 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 P---QEASIFRKLSVADNI-MAILE---TRKELDREGRRKELESLLQEFHI--SHIRDNLGmSLSGGERRRVEIARALAT 154
Cdd:COG1129 333 PedrKGEGLVLDLSIRENItLASLDrlsRGGLLDRRRERALAEEYIKRLRIktPSPEQPVG-NLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 155 APKFILLDEPFAGVDpisVG---DIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:COG1129 412 DPKVLILDEPTRGID---VGakaEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVGE 475
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-233 |
5.07e-30 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 114.02 E-value: 5.07e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKGR----QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG--RARAGI 80
Cdd:COG1135 5 ENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAARRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG1135 85 GMIFQHFNLLSSRTVAENVALPLEIAG-VPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 161 LDEPFAGVDPISVGDI----KQIIHHLkakGIG-VLITD--HNVREtldICETAYIVNDGQLIAEG-------DAQTILA 226
Cdd:COG1135 164 CDEATSALDPETTRSIldllKDINREL---GLTiVLITHemDVVRR---ICDRVAVLENGRIVEQGpvldvfaNPQSELT 237
|
....*..
gi 820872358 227 NELVKEV 233
Cdd:COG1135 238 RRFLPTV 244
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
5-234 |
8.51e-30 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 111.33 E-value: 8.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 5 KAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmhGRARAgigylp 84
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTP--SRELA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 85 qeasifRKLSV--ADNIMAILETRKELDREGR------------RKELESLLQEFHISHIRDNLGMSLSGGERRRVEIAR 150
Cdd:COG4604 75 ------KRLAIlrQENHINSRLTVRELVAFGRfpyskgrltaedREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAM 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 151 ALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHnvretlDI----CETAYIV--NDGQLIAEGDAQT 223
Cdd:COG4604 149 VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLH------DInfasCYADHIVamKDGRVVAQGTPEE 222
|
250
....*....|.
gi 820872358 224 ILANELVKEVY 234
Cdd:COG4604 223 IITPEVLSDIY 233
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
15-226 |
1.62e-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: 115.62 E-value: 1.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmhgRARAG--IGYLPQEASIFRK 92
Cdd:COG4618 344 KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REELGrhIGYLPQDVELFDG 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 lSVADNI----------------MA-----IL------ETRkeldregrrkelesllqefhishIRDNlGMSLSGGERRR 145
Cdd:COG4618 421 -TIAENIarfgdadpekvvaaakLAgvhemILrlpdgyDTR-----------------------IGEG-GARLSGGQRQR 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 146 VEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVReTLDICETAYIVNDGQLIAEGDAQTIL 225
Cdd:COG4618 476 IGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
|
.
gi 820872358 226 A 226
Cdd:COG4618 555 A 555
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
4-228 |
1.69e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 111.32 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQP---MHGRARAG 79
Cdd:PRK13639 2 LETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKkslLEVRKTVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQEASIFRKlSVADNImAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:PRK13639 82 IVFQNPDDQLFAP-TVEEDV-AFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 160 LLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDI 228
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
21-219 |
1.94e-29 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 109.50 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMhgrARAGIGYLPQEASIFRKLSVADNIM 100
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPP---ADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 101 AILETRKELdREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQII 180
Cdd:cd03298 93 LGLSPGLKL-TAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 820872358 181 HHLKA-KGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03298 172 LDLHAeTKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
12-219 |
3.55e-29 |
|
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: 109.22 E-value: 3.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQ--VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaRAGIGYLPQEASI 89
Cdd:cd03245 11 SYPNQEipALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 90 FrKLSVADNIM--AILETRKELDREGRRKELESLLQEfhisH-------IRDNlGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:cd03245 90 F-YGTLRDNITlgAPLADDERILRAAELAGVTDFVNK----HpngldlqIGER-GRGLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 161 LDEPFAGVDPISVgdiKQIIHHLKA--KGIGVLITDHNVReTLDICETAYIVNDGQLIAEG 219
Cdd:cd03245 164 LDEPTSAMDMNSE---ERLKERLRQllGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
15-215 |
4.69e-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: 107.52 E-value: 4.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYLP---QEASIFR 91
Cdd:cd03215 12 VKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPedrKREGLVL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KLSVADNIMailetrkeldregrrkelesllqefhishirdnLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPI 171
Cdd:cd03215 92 DLSVAENIA---------------------------------LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 820872358 172 SVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:cd03215 139 AKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-164 |
4.74e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 114.01 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 6 AQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNldvshqpmhgRARagIGYLPQ 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLR--IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 86 EASIFRKLSVADNIMAILETRKELDREGRR------------KELESLLQEFH----------ISHIRDNLGM------- 136
Cdd:COG0488 69 EPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlERLAELQEEFEalggweaearAEEILSGLGFpeedldr 148
|
170 180 190
....*....|....*....|....*....|.
gi 820872358 137 ---SLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:COG0488 149 pvsELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-164 |
5.90e-29 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 113.62 E-value: 5.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLI-DNLDvshqpmhgraragIGY 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLgETVK-------------IGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFR-KLSVADNImailetrKELDREGRRKELESLLQEF------HISHIRDnlgmsLSGGERRRVEIARALATA 155
Cdd:COG0488 383 FDQHQEELDpDKTVLDEL-------RDGAPGGTEQEVRGYLGRFlfsgddAFKPVGV-----LSGGEKARLALAKLLLSP 450
|
....*....
gi 820872358 156 PKFILLDEP 164
Cdd:COG0488 451 PNVLLLDEP 459
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-227 |
6.41e-29 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 109.07 E-value: 6.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDV------SHQPMHG 74
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 75 RA-RAGIGYLPQEASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALA 153
Cdd:PRK11264 81 RQlRQHVGFVFQNFNLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
18-215 |
8.14e-29 |
|
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: 106.92 E-value: 8.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 18 VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMhGRARAGIGYLPQEASIFrKLSVAD 97
Cdd:cd03246 17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDP-NELGDHVGYLPQDDELF-SGSIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 98 NImailetrkeldregrrkelesllqefhishirdnlgmsLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIK 177
Cdd:cd03246 95 NI--------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALN 136
|
170 180 190
....*....|....*....|....*....|....*...
gi 820872358 178 QIIHHLKAKGIGVLITDHNvRETLDICETAYIVNDGQL 215
Cdd:cd03246 137 QAIAALKAAGATRIVIAHR-PETLASADRILVLEDGRV 173
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
21-196 |
1.69e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 107.11 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpMHGRA----RAGIGYLPQEASIFRKLSVA 96
Cdd:cd03292 19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSD--LRGRAipylRRKIGVVFQDFRLLPDRNVY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 97 DNIMAILETRKELDREGRRKeLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDI 176
Cdd:cd03292 97 ENVAFALEVTGVPPREIRKR-VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180
....*....|....*....|
gi 820872358 177 KQIIHHLKAKGIGVLITDHN 196
Cdd:cd03292 176 MNLLKKINKAGTTVVVATHA 195
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
12-172 |
3.29e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 111.80 E-value: 3.29e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYLPQEASIF 90
Cdd:COG1132 348 SYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLE-SLRRQIGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 rKLSVADNI-MAiletRKELDREgrrkELESLLQEFHISHIRDNL-----------GMSLSGGERRRVEIARALATAPKF 158
Cdd:COG1132 427 -SGTIRENIrYG----RPDATDE----EVEEAAKAAQAHEFIEALpdgydtvvgerGVNLSGGQRQRIAIARALLKDPPI 497
|
170
....*....|....
gi 820872358 159 ILLDEPFAGVDPIS 172
Cdd:COG1132 498 LILDEATSALDTET 511
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
12-195 |
1.14e-27 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 104.24 E-value: 1.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVlidnldvshqpmHGRARAGIGYLPQEASIFR 91
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV------------RRAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KL--SVADNI-MAILETRKELDREGR--RKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:NF040873 69 SLplTVRDLVaMGRWARRGLWRRLTRddRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTT 148
|
170 180
....*....|....*....|....*....
gi 820872358 167 GVDPISVGDIKQIIHHLKAKGIGVLITDH 195
Cdd:NF040873 149 GLDAESRERIIALLAEEHARGATVVVVTH 177
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-226 |
1.26e-27 |
|
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: 109.89 E-value: 1.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKG--RQVVR---DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLI----DNLDVSHQPMHG 74
Cdd:TIGR03269 280 IKVRNVSKRYISvdRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDG 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 75 RARAG--IGYLPQEASIFRKLSVADNIM-AI-LETRKELdreGRRKELESL----LQEFHISHIRDNLGMSLSGGERRRV 146
Cdd:TIGR03269 360 RGRAKryIGILHQEYDLYPHRTVLDNLTeAIgLELPDEL---ARMKAVITLkmvgFDEEKAEEILDKYPDELSEGERHRV 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTIL 225
Cdd:TIGR03269 437 ALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIV 516
|
.
gi 820872358 226 A 226
Cdd:TIGR03269 517 E 517
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
12-195 |
1.45e-27 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 109.68 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGR-QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaRAGIGYLPQEASIF 90
Cdd:TIGR02857 330 AYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAWVPQHPFLF 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKlSVADNI-MAILE-TRKELDREGRRKELESLLQEF---HISHIRDNlGMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:TIGR02857 409 AG-TIAENIrLARPDaSDAEIREALERAGLDEFVAALpqgLDTPIGEG-GAGLSGGQAQRLALARAFLRDAPLLLLDEPT 486
|
170 180 190
....*....|....*....|....*....|
gi 820872358 166 AGVDPISVGDIKQIIHHLkAKGIGVLITDH 195
Cdd:TIGR02857 487 AHLDAETEAEVLEALRAL-AQGRTVLLVTH 515
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
3-234 |
1.76e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 105.48 E-value: 1.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIGY 82
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARR-LAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVadnimailetrKELDREGR--------------RKELESLLQEFHISHIRDNLGMSLSGGERRRVEI 148
Cdd:PRK11231 81 LPQHHLTPEGITV-----------RELVAYGRspwlslwgrlsaedNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 149 ARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:PRK11231 150 AMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPG 229
|
....*.
gi 820872358 229 LVKEVY 234
Cdd:PRK11231 230 LLRTVF 235
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-227 |
3.58e-27 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 104.73 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTT---CF---YMIVGLVQADqGRVLIDNLDVSHQ---PMHG 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLnrmNDLIPGARVE-GEILLDGEDIYDPdvdVVEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 75 RARagIGYLPQEASIFRKlSVADNIMAILETRKELDRegrrKEL----ESLLQEFHI-SHIRDNL---GMSLSGGERRRV 146
Cdd:COG1117 91 RRR--VGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSK----SELdeivEESLRKAALwDEVKDRLkksALGLSGGQQQRL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKgIGVLITDHNVRETLDICE-TAYIvNDGQLIAEGDAQTIL 225
Cdd:COG1117 164 CIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDyTAFF-YLGELVEFGPTEQIF 241
|
..
gi 820872358 226 AN 227
Cdd:COG1117 242 TN 243
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-230 |
4.67e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 108.21 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSH-QPMHGRArAGIGY 82
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQ-LGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAILETrkeldREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILD 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELV 230
Cdd:PRK15439 166 EPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
3-221 |
5.86e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 5.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDN--LDVSHQPMHGRARA-- 78
Cdd:COG4161 2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqFDFSQKPSEKAIRLlr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 79 -GIGYLPQEASIFRKLSVADN-IMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAP 156
Cdd:COG4161 82 qKVGMVFQQYNLWPHLTVMENlIEAPCKVLG-LSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 157 KFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDA 221
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA 225
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-218 |
6.54e-27 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 107.78 E-value: 6.54e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIG 81
Cdd:PRK10762 3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEAGIG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMailetrkeLDRE-----GR------RKELESLLQEFHISHIRDNLGMSLSGGERRRVEIAR 150
Cdd:PRK10762 83 IIHQELNLIPQLTIAENIF--------LGREfvnrfGRidwkkmYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 151 ALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:PRK10762 155 VLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
4-241 |
1.01e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYK-GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDN--LDVSHQPMHgRARAGI 80
Cdd:PRK13636 6 LKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGkpIDYSRKGLM-KLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQE-------ASIFRKLSVADNIMAILEtrKELdregrRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALA 153
Cdd:PRK13636 85 GMVFQDpdnqlfsASVYQDVSFGAVNLKLPE--DEV-----RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 154 TAPKFILLDEPFAGVDPISVGDI-KQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANelvKE 232
Cdd:PRK13636 158 MEPKVLVLDEPTAGLDPMGVSEImKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE---KE 234
|
....*....
gi 820872358 233 VYLGHEFRL 241
Cdd:PRK13636 235 MLRKVNLRL 243
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-234 |
1.94e-26 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 102.47 E-value: 1.94e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTcfymIVGLVQADQ---------------GRVLIDNLdvshqpmhgRA 76
Cdd:COG1119 12 RRGGKTILDDISWTVKPGEHWAILGPNGAGKST----LLSLITGDLpptygndvrlfgerrGGEDVWEL---------RK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 RagIGYLPQE--ASIFRKLSVADNIM----AILETRKELDREGRRKeLESLLQEFHISHIRDNLGMSLSGGERRRVEIAR 150
Cdd:COG1119 79 R--IGLVSPAlqLRFPRDETVLDVVLsgffDSIGLYREPTDEQRER-ARELLELLGLAHLADRPFGTLSQGEQRRVLIAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 151 ALATAPKFILLDEPFAGVDPISVGDIKQIIHHL---KAKGIgVLITdHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG1119 156 ALVKDPELLILDEPTAGLDLGARELLLALLDKLaaeGAPTL-VLVT-HHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTS 233
|
....*..
gi 820872358 228 ELVKEVY 234
Cdd:COG1119 234 ENLSEAF 240
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-235 |
2.38e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.96 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKG-RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG-RARA 78
Cdd:PRK13652 1 MHLIETRDLCYSYSGsKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 79 GIGYLPQEASIFRKLSVADniMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK13652 81 GLVFQNPDDQIFSPTVEQD--IAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 159 ILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI-LANELVKEVYL 235
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIfLQPDLLARVHL 237
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
16-236 |
2.44e-26 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 102.91 E-value: 2.44e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQP--MHGRARAGIGYLPQ--EASIFr 91
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKkkKLKDLRKKVGLVFQfpEHQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KLSVADNIM----AILETRKELDRegRRKEL-------ESLLQE--FHishirdnlgmsLSGGERRRVEIARALATAPKF 158
Cdd:TIGR04521 97 EETVYKDIAfgpkNLGLSEEEAEE--RVKEAlelvgldEEYLERspFE-----------LSGGQMRRVAIAGVLAMEPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 159 ILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN-ELVKEVYLG 236
Cdd:TIGR04521 164 LILDEPTAGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDvDELEKIGLD 243
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
3-222 |
3.18e-26 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 102.01 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDN--LDVSHQP--MHGRA-R 77
Cdd:PRK11124 2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhFDFSKTPsdKAIRElR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 78 AGIGYLPQEASIFRKLSVADNI----MAILEtrkeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALA 153
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLieapCRVLG----LSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQ 222
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
7-169 |
3.66e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 104.26 E-value: 3.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRAragIGYLPQE 86
Cdd:PRK09452 18 RGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---VNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 87 ASIFRKLSVADNIMAILETRKELDREGRRKELESL----LQEFHISHIRDnlgmsLSGGERRRVEIARALATAPKFILLD 162
Cdd:PRK09452 95 YALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALrmvqLEEFAQRKPHQ-----LSGGQQQRVAIARAVVNKPKVLLLD 169
|
....*..
gi 820872358 163 EPFAGVD 169
Cdd:PRK09452 170 ESLSALD 176
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
16-226 |
1.82e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 103.97 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSH--QPMHGRAragIGYLPQEASIFrKL 93
Cdd:TIGR01842 331 KPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwdRETFGKH---IGYLPQDVELF-PG 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 94 SVADNIMAI---LETRK--ELDREGRRKELESLLQEFHISHIRDNlGMSLSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:TIGR01842 407 TVAENIARFgenADPEKiiEAAKLAGVHELILRLPDGYDTVIGPG-GATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 169 DpiSVGDI--KQIIHHLKAKGIGVLITDHNVReTLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:TIGR01842 486 D--EEGEQalANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLA 542
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-222 |
1.83e-25 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 100.47 E-value: 1.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQ---GRVLIDNLDVSHQPMHGR----A 76
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKsagSHIELLGRTVQREGRLARdirkS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 RAGIGYLPQEASIFRKLSVADNIM--AILETR------KELDREGRRKELESLLQ--EFHISHIRDNlgmSLSGGERRRV 146
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLigALGSTPfwrtcfSWFTREQKQRALQALTRvgMVHFAHQRVS---TLSGGQQQRV 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQ 222
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQ 238
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
4-227 |
1.99e-25 |
|
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: 101.28 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGR----QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQA---DQGRVLIDNLDVSHqpMHGRA 76
Cdd:COG0444 2 LEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLK--LSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 R-----AGIGYLPQE--ASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGM---SLSGGERRRV 146
Cdd:COG0444 80 LrkirgREIQMIFQDpmTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRyphELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVL-ITdHN---VREtldICETAYIVNDGQLIAEGDA 221
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILfIT-HDlgvVAE---IADRVAVMYAGRIVEEGPV 235
|
....*.
gi 820872358 222 QTILAN 227
Cdd:COG0444 236 EELFEN 241
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-228 |
2.39e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 102.61 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgI 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-V 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNI-MAILETRKELDR--EGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPK 157
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVeMGRTPHRSRFDTwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 158 FILLDEPFAGVDpisvgdikqiIHH----------LKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK09536 160 VLLLDEPTASLD----------INHqvrtlelvrrLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTA 229
|
.
gi 820872358 228 E 228
Cdd:PRK09536 230 D 230
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
22-241 |
3.12e-25 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 99.53 E-value: 3.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 22 VSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAdQGRVLIDNLDVSHQPMHG--RARAgigYLPQEAS------IFRKL 93
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPG-QGEILLNGRPLSDWSAAElaRHRA---YLSQQQSppfampVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 94 SvadnimaiLETRKELDREGRRKELESLLQEFHIShirDNLG---MSLSGGERRRVEIARALAT-------APKFILLDE 163
Cdd:COG4138 91 A--------LHQPAGASSEAVEQLLAQLAEALGLE---DKLSrplTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 164 PFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYlGHEFRL 241
Cdd:COG4138 160 PMNSLDVAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF-GVKFRR 236
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-229 |
3.89e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.80 E-value: 3.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHL-AKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGY 82
Cdd:COG3845 258 LEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEasifRK-------LSVADNIMAILETRKE------LDREGRRKELESLLQEFHI--SHIRDNLGmSLSGGERRRVE 147
Cdd:COG3845 338 IPED----RLgrglvpdMSVAENLILGRYRRPPfsrggfLDRKAIRAFAEELIEEFDVrtPGPDTPAR-SLSGGNQQKVI 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATRE 492
|
..
gi 820872358 228 EL 229
Cdd:COG3845 493 EI 494
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
12-226 |
4.30e-25 |
|
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: 98.45 E-value: 4.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYLPQEASIF 90
Cdd:cd03254 11 SYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRK-SLRSMIGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKlSVADNI-MAILETRKEldregrrkELESLLQEFHISHIRDNL-----------GMSLSGGERRRVEIARALATAPKF 158
Cdd:cd03254 90 SG-TIMENIrLGRPNATDE--------EVIEAAKEAGAHDFIMKLpngydtvlgenGGNLSQGERQLLAIARAMLRDPKI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 159 ILLDEPFAGVDPISVGDIKQIIHHLKaKGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGDAQTILA 226
Cdd:cd03254 161 LILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-195 |
5.86e-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: 5.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKGRQ-VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVsHQPMHGRARAGI 80
Cdd:TIGR02868 333 PTLELRDLSAGYPGAPpVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPV-SSLDQDEVRRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKlSVADNIMAILE--TRKELDREGRRKELESLLQEfhishIRDNL-------GMSLSGGERRRVEIARA 151
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLARPdaTDEELWAALERVGLADWLRA-----LPDGLdtvlgegGARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 820872358 152 LATAPKFILLDEPFAGVDPisvGDIKQIIHHLKAKGIG---VLITDH 195
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDA---ETADELLEDLLAALSGrtvVLITHH 529
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-169 |
8.99e-25 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 98.23 E-value: 8.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNldvshQPMHGRArAGIGYL 83
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDG-----KPVEGPG-AERGVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLAG-VEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
....*.
gi 820872358 164 PFAGVD 169
Cdd:PRK11248 155 PFGALD 160
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-231 |
1.06e-24 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 101.78 E-value: 1.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYL 83
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNI-MAILETRKEL-----DREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPK 157
Cdd:PRK09700 86 YQELSVIDELTVLENLyIGRHLTKKVCgvniiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 158 FILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVK 231
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-227 |
1.24e-24 |
|
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: 98.48 E-value: 1.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmHGRARA----GIGYLPQEASIFRKLS 94
Cdd:cd03294 40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS-RKELRElrrkKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIMAILETRKELDREGRRKELESL----LQEFHISHIRDnlgmsLSGGERRRVEIARALATAPKFILLDEPFAGVDP 170
Cdd:cd03294 119 VLENVAFGLEVQGVPRAEREERAAEALelvgLEGWEHKYPDE-----LSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 171 ISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:cd03294 194 LIRREMQDELLRLQAElQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
4-198 |
1.47e-24 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 97.04 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGR----QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVShqPMHGRARAG 79
Cdd:TIGR02211 2 LKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLS--KLSSNERAK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 I-----GYLPQEASIFRKLSVADNIMAILETRKELDREGRRKELEsLLQEFHISHIRDNLGMSLSGGERRRVEIARALAT 154
Cdd:TIGR02211 80 LrnkklGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYE-MLEKVGLEHRINHRPSELSGGERQRVAIARALVN 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVR 198
Cdd:TIGR02211 159 QPSLVLADEPTGNLDNNNAKIIFDLMLELnRELNTSFLVVTHDLE 203
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
7-227 |
2.22e-24 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 97.09 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA-RAGIGYLPQ 85
Cdd:PRK09493 5 KNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 86 EASIFRKLSVADNIM-AILETRKELDREGRRKELEsLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK09493 85 QFYLFPHLTALENVMfGPLRVRGASKEEAEKQARE-LLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820872358 165 FAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK09493 164 TSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-199 |
2.53e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 97.55 E-value: 2.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTT---CFYMIVGLVQA--DQGRVLI--DNLDVSH-QPMHGR 75
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTilrCFNRLNDLIPGfrVEGKVTFhgKNLYAPDvDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 76 ARagIGYLPQEASIFRKlSVADNIM---AILETRKELDREGRRkeleSLLQEFHISHIRDNL---GMSLSGGERRRVEIA 149
Cdd:PRK14243 91 RR--IGMVFQKPNPFPK-SIYDNIAygaRINGYKGDMDELVER----SLRQAALWDEVKDKLkqsGLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 820872358 150 RALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVRE 199
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVT-HNMQQ 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
23-236 |
2.75e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.57 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 23 SLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMhgrARAGIGYLPQEASIFRKLSVADNIMAI 102
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPP---SRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 103 LETRKELDREGRRKeLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHH 182
Cdd:PRK10771 96 LNPGLKLNAAQREK-LHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 183 L-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYLG 236
Cdd:PRK10771 175 VcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASASALLG 229
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
7-224 |
2.88e-24 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 99.02 E-value: 2.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGIGYLPQE 86
Cdd:PRK11432 10 KNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DICMVFQS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 87 ASIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:PRK11432 87 YALFPHMSLGENVGYGLKMLG-VPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 167 GVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-234 |
4.97e-24 |
|
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: 96.18 E-value: 4.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVG--LVQADQGRVLIDNLDVSHQPMHGRARAGIg 81
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDERARAGL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YL----PQE-----ASIFrkLSVADNIMAILETRKELDREGRRKELESLLQ--EFHISHIRDNLGMSLSGGERRRVEIAR 150
Cdd:TIGR01978 80 FLafqyPEEipgvsNLEF--LRSALNARRSARGEEPLDLLDFEKLLKEKLAllDMDEEFLNRSVNEGFSGGEKKRNEILQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 151 ALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVReTLD--ICETAYIVNDGQLIAEGDAQtiLANE 228
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQR-LLNyiKPDYVHVLLDGRIVKSGDVE--LAKE 234
|
....*.
gi 820872358 229 LVKEVY 234
Cdd:TIGR01978 235 LEAKGY 240
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-236 |
5.73e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 96.27 E-value: 5.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQ------ADQGRVLIDNLDVsHQPMHGRARAGIGYLPQEASI 89
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDI-FQIDAIKLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 90 FRKLSVADNIMAILETRKELDREGRRKELESLLQEFHI-SHIRDNL---GMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 166 AGVDPISVGDIKQIIHHLKaKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA---NELVKEVYLG 236
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTspkNELTEKYVIG 254
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
13-235 |
8.30e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 96.23 E-value: 8.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 13 YKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNldvshQPMHGRARAGIGYLPQEASIFRK 92
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQG-----KPLDYSKRGLLALRQQVATVFQD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 -------LSVADNIMAILETRKELDREGRRKeLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK13638 86 peqqifyTDIDSDIAFSLRNLGVPEAEITRR-VDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPT 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 166 AGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA-NELVKEVYL 235
Cdd:PRK13638 165 AGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAMEQAGL 235
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
4-232 |
8.59e-24 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 95.61 E-value: 8.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA------R 77
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVYNGHNIYSPRtdtvdlR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 78 AGIGYLPQEASIFrKLSVADNIMAILETRKELDREGRRKELESLLQEFHI-SHIRDNL---GMSLSGGERRRVEIARALA 153
Cdd:PRK14239 86 KEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIwDEVKDRLhdsALGLSGGQQQRVCIARVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVRETLDICE-TAYIVnDGQLIAEGDAQTILANELVKE 232
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDrTGFFL-DGDLIEYNDTKQMFMNPKHKE 242
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-195 |
1.01e-23 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 94.48 E-value: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQpmHGRARAGIGYL 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ--RDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNImailetrKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03231 79 GHAPGIKTTLSVLENL-------RFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|...
gi 820872358 164 PFAGVDPISVGDIKQII-HHLKAKGIGVLITDH 195
Cdd:cd03231 152 PTTALDKAGVARFAEAMaGHCARGGMVVLTTHQ 184
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-224 |
1.18e-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: 98.74 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD--QGRVLIDNLDVSHQPMHGRARAGIG 81
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGtwDGEIYWSGSPLKASNIRDTERAGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMaileTRKELDREGRR-------KELESLLQEFHISHIRDNLG-MSLSGGERRRVEIARALA 153
Cdd:TIGR02633 82 IIHQELTLVPELSVAENIF----LGNEITLPGGRmaynamyLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALN 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
17-216 |
1.82e-23 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 93.63 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYLPQEASIFrklsva 96
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE-DLRSSLTIIPQDPTLF------ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 97 dniMAILetRKELDREGRRKElESLLQEFHIShirdNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDI 176
Cdd:cd03369 95 ---SGTI--RSNLDPFDEYSD-EEIYGALRVS----EGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 820872358 177 KQIIHHLkAKGIGVLITDHNVRETLDiCETAYIVNDGQLI 216
Cdd:cd03369 165 QKTIREE-FTNSTILTIAHRLRTIID-YDKILVMDAGEVK 202
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-219 |
2.66e-23 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 98.16 E-value: 2.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVshQPMHGRARAGIGYLPQEASIFRKLS 94
Cdd:TIGR01257 942 GRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI--ETNLDAVRQSLGMCPQHNILFHHLT 1019
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIM--AILETRKEldrEGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS 172
Cdd:TIGR01257 1020 VAEHILfyAQLKGRSW---EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 820872358 173 VGDIKQIIHHLKAkGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:TIGR01257 1097 RRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
12-201 |
2.71e-23 |
|
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: 93.00 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLV--QADQGRVLIDNldvshQPMHGRA-RAGIGYLPQEAS 88
Cdd:cd03213 18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRtgLGVSGEVLING-----RPLDKRSfRKIIGYVPQDDI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 89 IFRKLSVADNIMailetrkeldregrrkelesllqefHISHIRdnlgmSLSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:cd03213 93 LHPTLTVRETLM-------------------------FAAKLR-----GLSGGERKRVSIALELVSNPSLLFLDEPTSGL 142
|
170 180 190
....*....|....*....|....*....|...
gi 820872358 169 DPISVGDIKQIIHHLKAKGIGVLITDHNVRETL 201
Cdd:cd03213 143 DSSSALQVMSLLRRLADTGRTIICSIHQPSSEI 175
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
4-220 |
3.23e-23 |
|
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: 94.49 E-value: 3.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY--------KGR-QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSH-QPMH 73
Cdd:TIGR02769 3 LEVRDVTHTYrtgglfgaKQRaPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQlDRKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 74 GRA-RAGIGYLPQEA--SIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHI-SHIRDNLGMSLSGGERRRVEIA 149
Cdd:TIGR02769 83 RRAfRRDVQLVFQDSpsAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 150 RALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGD 220
Cdd:TIGR02769 163 RALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECD 234
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-195 |
3.88e-23 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 92.81 E-value: 3.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMH-GRARAGIGY 82
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEpHENILYLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPqeaSIFRKLSVADNIMAILEtrkelDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:TIGR01189 81 LP---GLKPELSALENLHFWAA-----IHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190
....*....|....*....|....*....|...
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDH 195
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-201 |
4.42e-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: 93.30 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVShQPMHGRAragigYLPQEASIFRKLSVADN 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT-EPGPDRM-----VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 99 I-MAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIK 177
Cdd:TIGR01184 75 IaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180
....*....|....*....|....*
gi 820872358 178 -QIIHHLKAKGIGVLITDHNVRETL 201
Cdd:TIGR01184 155 eELMQIWEEHRVTVLMVTHDVDEAL 179
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-233 |
5.19e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.80 E-value: 5.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQ--ADQGRVL-------------------- 61
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIyhvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 62 -------------IDNLDVShQPMHGRARAGIGYLPQEA-SIFRKLSVADNIMAILETRKELDREGRRKELEsLLQEFHI 127
Cdd:TIGR03269 81 pcpvcggtlepeeVDFWNLS-DKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVD-LIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 128 SHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDI-KQIIHHLKAKGIGVLITDHNVRETLDICET 206
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVhNALEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250 260
....*....|....*....|....*....
gi 820872358 207 AYIVNDGQLIAEGDAQTILAN--ELVKEV 233
Cdd:TIGR03269 239 AIWLENGEIKEEGTPDEVVAVfmEGVSEV 267
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-169 |
6.31e-23 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 95.48 E-value: 6.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaraGI 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNiMAI---LETRKELDREGRRKELESLLQefhISHIRDNLGMSLSGGERRRVEIARALATAPK 157
Cdd:PRK11000 78 GMVFQSYALYPHLSVAEN-MSFglkLAGAKKEEINQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170
....*....|..
gi 820872358 158 FILLDEPFAGVD 169
Cdd:PRK11000 154 VFLLDEPLSNLD 165
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-214 |
6.75e-23 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 90.59 E-value: 6.75e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDnldvshqpmhgrARAGIGYL 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKIGYF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQeasifrklsvadnimailetrkeldregrrkelesllqefhishirdnlgmsLSGGERRRVEIARALATAPKFILLDE 163
Cdd:cd03221 69 EQ----------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 820872358 164 PFAGVDPISvgdIKQIIHHLKAKGIGVLITDHNvRETLD-ICETAYIVNDGQ 214
Cdd:cd03221 97 PTNHLDLES---IEALEEALKEYPGTVILVSHD-RYFLDqVATKIIELEDGK 144
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
15-236 |
1.14e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 93.02 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGrvlidNLDVSHQPMHGRARAG-IGYLPQEASI---F 90
Cdd:PRK15056 19 GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASG-----KISILGQPTRQALQKNlVAYVPQSEEVdwsF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLsVADNIM-------AILETRKELDREGRRKELESL-LQEFHISHIRDnlgmsLSGGERRRVEIARALATAPKFILLD 162
Cdd:PRK15056 94 PVL-VEDVVMmgryghmGWLRRAKKRDRQIVTAALARVdMVEFRHRQIGE-----LSGGQKKRVFLARAIAQQGQVILLD 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNdGQLIAEGDAQTILANELVKEVYLG 236
Cdd:PRK15056 168 EPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK-GTVLASGPTETTFTAENLELAFSG 240
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-219 |
1.39e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 90.84 E-value: 1.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKG--RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpMHGRARAGIG 81
Cdd:cd03247 1 LSINNVSFSYPEqeQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD--LEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRklsvadnimailetrkeldregrrkelesllqefhiSHIRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03247 79 VLNQRPYLFD------------------------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIVLL 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 162 DEPFAGVDPISVGDI-KQIIHHLKAKGIgVLITDHNVreTLDICETAYIVNDGQLIAEG 219
Cdd:cd03247 123 DEPTVGLDPITERQLlSLIFEVLKDKTL-IWITHHLT--GIEHMDKILFLENGKIIMQG 178
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-223 |
1.45e-22 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 92.83 E-value: 1.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKG---------RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYAHgglsgkhqhQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 72 MHGRA--RAGIGYLPQEA--SIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHIS-HIRDNLGMSLSGGERRRV 146
Cdd:PRK10419 81 RAQRKafRRDIQMVFQDSisAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAE---GDAQ 222
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIVETqpvGDKL 240
|
.
gi 820872358 223 T 223
Cdd:PRK10419 241 T 241
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-164 |
3.31e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.87 E-value: 3.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY--------KGRQVVR---DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpM 72
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgRTVGVVKavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITG--L 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 73 HGRA----RAGIGYLPQE--ASIFRKLSVADNIMAILETRKELDREGRRKELESLLQ--------------EFhishird 132
Cdd:COG4608 86 SGRElrplRRRMQMVFQDpyASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLElvglrpehadryphEF------- 158
|
170 180 190
....*....|....*....|....*....|..
gi 820872358 133 nlgmslSGGERRRVEIARALATAPKFILLDEP 164
Cdd:COG4608 159 ------SGGQRQRIGIARALALNPKLIVCDEP 184
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-228 |
3.99e-22 |
|
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: 91.01 E-value: 3.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMhGRARAGIGYLPQEASIFRKlS 94
Cdd:cd03252 14 GPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADP-AWLRRQVGVVLQENVLFNR-S 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIMAileTRKELDREgRRKELESL--LQEFhISHIRDNL-------GMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:cd03252 92 IRDNIAL---ADPGMSME-RVIEAAKLagAHDF-ISELPEGYdtivgeqGAGLSGGQRQRIAIARALIHNPRILIFDEAT 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820872358 166 AGVDPISVGDIKQIIHHLKAkGIGVLITDHNVrETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:cd03252 167 SALDYESEHAIMRNMHDICA-GRTVIIIAHRL-STVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
13-235 |
5.83e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.34 E-value: 5.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 13 YK-GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG-RARAGIGYLPQEASIF 90
Cdd:PRK13647 14 YKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGLVFQDPDDQVF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 rKLSVADNImAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDP 170
Cdd:PRK13647 94 -SSTVWDDV-AFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDP 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 171 ISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYL 235
Cdd:PRK13647 172 RGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGL 236
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
20-215 |
9.24e-22 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.19 E-value: 9.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 20 RDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYLP---QEASIFRKLSVA 96
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrQSSGLYLDAPLA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 97 DNIMAILETRKE--LDREGRRKELESLLQEFHI--SHIRDNLGmSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS 172
Cdd:PRK15439 360 WNVCALTHNRRGfwIKPARENAVLERYRRALNIkfNHAEQAAR-TLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSA 438
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 820872358 173 VGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:PRK15439 439 RNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-232 |
9.36e-22 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 93.05 E-value: 9.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGI 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKLSVADNIM--AILETRKELDREGRRKELESLLQEfhishirdnLGM---------SLSGGERRRVEIA 149
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYlgQLPHKGGIVNRRLLNYEAREQLEH---------LGVdidpdtplkYLSIGQRQMVEIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 150 RALATAPKFILLDEPfagVDPISVGDIKQ---IIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK11288 153 KALARNARVIAFDEP---TSSLSAREIEQlfrVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVATFDDMAQVD 229
|
....*..
gi 820872358 227 NE-LVKE 232
Cdd:PRK11288 230 RDqLVQA 236
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
5-233 |
9.80e-22 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 91.79 E-value: 9.80e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 5 KAQHLAKSY--KGRQV--VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG--RARA 78
Cdd:PRK11153 3 ELKNISKVFpqGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 79 GIGYLPQEasiFRKLS---VADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATA 155
Cdd:PRK11153 83 QIGMIFQH---FNLLSsrtVFDNVALPLELAG-TPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 156 PKFILLDEPFAGVDPISVGDI----KQIIHHLkakGIG-VLITdHN---VREtldICETAYIVNDGQLIAEG-------D 220
Cdd:PRK11153 159 PKVLLCDEATSALDPATTRSIlellKDINREL---GLTiVLIT-HEmdvVKR---ICDRVAVIDAGRLVEQGtvsevfsH 231
|
250
....*....|...
gi 820872358 221 AQTILANELVKEV 233
Cdd:PRK11153 232 PKHPLTREFIQST 244
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-201 |
9.86e-22 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 89.80 E-value: 9.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MAT-LKAQHLAKSY-------KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDN----LDVS 68
Cdd:COG4778 1 MTTlLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 69 ----HQPMHGRARAgIGYLPQeasiFrkLSV-----ADNIMA--ILEtrKELDREGRRKELESLLQEFHI-SHIRDNLGM 136
Cdd:COG4778 81 qaspREILALRRRT-IGYVSQ----F--LRViprvsALDVVAepLLE--RGVDREEARARARELLARLNLpERLWDLPPA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 137 SLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVL-IT-DHNVRETL 201
Cdd:COG4778 152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIgIFhDEEVREAV 218
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-220 |
1.05e-21 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 91.30 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 13 YKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDvshqPMHGRARagigYLPQEASIF-R 91
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PFKRRKE----FARRIGVVFgQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 K------LSVADNimaiLETRKE---LDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:COG4586 104 RsqlwwdLPAIDS----FRLLKAiyrIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 163 EPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGD 220
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
4-169 |
1.10e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 89.80 E-value: 1.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGR----QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRAR-- 77
Cdd:COG4181 9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARlr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 78 -AGIGYLPQEASIFRKLSVADNIMAILETRKELDREGRRKELeslLQEFHISHIRDNLGMSLSGGERRRVEIARALATAP 156
Cdd:COG4181 89 aRHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARAL---LERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170
....*....|...
gi 820872358 157 KFILLDEPFAGVD 169
Cdd:COG4181 166 AILFADEPTGNLD 178
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-197 |
1.30e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 89.79 E-value: 1.30e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKA-QHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLidnldvsHQPmhgraRAG 79
Cdd:PRK09544 1 MTSLVSlENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNG-----KLR 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQEASIfrklsvaDNIMAILETRKELDREG-RRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK09544 69 IGYVPQKLYL-------DTTLPLTVNRFLRLRPGtKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 820872358 159 ILLDEPFAGVD---PISVGD-IKQIIHHLkakGIGVLITDHNV 197
Cdd:PRK09544 142 LVLDEPTQGVDvngQVALYDlIDQLRREL---DCAVLMVSHDL 181
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
14-226 |
1.37e-21 |
|
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: 89.60 E-value: 1.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 14 KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGrARAGIGYLPQEASIFRKl 93
Cdd:cd03251 13 DGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLAS-LRRQIGLVSQDVFLFND- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 94 SVADNIM--AILETRKELDREGRRKELESLLQEF---HISHIRDNlGMSLSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:cd03251 91 TVAENIAygRPGATREEVEEAARAANAHEFIMELpegYDTVIGER-GVKLSGGQRQRIAIARALLKDPPILILDEATSAL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 169 DPISVGDIKQIIHHLkAKGIGVLITDH---NVRETLDICetayIVNDGQLIAEGDAQTILA 226
Cdd:cd03251 170 DTESERLVQAALERL-MKNRTTFVIAHrlsTIENADRIV----VLEDGKIVERGTHEELLA 225
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
17-228 |
1.46e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 90.92 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRV--LIDNLDVSHQPMHG-------------------- 74
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKekvleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 75 ---RARAGIGYLPQEASIFrKLSVADNIM--AI-LETRKELDREGRRK--ELESLLQEFhishirdnLGMS---LSGGER 143
Cdd:PRK13651 101 keiRRRVGVVFQFAEYQLF-EQTIEKDIIfgPVsMGVSKEEAKKRAAKyiELVGLDESY--------LQRSpfeLSGGQK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 144 RRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQT 223
Cdd:PRK13651 172 RRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251
|
....*
gi 820872358 224 ILANE 228
Cdd:PRK13651 252 ILSDN 256
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-227 |
1.87e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 89.71 E-value: 1.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTcFYMIVGLVQADQGRVLID-NLDVSHQPMHGRaRAGIGY 82
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKST-FLKCLNRMNELESEVRVEgRVEFFNQNIYER-RVNLNR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEAS-IFRK-----LSVADNI---MAILETRKELDREGRrkeLESLLQEF----HISHIRDNLGMSLSGGERRRVEIA 149
Cdd:PRK14258 86 LRRQVSmVHPKpnlfpMSVYDNVaygVKIVGWRPKLEIDDI---VESALKDAdlwdEIKHKIHKSALDLSGGQQQRLCIA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 150 RALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKG-IGVLITDHNVRETLDICE-TAYIVND----GQLIAEGDAQT 223
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDfTAFFKGNenriGQLVEFGLTKK 242
|
....
gi 820872358 224 ILAN 227
Cdd:PRK14258 243 IFNS 246
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-234 |
2.85e-21 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 88.84 E-value: 2.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 22 VSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAdQGRVLIDNLDVSHQPMHGRARAGiGYLPQEAS------IFR--KL 93
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLPG-SGSIQFAGQPLEAWSAAELARHR-AYLSQQQTppfampVFQylTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 94 SVADNImAILETRKELDREGRRKELESLLqEFHISHirdnlgmsLSGGERRRVEIA-------RALATAPKFILLDEPFA 166
Cdd:PRK03695 93 HQPDKT-RTEAVASALNEVAEALGLDDKL-GRSVNQ--------LSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 167 GVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVY 234
Cdd:PRK03695 163 SLDVAQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
7-235 |
5.04e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 89.09 E-value: 5.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKG--RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLV---QADQGRVLIDNLDVSHQPMHG-RARAGI 80
Cdd:PRK13640 9 KHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDiREKVGI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASiFRKLSVADNIMAILETRkELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13640 89 VFQNPDNQ-FVGATVGDDVAFGLENR-AVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIII 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETlDICETAYIVNDGQLIAEGDAQTILAN-ELVKEVYL 235
Cdd:PRK13640 167 LDESTSMLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKvEMLKEIGL 242
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-224 |
5.22e-21 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 91.14 E-value: 5.22e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD--QGRVLIDNLDVSHQPMHGRARAGIG 81
Cdd:PRK13549 6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEELQASNIRDTERAGIA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMaileTRKELDREGR------RKELESLLQEFHIsHIRDNLG-MSLSGGERRRVEIARALAT 154
Cdd:PRK13549 86 IIHQELALVKELSVLENIF----LGNEITPGGImdydamYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEIAKALNK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:PRK13549 161 QARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGM 230
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-227 |
6.05e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.05 E-value: 6.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQ-----ADQGRVLIDNLDVSHQPM-HG 74
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypeaRVSGEVYLDGQDIFKMDViEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 75 RARAGIGY-LPQ---EASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEfhisHIRDNLGM---SLSGGERRRVE 147
Cdd:PRK14247 81 RRRVQMVFqIPNpipNLSIFENVALGLKLNRLVKSKKELQERVRWALEKAQLWD----EVKDRLDApagKLSGGQQQRLC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK14247 157 IARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVT-HFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
19-236 |
6.11e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.48 E-value: 6.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDV---SHQPMHGRARAGIGYLPQEASIFRKLSV 95
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIakiSDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 ADNIMAILETRKELDREGRRKELESLLQeFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGD 175
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQ-VGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 176 IKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTIL---ANELVKEVYLG 236
Cdd:PRK10070 203 MQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILnnpANDYVRTFFRG 267
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-227 |
1.02e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 88.23 E-value: 1.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCF------------YMIVGLVQADqGRVLIDNLDVshqp 71
Cdd:PRK14271 22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlnrmndkvsgYRYSGDVLLG-GRSIFNYRDV---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 72 MHGRARagIGYLPQEASIFrKLSVADNIMAILETRKELDREGRRKELESLLQEFHI-SHIRDNLGMS---LSGGERRRVE 147
Cdd:PRK14271 97 LEFRRR--VGMLFQRPNPF-PMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwDAVKDRLSDSpfrLSGGQQQLLC 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLkAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-215 |
3.58e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 86.27 E-value: 3.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpmhgrARAGIGYL 83
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAE------AREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILetrkeldREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGL-------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 820872358 164 PFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
15-196 |
3.85e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 84.93 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDvSHQPMHGRAragIGYLPQEASIFRKLS 94
Cdd:PRK13539 14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD-IDDPDVAEA---CHYLGHRNAMKPALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNimaiLETRKELdREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:PRK13539 90 VAEN----LEFWAAF-LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
|
170 180
....*....|....*....|...
gi 820872358 175 DIKQII-HHLKAKGIgVLITDHN 196
Cdd:PRK13539 165 LFAELIrAHLAQGGI-VIAATHI 186
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
17-228 |
4.06e-20 |
|
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: 85.67 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTcfymIVGLVQ----ADQGRVLIDNLDVSHQPMHGRaRAGIGYLPQEASIFrK 92
Cdd:cd03249 17 PILKGLSLTIPPGKTVALVGSSGCGKST----VVSLLErfydPTSGEILLDGVDIRDLNLRWL-RSQIGLVSQEPVLF-D 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 LSVADNIMAILETRKELDREGRRKE------LESLLQEFHiSHIRDNlGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:cd03249 91 GTIAENIRYGKPDATDEEVEEAAKKanihdfIMSLPDGYD-TLVGER-GSQLSGGQKQRIAIARALLRNPKILLLDEATS 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 167 GVDPISVGDIKQIIHHLkAKGIGVLITDHNVrETLDICETAYIVNDGQLIAEGDAQTILANE 228
Cdd:cd03249 169 ALDAESEKLVQEALDRA-MKGRTTIVIAHRL-STIRNADLIAVLQNGQVVEQGTHDELMAQK 228
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
13-227 |
5.88e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.66 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 13 YKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQ-----GRVLIDNLDVSHQPMHG-RARAGIGYLPQE 86
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDPiEVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 87 ASIFRKLSVADNIM------AILETRKELDREGRRKELESLLQEFHISHIRDNLGmSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK14267 94 PNPFPHLTIYDNVAigvklnGLVKSKKELDERVEWALKKAALWDEVKDRLNDYPS-NLSGGQRQRLVIARALAMKPKILL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK14267 173 MDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLGKLIEVGPTRKVFEN 238
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-234 |
1.08e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 85.04 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIG 81
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVadnimailetrKELDREGR----------RKELE----SLLQEFHISHIRDNLGMSLSGGERRRVE 147
Cdd:PRK10253 85 LLAQNATTPGDITV-----------QELVARGRyphqplftrwRKEDEeavtKAMQATGITHLADQSVDTLSGGQRQRAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK10253 154 IAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
|
....*...
gi 820872358 227 NELVKEVY 234
Cdd:PRK10253 234 AELIERIY 241
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-222 |
1.23e-19 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 86.98 E-value: 1.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVS-HQPMHGRArAGIGYLPQEasifRK----- 92
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVtRSPQDGLA-NGIVYISED----RKrdglv 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 --LSVADNiMAILETRK------ELDREGRRKELESLLQEFHI-SHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK10762 343 lgMSVKEN-MSLTALRYfsraggSLKHADEQQAVSDFIRLFNIkTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 164 PFAGVDpisVG---DIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQ 222
Cdd:PRK10762 422 PTRGVD---VGakkEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTRE 480
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
9-217 |
1.28e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 87.09 E-value: 1.28e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 9 LAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYLPQEAS 88
Cdd:PRK10982 4 ISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 89 IFRKLSVADNIMAILETRKEL--DREGRRKELESLLQEFHIS-HIRDNLGmSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK10982 84 LVLQRSVMDNMWLGRYPTKGMfvDQDKMYRDTKAIFDELDIDiDPRAKVA-TLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 820872358 166 AGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIA 217
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIA 214
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
12-228 |
1.53e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 86.80 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQ--VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPmHGRARAGIGYLPQEASI 89
Cdd:PRK11160 347 TYPDQPqpVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAALRQAISVVSQRVHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 90 FRKlSVADN--IMAILETRKELDREGRRKELESLLQEFHishiRDNL-----GMSLSGGERRRVEIARA-LATAPkFILL 161
Cdd:PRK11160 426 FSA-TLRDNllLAAPNASDEALIEVLQQVGLEKLLEDDK----GLNAwlgegGRQLSGGEQRRLGIARAlLHDAP-LLLL 499
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLkAKGIGVLITDHNVR--ETLD-ICetayIVNDGQLIAEGDAQTILANE 228
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLTglEQFDrIC----VMDNGQIIEQGTHQELLAQQ 564
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-231 |
2.42e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 84.30 E-value: 2.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKG--RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIG 81
Cdd:PRK13635 6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVW-DVRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEA-SIFRKLSVADNIMAILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13635 85 MVFQNPdNQFVGATVQDDVAFGLENIG-VPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIII 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHLKA-KGIGVLITDHnvretlDICETAY-----IVNDGQLIAEGDAQTI--LANELVK 231
Cdd:PRK13635 164 LDEATSMLDPRGRREVLETVRQLKEqKGITVLSITH------DLDEAAQadrviVMNKGEILEEGTPEEIfkSGHMLQE 236
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-195 |
2.52e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.54 E-value: 2.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQ-PMHGRARAGIGY 82
Cdd:PRK13538 2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrDEYHQDLLYLGH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPqeaSIFRKLSVADNIMAILETRKELDREGRRKELESL-LQEFhishiRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:PRK13538 82 QP---GIKTELTALENLRFYQRLHGPGDDEALWEALAQVgLAGF-----EDVPVRQLSAGQQRRVALARLWLTRAPLWIL 153
|
170 180 190
....*....|....*....|....*....|....*
gi 820872358 162 DEPFAGVDPISVGDIKQII-HHLKAKGIgVLITDH 195
Cdd:PRK13538 154 DEPFTAIDKQGVARLEALLaQHAEQGGM-VILTTH 187
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
21-169 |
2.94e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 84.93 E-value: 2.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQG------RVLIDnldvSHQ----PMHGRaraGIGYLPQEASIF 90
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGrivlngRVLFD----AEKgiclPPEKR---RIGYVFQDARLF 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLSVADNI---MAiletrkeldrEGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:PRK11144 89 PHYKVRGNLrygMA----------KSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
..
gi 820872358 168 VD 169
Cdd:PRK11144 159 LD 160
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-226 |
3.88e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 83.21 E-value: 3.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 11 KSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIdnldvshqpmHGRARA----GIGYLPQe 86
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEV----------NGRVSAllelGAGFHPE- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 87 asifrkLSVADNIM---AIL-ETRKELDRegRRKELEsllqEFhiSHIRDNLGM---SLSGGERRRVEIARALATAPKFI 159
Cdd:COG1134 103 ------LTGRENIYlngRLLgLSRKEIDE--KFDEIV----EF--AELGDFIDQpvkTYSSGMRARLAFAVATAVDPDIL 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820872358 160 LLDEpfagVdpISVGDI------KQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:COG1134 169 LVDE----V--LAVGDAafqkkcLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIA 235
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
4-222 |
3.91e-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: 86.22 E-value: 3.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQ--VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVG---LVQADQ---GRVLIDNLDVSHQPMhgr 75
Cdd:TIGR01257 1938 LRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdttVTSGDAtvaGKSILTNISDVHQNM--- 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 76 aragiGYLPQeasifrklsvADNIMAILETRKELDREGR-----RKELESL----LQEFHISHIRDNLGMSLSGGERRRV 146
Cdd:TIGR01257 2015 -----GYCPQ----------FDAIDDLLTGREHLYLYARlrgvpAEEIEKVanwsIQSLGLSLYADRLAGTYSGGNKRKL 2079
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQ 222
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
15-219 |
3.98e-19 |
|
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: 83.05 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGrARAGIGYLPQEASIFRKlS 94
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS-LRRAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNImailetrkeldREGR----RKELESLLQEFHISHIRDNL-----------GMSLSGGERRRVEIARALATAPKFI 159
Cdd:cd03253 91 IGYNI-----------RYGRpdatDEEVIEAAKAAQIHDKIMRFpdgydtivgerGLKLSGGEKQRVAIARAILKNPPIL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 160 LLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVRETLDiCETAYIVNDGQLIAEG 219
Cdd:cd03253 160 LLDEATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-236 |
5.55e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 83.56 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPM---HGRARAGIGYLPQEASIFRKlSVAD 97
Cdd:PRK13637 25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVklsDIRKKVGLVFQYPEYQLFEE-TIEK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 98 NIMAILETRKELDREGRRKELESL-LQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDI 176
Cdd:PRK13637 104 DIAFGPINLGLSEEEIENRVKRAMnIVGLDYEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEI 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 177 KQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN-ELVKEVYLG 236
Cdd:PRK13637 184 LNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEvETLESIGLA 245
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-183 |
8.59e-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: 84.79 E-value: 8.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYK-GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGY 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRH-TLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKlSVADNIM-------AILETRKELDREGRRKELESLLQEFHISHIRDnlGMSLSGGERRRVEIARALATA 155
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLlgakenvSQDEIWAACEIAEIKDDIENMPLGYQTELSEE--GSSISGGQKQRIALARALLTD 629
|
170 180
....*....|....*....|....*...
gi 820872358 156 PKFILLDEPFAGVDPISVgdiKQIIHHL 183
Cdd:TIGR01193 630 SKVLILDESTSNLDTITE---KKIVNNL 654
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-227 |
1.04e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 82.32 E-value: 1.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVS--------------H 69
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 70 QPMHGRARAGIGYlpQEASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISH-IRDNLGMSLSGGERRRVEI 148
Cdd:PRK10619 86 QLRLLRTRLTMVF--QHFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSI 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 149 ARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK10619 164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-219 |
2.09e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.09 E-value: 2.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG-----RARAGIGYLPQEASIFRKLSV 95
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvRKKVGVVFQFPESQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 ADNIMAILE---TRKELDREGRRK-ELESLLQEFHishirDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPI 171
Cdd:PRK13643 104 KDVAFGPQNfgiPKEKAEKIAAEKlEMVGLADEFW-----EKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPK 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 820872358 172 SVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:PRK13643 179 ARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-224 |
2.32e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 81.34 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYLPQE------ASIFrKLS 94
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE-KLRKHIGIVFQNpdnqfvGSIV-KYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIMAILETRKELDREgrrkeLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:PRK13648 105 VAFGLENHAVPYDEMHRR-----VSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQ 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 820872358 175 DIKQIIHHLKA-KGIGVLITDHNVRETLdicETAYIV--NDGQLIAEGDAQTI 224
Cdd:PRK13648 180 NLLDLVRKVKSeHNITIISITHDLSEAM---EADHVIvmNKGTVYKEGTPTEI 229
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
18-182 |
2.96e-18 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 80.23 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 18 VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYLPQEASIFRKlSVad 97
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLH-DLRSRISIIPQDPVLFSG-TI-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 98 nimailetRKELDREGRR--KELESLLQEFHI-SHIRDNLGM----------SLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:cd03244 95 --------RSNLDPFGEYsdEELWQALERVGLkEFVESLPGGldtvveeggeNLSVGQRQLLCLARALLRKSKILVLDEA 166
|
170
....*....|....*...
gi 820872358 165 FAGVDPISVGDIKQIIHH 182
Cdd:cd03244 167 TASVDPETDALIQKTIRE 184
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
2-234 |
3.14e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.99 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIG 81
Cdd:PRK10575 10 TTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARK-VA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEasifrkLSVADNImaileTRKELDREGR--------------RKELESLLQEFHISHIRDNLGMSLSGGERRRVE 147
Cdd:PRK10575 89 YLPQQ------LPAAEGM-----TVRELVAIGRypwhgalgrfgaadREKVEEAISLVGLKPLAHRLVDSLSGGERQRAW 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK10575 158 IAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMR 237
|
....*...
gi 820872358 227 NELVKEVY 234
Cdd:PRK10575 238 GETLEQIY 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
7-228 |
4.12e-18 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 82.85 E-value: 4.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKGR---QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVS---HQPMHGRaragI 80
Cdd:TIGR00958 482 QDVSFSYPNRpdvPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVqydHHYLHRQ----V 557
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKlSVADNIMAILeTRKElDREGRRKELESLLQEFhISHIRDNL-------GMSLSGGERRRVEIARALA 153
Cdd:TIGR00958 558 ALVGQEPVLFSG-SVRENIAYGL-TDTP-DEEIMAAAKAANAHDF-IMEFPNGYdtevgekGSQLSGGQKQRIAIARALV 633
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 154 TAPKFILLDEPFAGVDpisvGDIKQIIHHLK-AKGIGVLITDHNvretLDICETA---YIVNDGQLIAEGDAQTILANE 228
Cdd:TIGR00958 634 RKPRVLILDEATSALD----AECEQLLQESRsRASRTVLLIAHR----LSTVERAdqiLVLKKGSVVEMGTHKQLMEDQ 704
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
10-218 |
4.24e-18 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 82.65 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 10 AKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYLPQ---E 86
Cdd:PRK11288 260 LDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMLCPEdrkA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 87 ASIFRKLSVADNImAILETRKELdREG----RRKELEslLQEFHISHI------RDNLGMSLSGGERRRVEIARALATAP 156
Cdd:PRK11288 340 EGIIPVHSVADNI-NISARRHHL-RAGclinNRWEAE--NADRFIRSLniktpsREQLIMNLSGGNQQKAILGRWLSEDM 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 157 KFILLDEPFAGVDpisVG---DIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:PRK11288 416 KVILLDEPTRGID---VGakhEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
4-181 |
7.49e-18 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 79.44 E-value: 7.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGR---QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVShQPMHGRARAGI 80
Cdd:cd03248 12 VKFQNVTFAYPTRpdtLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHKYLHSKV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEASIFRKlSVADNIMAILETrkeldregrrKELESLLQEFHISHIRDNL--------------GMSLSGGERRRV 146
Cdd:cd03248 91 SLVGQEPVLFAR-SLQDNIAYGLQS----------CSFECVKEAAQKAHAHSFIselasgydtevgekGSQLSGGQKQRV 159
|
170 180 190
....*....|....*....|....*....|....*
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIH 181
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALY 194
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
4-228 |
7.55e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 80.66 E-value: 7.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQ-----VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDnlDVSHQPMHGRARA 78
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVG--DIYIGDKKNNHEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 79 GIGYLPQEASIFRKL------------------SVADNIM---AILETRKELDREGRRKELESL-LQEFHIShiRDNLGm 136
Cdd:PRK13631 100 ITNPYSKKIKNFKELrrrvsmvfqfpeyqlfkdTIEKDIMfgpVALGVKKSEAKKLAKFYLNKMgLDDSYLE--RSPFG- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 137 sLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLI 216
Cdd:PRK13631 177 -LSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
|
250
....*....|..
gi 820872358 217 AEGDAQTILANE 228
Cdd:PRK13631 256 KTGTPYEIFTDQ 267
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
16-195 |
7.88e-18 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 82.02 E-value: 7.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD---QGRVLIDNLDVSHQPMHGRAragiGYLPQEASIFRK 92
Cdd:TIGR00955 38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAIS----AYVQQDDLFIPT 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 LSVAD--NIMAILETRKELDREGRRKELESLLQEFHISHIRD------NLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:TIGR00955 114 LTVREhlMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASELLTDPPLLFCDEP 193
|
170 180 190
....*....|....*....|....*....|.
gi 820872358 165 FAGVDPISVGDIKQIIHHLKAKGIGVLITDH 195
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
4-199 |
1.25e-17 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 78.60 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgRARAGIGYL 83
Cdd:PRK10247 8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE-IYRQQVSYC 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKlSVADNIMAILETRKELDREgrrKELESLLQEFHI-SHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:PRK10247 87 AQTPTLFGD-TVYDNLIFPWQIRNQQPDP---AIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLD 162
|
170 180 190
....*....|....*....|....*....|....*...
gi 820872358 163 EPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRE 199
Cdd:PRK10247 163 EITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDE 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
18-235 |
1.56e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 79.36 E-value: 1.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 18 VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQP--MHGRARAGIgylpqeasIFRKlsv 95
Cdd:PRK13633 25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlWDIRNKAGM--------VFQN--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 ADN--IMAILETRKE-------LDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:PRK13633 94 PDNqiVATIVEEDVAfgpenlgIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTA 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 167 GVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDiCETAYIVNDGQLIAEGDAQTILAN-ELVKEVYL 235
Cdd:PRK13633 174 MLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKEvEMMKKIGL 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-164 |
1.68e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 81.13 E-value: 1.68e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLI-DNLDVSHQpmhGRARAGigy 82
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKLAYV---DQSRDA--- 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASIFRKLSVADNIMAI----LETRKELDREGrrkelesllqeFHISHIRDNLGMsLSGGERRRVEIARALATAPKF 158
Cdd:TIGR03719 397 LDPNKTVWEEISGGLDIIKLgkreIPSRAYVGRFN-----------FKGSDQQKKVGQ-LSGGERNRVHLAKTLKSGGNV 464
|
....*.
gi 820872358 159 ILLDEP 164
Cdd:TIGR03719 465 LLLDEP 470
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-197 |
2.03e-17 |
|
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: 78.60 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 25 SIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVShqpmhgraragigYLPQEASIFRKLSVADNIMAIle 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-------------YKPQYIKADYEGTVRDLLSSI-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 105 trkeLDREGRRKELES-LLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDP----ISVGDIKQI 179
Cdd:cd03237 86 ----TKDFYTHPYFKTeIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVeqrlMASKVIRRF 161
|
170
....*....|....*...
gi 820872358 180 IHHLKAkgiGVLITDHNV 197
Cdd:cd03237 162 AENNEK---TAFVVEHDI 176
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
4-236 |
2.23e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 78.88 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGY 82
Cdd:PRK13644 2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQEASI-FRKLSVADNI--------MAILETRKELDREgrrkeleslLQEFHISHIRDNLGMSLSGGERRRVEIARALA 153
Cdd:PRK13644 82 VFQNPETqFVGRTVEEDLafgpenlcLPPIEIRKRVDRA---------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVREtLDICETAYIVNDGQLIAEGDAQTILANELVKev 233
Cdd:PRK13644 153 MEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ-- 229
|
...
gi 820872358 234 YLG 236
Cdd:PRK13644 230 TLG 232
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
15-215 |
2.56e-17 |
|
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: 78.74 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADqGRVLIDNLDVSHQPMHgRARAGIGYLPQEASIFRKls 94
Cdd:cd03289 16 GNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQ-KWRKAFGVIPQKVFIFSG-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 vadnimailETRKELDREGRRKE-----------LESLLQEF--HISHIRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:cd03289 92 ---------TFRKNLDPYGKWSDeeiwkvaeevgLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLL 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAkGIGVLITDHNVRETLDiCETAYIVNDGQL 215
Cdd:cd03289 163 DEPSAHLDPITYQVIRKTLKQAFA-DCTVILSEHRIEAMLE-CQRFLVIEENKV 214
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-226 |
2.72e-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: 80.53 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGrARAGIGYLPQEASIFRKlS 94
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLAS-LRRQVALVSQDVVLFND-T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNImAILETRKELDREGRRKELESLLQEFhISHIRDNL-------GMSLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:TIGR02203 422 IANNI-AYGRTEQADRAEIERALAAAYAQDF-VDKLPLGLdtpigenGVLLSGGQRQRLAIARALLKDAPILILDEATSA 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 168 VDPISVGDIKQIIHHLKaKGIGVLITDHNVrETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:TIGR02203 500 LDNESERLVQAALERLM-QGRTTLVIAHRL-STIEKADRIVVMDDGRIVERGTHNELLA 556
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-171 |
3.73e-17 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 80.17 E-value: 3.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARagIGYLPQEASIFRKLSVADN 98
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRR--VGYMSQAFSLYGELTVRQN 359
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 99 IMaiLETRK-ELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPI 171
Cdd:NF033858 360 LE--LHARLfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-227 |
4.28e-17 |
|
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: 79.73 E-value: 4.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQ-----------VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAdQGRVLIDNLDVSH--- 69
Cdd:COG4172 276 LEARDLKVWFPIKRglfrrtvghvkAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPS-EGEIRFDGQDLDGlsr 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 70 ---QPMhgRARAGIgylpqeasIFR--------KLSVADNI---MAILETrkELDREGRRKELESLLQEFHISH-IRDNL 134
Cdd:COG4172 355 ralRPL--RRRMQV--------VFQdpfgslspRMTVGQIIaegLRVHGP--GLSAAERRARVAEALEEVGLDPaARHRY 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 135 GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDpISVGdiKQIIHHLKA----KGIG-VLITdHN---VREtldICET 206
Cdd:COG4172 423 PHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQ--AQILDLLRDlqreHGLAyLFIS-HDlavVRA---LAHR 495
|
250 260
....*....|....*....|.
gi 820872358 207 AYIVNDGQLIAEGDAQTILAN 227
Cdd:COG4172 496 VMVMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-236 |
5.17e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 77.86 E-value: 5.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG-----RARAGIGYLPQEASIFRKLSV 95
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 AD------NIMAILETRKELDREgrrkelesllqEFHISHIRDNL----GMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK13649 105 KDvafgpqNFGVSQEEAEALARE-----------KLALVGISESLfeknPFELSGGQMRRVAIAGILAMEPKILVLDEPT 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 166 AGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN-ELVKEVYLG 236
Cdd:PRK13649 174 AGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvDFLEEKQLG 245
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-169 |
9.56e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 77.96 E-value: 9.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 1 MATLKAQHLAKSYKGR-QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpMHGRARaG 79
Cdd:PRK11650 1 MAGLKLQAVRKSYDGKtQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNE--LEPADR-D 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQEASIFRKLSVADNIMAILETRKeLDREGRRK---------ELESLLqefhishirDNLGMSLSGGERRRVEIAR 150
Cdd:PRK11650 78 IAMVFQNYALYPHMSVRENMAYGLKIRG-MPKAEIEErvaeaarilELEPLL---------DRKPRELSGGQRQRVAMGR 147
|
170
....*....|....*....
gi 820872358 151 ALATAPKFILLDEPFAGVD 169
Cdd:PRK11650 148 AIVREPAVFLFDEPLSNLD 166
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
7-193 |
9.81e-17 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 78.82 E-value: 9.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGlvqadqgrvlIDnldvshQPMHGRARAG----IG 81
Cdd:TIGR03719 8 NRVSKVVpPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG----------VD------KDFNGEARPQpgikVG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIM-AILETRKELDR------------------EGRRKELESLLQEFHISHIRDNLGMS----- 137
Cdd:TIGR03719 72 YLPQEPQLDPTKTVRENVEeGVAEIKDALDRfneisakyaepdadfdklAAEQAELQEIIDAADAWDLDSQLEIAmdalr 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 138 ----------LSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQiihHLKA-KGIGVLIT 193
Cdd:TIGR03719 152 cppwdadvtkLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLER---HLQEyPGTVVAVT 215
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-173 |
1.15e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.50 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGI--- 80
Cdd:PRK11701 7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERrrl 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 -----GYLPQEA--SIFRKLSVADNI----MAILEtrkeldRE-GR-RKELESLLQEFHISHIR-DNLGMSLSGGERRRV 146
Cdd:PRK11701 87 lrtewGFVHQHPrdGLRMQVSAGGNIgerlMAVGA------RHyGDiRATAGDWLERVEIDAARiDDLPTTFSGGMQQRL 160
|
170 180
....*....|....*....|....*..
gi 820872358 147 EIARALATAPKFILLDEPFAGVDpISV 173
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLD-VSV 186
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-219 |
1.28e-16 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 76.03 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 10 AKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIdnldvshqpmHGRARA----GIGYLPQ 85
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV----------RGRVSSllglGGGFNPE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 86 easifrkLSVADNIMAILE----TRKELDRegRRKELESL--LQEFHISHIRdnlgmSLSGGERRRVEIARALATAPKFI 159
Cdd:cd03220 99 -------LTGRENIYLNGRllglSRKEIDE--KIDEIIEFseLGDFIDLPVK-----TYSSGMKARLAFAIATALEPDIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 160 LLDEPFAgvdpisVGDI------KQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:cd03220 165 LIDEVLA------VGDAafqekcQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
18-214 |
1.36e-16 |
|
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: 75.20 E-value: 1.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 18 VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLidnldvshqpMHGRaragIGYLPQEASIFRkLSVAD 97
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS----------VPGS----IAYVSQEPWIQN-GTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 98 NIMAiletRKELDREGRRKELE--SLLQEFHISHIRDNL-----GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDP 170
Cdd:cd03250 85 NILF----GKPFDEERYEKVIKacALEPDLEILPDGDLTeigekGINLSGGQKQRISLARAVYSDADIYLLDDPLSAVDA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 820872358 171 iSVGD--IKQ-IIHHLKAKGIGVLITdHNVrETLDICETAYIVNDGQ 214
Cdd:cd03250 161 -HVGRhiFENcILGLLLNNKTRILVT-HQL-QLLPHADQIVVLDNGR 204
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-235 |
1.55e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 76.79 E-value: 1.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG-----RARAGIGYLPQEASIFRKlSV 95
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklRKKVSLVFQFPEAQLFEN-TV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 ADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGD 175
Cdd:PRK13641 104 LKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKE 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 176 IKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN-ELVKEVYL 235
Cdd:PRK13641 184 MMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDkEWLKKHYL 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
16-218 |
1.62e-16 |
|
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: 77.94 E-value: 1.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQ-ADQGRVLIDNLDVSHQPMHGRARAGIGYLPQEAS---IFR 91
Cdd:TIGR02633 273 RKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKrhgIVP 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KLSVADNI-MAILE---TRKELDREGRRKELESLLQEFHISHIRDNLGM-SLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:TIGR02633 353 ILGVGKNItLSVLKsfcFKMRIDAAAELQIIGSAIQRLKVKTASPFLPIgRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 820872358 167 GVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
15-218 |
2.54e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.28 E-value: 2.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQ-ADQGRVLIDNLDVSHQPMHGRARAGIGYLPQEasifRK- 92
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKIRNPQQAIAQGIAMVPED----RKr 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 ------LSVADNI-MAILET---RKELDREGRRKELESLLQEFHI--SHIRDNLGmSLSGGERRRVEIARALATAPKFIL 160
Cdd:PRK13549 350 dgivpvMGVGKNItLAALDRftgGSRIDDAAELKTILESIQRLKVktASPELAIA-RLSGGNQQKAVLAKCLLLNPKILI 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 161 LDEPFAGVDpisVG---DIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:PRK13549 429 LDEPTRGID---VGakyEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLKGD 486
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-163 |
5.23e-16 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 76.54 E-value: 5.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSYKG-RQVVRDVSLSIDSGQIVGLLGPNGAGKTTcfymIVGLVQ----ADQGRVLIDNLDVSHQPMHGRARAgIG 81
Cdd:PRK13657 338 DDVSFSYDNsRQGVEDVSFEAKPGQTVAIVGPTGAGKST----LINLLQrvfdPQSGRILIDGTDIRTVTRASLRRN-IA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKlSVADNI------------MAILETRKELD-REGRRKELESLLQEfhishiRdnlGMSLSGGERRRVEI 148
Cdd:PRK13657 413 VVFQDAGLFNR-SIEDNIrvgrpdatdeemRAAAERAQAHDfIERKPDGYDTVVGE------R---GRQLSGGERQRLAI 482
|
170
....*....|....*
gi 820872358 149 ARALATAPKFILLDE 163
Cdd:PRK13657 483 ARALLKDPPILILDE 497
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
16-163 |
5.35e-16 |
|
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: 76.78 E-value: 5.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGrARAGIGYLPQEASIFRKlSV 95
Cdd:COG5265 371 RPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQAS-LRAAIGIVPQDTVLFND-TI 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 ADNImailetrkeldREGR----RKELESLLQEFHISHIRDNL-----------GMSLSGGERRRVEIARALATAPKFIL 160
Cdd:COG5265 449 AYNI-----------AYGRpdasEEEVEAAARAAQIHDFIESLpdgydtrvgerGLKLSGGEKQRVAIARTLLKNPPILI 517
|
...
gi 820872358 161 LDE 163
Cdd:COG5265 518 FDE 520
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
11-195 |
5.80e-16 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 76.46 E-value: 5.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 11 KSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD--QGRVLIDNLDVSHQPMHGraragIGYLPQEAS 88
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPTKQILKR-----TGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 89 IFRKLSVADNIM--AILETRKELDREGRRKELESLLQEFHISH-----IRDNLGMSLSGGERRRVEIARALATAPKFILL 161
Cdd:PLN03211 151 LYPHLTVRETLVfcSLLRLPKSLTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190
....*....|....*....|....*....|....
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDH 195
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
15-241 |
7.04e-16 |
|
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: 76.49 E-value: 7.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADqGRVLIDNL---DVSHQpmhgRARAGIGYLPQEASIFR 91
Cdd:TIGR01271 1231 GRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVswnSVTLQ----TWRKAFGVIPQKVFIFS 1305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KlsvadnimailETRKELDREGRRKE-----------LESLLQEF--HISHIRDNLGMSLSGGERRRVEIARALATAPKF 158
Cdd:TIGR01271 1306 G-----------TFRKNLDPYEQWSDeeiwkvaeevgLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSILSKAKI 1374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 159 ILLDEPFAGVDPISVGDIKQIIHHLKAKgIGVLITDHNVRETLDiCETaYIVNDGQLIAEGDAQTILANE--LVKEVyLG 236
Cdd:TIGR01271 1375 LLLDEPSAHLDPVTLQIIRKTLKQSFSN-CTVILSEHRVEALLE-CQQ-FLVIEGSSVKQYDSIQKLLNEtsLFKQA-MS 1450
|
....*
gi 820872358 237 HEFRL 241
Cdd:TIGR01271 1451 AADRL 1455
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
4-198 |
1.07e-15 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 73.70 E-value: 1.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQ----VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpMHGRARAG 79
Cdd:PRK11629 6 LQCDNLCKRYQEGSvqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSK--LSSAAKAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 -----IGYLPQEASIFRKLSVADNIMAILETRKELDREGRRKELEsLLQEFHISHIRDNLGMSLSGGERRRVEIARALAT 154
Cdd:PRK11629 84 lrnqkLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALE-MLAAVGLEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVR 198
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQ 207
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
14-238 |
1.20e-15 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 75.59 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 14 KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYLPQ---EASIF 90
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLSVADNI--------------MAILETRKELDREGRRKELESLlqefHISHIRDNLGmSLSGGERRRVEIARALATAP 156
Cdd:PRK09700 354 PNFSIAQNMaisrslkdggykgaMGLFHEVDEQRTAENQRELLAL----KCHSVNQNIT-ELSGGNQQKVLISKWLCCCP 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 157 KFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILANELVKEVYLG 236
Cdd:PRK09700 429 EVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWALP 508
|
..
gi 820872358 237 HE 238
Cdd:PRK09700 509 QE 510
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-196 |
1.37e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 75.53 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAQHLAKSYK-GRQ---VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA- 76
Cdd:PRK10535 3 ALLELKDIRRSYPsGEEqveVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 --RAGIGYLPQEASIFRKLSVADNImAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALAT 154
Cdd:PRK10535 83 lrREHFGFIFQRYHLLSHLTAAQNV-EVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHN 196
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-164 |
1.52e-15 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 75.16 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLI-DNLDVSH--QpmhgrARAGi 80
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKLAYvdQ-----SRDA- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 gyLPQEASIFRKLSVADNIMAI----LETRKELDREGrrkelesllqeFHISHIRDNLGMsLSGGERRRVEIARALATAP 156
Cdd:PRK11819 399 --LDPNKTVWEEISGGLDIIKVgnreIPSRAYVGRFN-----------FKGGDQQKKVGV-LSGGERNRLHLAKTLKQGG 464
|
....*...
gi 820872358 157 KFILLDEP 164
Cdd:PRK11819 465 NVLLLDEP 472
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-219 |
2.18e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 73.66 E-value: 2.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPM-----HGRARAGIGYLPQEASIFR 91
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdkyirPVRKRIGMVFQFPESQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 klsvaDNI-MAILETRKE--LDREGRRKELESLLQEFHIShiRDNLGMS---LSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK13646 101 -----DTVeREIIFGPKNfkMNLDEVKNYAHRLLMDLGFS--RDVMSQSpfqMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 166 AGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
4-203 |
2.77e-15 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 72.19 E-value: 2.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNldvSHQPMHGRARAgIGYL 83
Cdd:PRK13543 12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRSRF-MAYL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILETrkeldrEGRRKEL--ESLLQEFHISHIRDNLGMSLSGGERRRVEIARA-LATAPKFiL 160
Cdd:PRK13543 88 GHLPGLKADLSTLENLHFLCGL------HGRRAKQmpGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLwLSPAPLW-L 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 820872358 161 LDEPFAGVDPISVGDIKQIIH-HLKAKGiGVLITDHNVRETLDI 203
Cdd:PRK13543 161 LDEPYANLDLEGITLVNRMISaHLRGGG-AALVTTHGAYAAPPV 203
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-224 |
3.60e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 74.11 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 3 TLKAQHLA-KSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVqADQGRVLIDNLDVSHQPMhGRARAGIG 81
Cdd:PRK11174 349 TIEAEDLEiLSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDP-ESWRKHLS 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFrKLSVADNImaiLETRKELDREgrrkELESLLQEFHISHIRDNL-----------GMSLSGGERRRVEIAR 150
Cdd:PRK11174 427 WVGQNPQLP-HGTLRDNV---LLGNPDASDE----QLQQALENAWVSEFLPLLpqgldtpigdqAAGLSVGQAQRLALAR 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 151 ALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVrETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVT-HQL-EDLAQWDQIWVMQDGQIVQQGDYAEL 570
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-226 |
4.34e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 72.82 E-value: 4.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 22 VSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIGYLPQEA-SIFRKLSVADNIM 100
Cdd:PRK13642 26 VSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK-IGMVFQNPdNQFVGATVEDDVA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 101 AILETRKeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQII 180
Cdd:PRK13642 105 FGMENQG-IPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRVI 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 820872358 181 HHLKAK-GIGVLITDHNVRETLDiCETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK13642 184 HEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
4-197 |
4.99e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.44 E-value: 4.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpMHGRA----RA 78
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITR--LKNREvpflRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 79 GIGYLPQEASIFRKLSVADNImAILETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK10908 80 QIGMIFQDHHLLMDRTVYDNV-AIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158
|
170 180 190
....*....|....*....|....*....|....*....
gi 820872358 159 ILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNV 197
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDI 197
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
13-226 |
1.40e-14 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 72.46 E-value: 1.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 13 YKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVShQPMHgRARAG--IGYLPQ--EAS 88
Cdd:NF033858 11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA-DARH-RRAVCprIAYMPQglGKN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 89 IFRKLSVADNI--MAILETrkeLDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:NF033858 89 LYPTLSVFENLdfFGRLFG---QDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTT 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820872358 167 GVDPISVGDIKQIIHHLKAK--GIGVLITdhnvretldiceTAYI-----------VNDGQLIAEGDAQTILA 226
Cdd:NF033858 166 GVDPLSRRQFWELIDRIRAErpGMSVLVA------------TAYMeeaerfdwlvaMDAGRVLATGTPAELLA 226
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
16-227 |
3.50e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 70.05 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQ-------PMhgRARAGIGYLPQEAS 88
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGkknkklkPL--RKKVGIVFQFPEHQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 89 IFRKlSVADNIM--AILETRKELDREGRRKELESL--LQEfhisHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK13634 98 LFEE-TVEKDICfgPMNFGVSEEDAKQKAREMIELvgLPE----ELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEP 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 165 FAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK13634 173 TAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
13-195 |
3.64e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 68.82 E-value: 3.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 13 YKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQpmHGRARAGIGYLPQEASIFRK 92
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKD--LCTYQKQLCFVGHRSGINPY 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 LSVADNIMAILETrkeldrEGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPIS 172
Cdd:PRK13540 89 LTLRENCLYDIHF------SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|...
gi 820872358 173 VGDIKQIIHHLKAKGIGVLITDH 195
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSH 185
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
4-169 |
4.13e-14 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 69.04 E-value: 4.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY-KGRQ---VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRA--R 77
Cdd:PRK10584 7 VEVHHLKKSVgQGEHelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAklR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 78 A-GIGYLPQEASIFRKLSVADNIMAILETRKELDREGRRKELEsLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAP 156
Cdd:PRK10584 87 AkHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKA-LLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
|
170
....*....|...
gi 820872358 157 KFILLDEPFAGVD 169
Cdd:PRK10584 166 DVLFADEPTGNLD 178
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-226 |
4.69e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 70.89 E-value: 4.69e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGL-----VQADQGRVLIDNLDVSHQPmHGRARAGIGylPQEASIF 90
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHAS-EQTLRGVRG--NKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLSVADNIMAILETR--------KELDREGRRKELESLLQEFHISHIRDNLG---MSLSGGERRRVEIARALATAPKFI 159
Cdd:PRK15134 99 QEPMVSLNPLHTLEKQlyevlslhRGMRREAARGEILNCLDRVGIRQAAKRLTdypHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 160 LLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFS 246
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-234 |
5.07e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 69.29 E-value: 5.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVG--LVQADQGRVLIDNLDVSHQPMHGRARAGIG 81
Cdd:CHL00131 8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHLGIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMAILETRKeldREGRRKELESLlqEFH--ISHIRDNLGMS-----------LSGGERRRVEI 148
Cdd:CHL00131 88 LAFQYPIEIPGVSNADFLRLAYNSKR---KFQGLPELDPL--EFLeiINEKLKLVGMDpsflsrnvnegFSGGEKKRNEI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 149 ARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVReTLDICETAY--IVNDGQLIAEGDAQtiLA 226
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQR-LLDYIKPDYvhVMQNGKIIKTGDAE--LA 239
|
....*...
gi 820872358 227 NELVKEVY 234
Cdd:CHL00131 240 KELEKKGY 247
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-233 |
6.30e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 6.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLID------NLDVSHQPMHGRARAGIGYLPQEASIF 90
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGdyaipaNLKKIKEVKRLRKEIGLVFQFPEYQLF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLSVADniMAILETRKELDREGRRKELESLLQefHISHIRDNLGMS---LSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:PRK13645 105 QETIEKD--IAFGPVNLGENKQEAYKKVPELLK--LVQLPEDYVKRSpfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 168 VDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN-ELVKEV 233
Cdd:PRK13645 181 LDPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNqELLTKI 248
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
9-197 |
8.75e-14 |
|
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: 70.20 E-value: 8.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 9 LAKSYKGrqvvrdVSLSIDSGQI-----VGLLGPNGAGKTTCFYMIVGLVQADQGRVlIDNLDVShqpmhgraragigYL 83
Cdd:COG1245 347 LTKSYGG------FSLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEV-DEDLKIS-------------YK 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILEtrkelDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:COG1245 407 PQYISPDYDGTVEEFLRSANT-----DDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDE 481
|
170 180 190
....*....|....*....|....*....|....*..
gi 820872358 164 PFAGVD---PISVGdiKQIIHHLKAKGIGVLITDHNV 197
Cdd:COG1245 482 PSAHLDveqRLAVA--KAIRRFAENRGKTAMVVDHDI 516
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-226 |
9.76e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 69.73 E-value: 9.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAdQGRVLIDNldvshQPMHG---------RARAGIGYLPQEA 87
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS-QGEIWFDG-----QPLHNlnrrqllpvRHRIQVVFQDPNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 88 SIFRKLSVADNIMAILET-RKELDREGRRKELESLLQEFHIS-HIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK15134 374 SLNPRLNVLQIIEEGLRVhQPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 166 AGVDPiSVGdiKQIIHHLKA----KGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK15134 454 SSLDK-TVQ--AQILALLKSlqqkHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFA 515
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
16-227 |
1.21e-13 |
|
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: 69.71 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD----QGRVLIDNLDVSHQP------MHGRAragIGYLPQ 85
Cdd:COG4172 23 VEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSerelrrIRGNR---IAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 86 E--ASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGM---SLSGGERRRVEIARALATAPKFIL 160
Cdd:COG4172 100 EpmTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLDAyphQLSGGQRQRVMIAMALANEPDLLI 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 161 LDEPFAGVDPISVGDIKQIIHHLKAK-GIGVL-ITdHN---VREtldICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG4172 180 ADEPTTALDVTVQAQILDLLKDLQRElGMALLlIT-HDlgvVRR---FADRVAVMRQGEIVEQGPTAELFAA 247
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
4-234 |
1.42e-13 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 68.31 E-value: 1.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLV---QADQGRVLIDNLDVSHQPMH------- 73
Cdd:PRK13547 2 LTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtggGAPRGARVTGDVTLNGEPLAaidaprl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 74 GRARAgigYLPQEASIFRKLSVADNIM------------AILETRKELDREGRRKELESLLQefhishiRDNlgMSLSGG 141
Cdd:PRK13547 82 ARLRA---VLPQAAQPAFAFSAREIVLlgrypharragaLTHRDGEIAWQALALAGATALVG-------RDV--TTLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 142 ERRRVEIARALA---------TAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVN 211
Cdd:PRK13547 150 ELARVQFARVLAqlwpphdaaQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLA 229
|
250 260
....*....|....*....|...
gi 820872358 212 DGQLIAEGDAQTILANELVKEVY 234
Cdd:PRK13547 230 DGAIVAHGAPADVLTPAHIARCY 252
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
12-226 |
2.65e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 68.51 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQV--VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMhGRARAGIGYLPQEASI 89
Cdd:PRK11176 350 TYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTL-ASLRNQVALVSQNVHL 428
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 90 FRKlSVADNIMAILE---TRKELDREGRRkeleSLLQEFhISHIRDNL-------GMSLSGGERRRVEIARALATAPKFI 159
Cdd:PRK11176 429 FND-TIANNIAYARTeqySREQIEEAARM----AYAMDF-INKMDNGLdtvigenGVLLSGGQRQRIAIARALLRDSPIL 502
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 160 LLDEPFAGVDPISVGDIKQIIHHLKaKGIGVLITDHNVrETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQ-KNRTSLVIAHRL-STIEKADEILVVEDGEIVERGTHAELLA 567
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
9-197 |
3.14e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 68.30 E-value: 3.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 9 LAKSYKgrqvvrDVSLSIDSGQI-----VGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDnLDVShqpmhgraragigYL 83
Cdd:PRK13409 346 LTKKLG------DFSLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIS-------------YK 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASIFRKLSVADNIMAILET------RKELdreGRRKELESLLQefhiSHIRDnlgmsLSGGERRRVEIARALATAPK 157
Cdd:PRK13409 406 PQYIKPDYDGTVEDLLRSITDDlgssyyKSEI---IKPLQLERLLD----KNVKD-----LSGGELQRVAIAACLSRDAD 473
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 820872358 158 FILLDEPFAGVD---PISVGdiKQIIHHLKAKGIGVLITDHNV 197
Cdd:PRK13409 474 LYLLDEPSAHLDveqRLAVA--KAIRRIAEEREATALVVDHDI 514
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
4-237 |
3.59e-13 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 67.12 E-value: 3.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGR---------QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG 74
Cdd:PRK15112 5 LEVRNLSKTFRYRtgwfrrqtvEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 75 RARAgIGYLPQEASifRKLSVADNIMAILET----RKELDREGRRKELESLLQEfhISHIRDNLGM---SLSGGERRRVE 147
Cdd:PRK15112 85 RSQR-IRMIFQDPS--TSLNPRQRISQILDFplrlNTDLEPEQREKQIIETLRQ--VGLLPDHASYyphMLAPGQKQRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 148 IARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239
|
250
....*....|....
gi 820872358 227 ---NELVKEVYLGH 237
Cdd:PRK15112 240 splHELTKRLIAGH 253
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
2-185 |
4.09e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 4.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 2 ATLKAqhlaksykgrqvVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLI---DNLDVSHQPMHgRARA 78
Cdd:PRK15079 32 KTLKA------------VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgkDLLGMKDDEWR-AVRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 79 GIGYLPQE--ASIFRKLSVADNIMAILET-RKELDREGRRKELESLLQEFHIshiRDNL----GMSLSGGERRRVEIARA 151
Cdd:PRK15079 99 DIQMIFQDplASLNPRMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGL---LPNLinryPHEFSGGQCQRIGIARA 175
|
170 180 190
....*....|....*....|....*....|....
gi 820872358 152 LATAPKFILLDEPFAGVDpisVGDIKQIIHHLKA 185
Cdd:PRK15079 176 LILEPKLIICDEPVSALD---VSIQAQVVNLLQQ 206
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
15-202 |
4.16e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.91 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQivGLL--GPNGAGKTTCFYMIVGLVQADQGRVlidnldvsHQPMHGRA-----RAgigYLPQEa 87
Cdd:COG4178 375 GRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLWPYGSGRI--------ARPAGARVlflpqRP---YLPLG- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 88 sifrklSVADnimAIL--ETRKELDREgrrkELESLLQEFHISHIRDNL------GMSLSGGERRRVEIARALATAPKFI 159
Cdd:COG4178 441 ------TLRE---ALLypATAEAFSDA----ELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWL 507
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 820872358 160 LLDEPFAGVDPISVGDI-KQIIHHLkaKGIGVLITDHnvRETLD 202
Cdd:COG4178 508 FLDEATSALDEENEAALyQLLREEL--PGTTVISVGH--RSTLA 547
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
119-230 |
4.42e-13 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 67.73 E-value: 4.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 119 ESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVR 198
Cdd:PRK10938 117 EQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFD 196
|
90 100 110
....*....|....*....|....*....|..
gi 820872358 199 ETLDICETAYIVNDGQLIAEGDAQTILANELV 230
Cdd:PRK10938 197 EIPDFVQFAGVLADCTLAETGEREEILQQALV 228
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
7-164 |
4.89e-13 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 67.84 E-value: 4.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVlidnldvshQPMHGrarAGIGYLPQ 85
Cdd:PRK11819 10 NRVSKVVpPKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEA---------RPAPG---IKVGYLPQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 86 EASIFRKLSVADNIM-AILETRKELDR------------------EGRRKELESLLQEFHISHIRDNLGM---------- 136
Cdd:PRK11819 78 EPQLDPEKTVRENVEeGVAEVKAALDRfneiyaayaepdadfdalAAEQGELQEIIDAADAWDLDSQLEIamdalrcppw 157
|
170 180 190
....*....|....*....|....*....|...
gi 820872358 137 -----SLSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK11819 158 dakvtKLSGGERRRVALCRLLLEKPDMLLLDEP 190
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
18-221 |
5.11e-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: 68.05 E-value: 5.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 18 VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGrARAGIGYLPQEASIFRKlsvad 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHD-LRFKITIIPQDPVLFSG----- 1374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 98 nimailETRKELDREGRRKElESLLQEFHISHIRDNL--------------GMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:TIGR00957 1375 ------SLRMNLDPFSQYSD-EEVWWALELAHLKTFVsalpdkldhecaegGENLSVGQRQLVCLARALLRKTKILVLDE 1447
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 164 PFAGVDpISVGDIKQIIHHLKAKGIGVLITDHNVRETLDIceTAYIVNDGQLIAEGDA 221
Cdd:TIGR00957 1448 ATAAVD-LETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDY--TRVIVLDKGEVAEFGA 1502
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-202 |
5.18e-13 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 64.87 E-value: 5.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVlidnldvsHQPmhgrARAGIGYLPQEASifrkls 94
Cdd:cd03223 13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI--------GMP----EGEDLLFLPQRPY------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 vadnimailetrkeldregrrkelesllqeFHISHIRDNL----GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDP 170
Cdd:cd03223 75 ------------------------------LPLGTLREQLiypwDDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
170 180 190
....*....|....*....|....*....|..
gi 820872358 171 ISVGDIKQIihhLKAKGIGVLITDHnvRETLD 202
Cdd:cd03223 125 ESEDRLYQL---LKELGITVISVGH--RPSLW 151
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
19-199 |
1.20e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 65.91 E-value: 1.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRaRAGIGYLPQEA-SIFRKLSVAD 97
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDI-RHKIGMVFQNPdNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 98 NIMAILETrKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIK 177
Cdd:PRK13650 102 DVAFGLEN-KGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELI 180
|
170 180
....*....|....*....|...
gi 820872358 178 QIIHHLKAK-GIGVLITDHNVRE 199
Cdd:PRK13650 181 KTIKGIRDDyQMTVISITHDLDE 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-218 |
1.27e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 66.74 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTcFYMIV-----GlvQADQGRVLIDNLDVSHQPMHGRARAGIGYLPQEasi 89
Cdd:NF040905 272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMSVfgrsyG--RNISGTVFKDGKEVDVSTVSDAIDAGLAYVTED--- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 90 fRK---LSVADNI-----MAILE---TRKELDREGRRKELESLLQEFHI--SHIRDNLGmSLSGGERRRVEIARALATAP 156
Cdd:NF040905 346 -RKgygLNLIDDIkrnitLANLGkvsRRGVIDENEEIKVAEEYRKKMNIktPSVFQKVG-NLSGGNQQKVVLSKWLFTDP 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 157 KFILLDEPFAGVDpisVG---DIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAE 218
Cdd:NF040905 424 DVLILDEPTRGID---VGakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
15-201 |
2.42e-12 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 65.93 E-value: 2.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDnldvshqpmhgrARAGIGYLPQEASIFRKlS 94
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP------------AKGKLFYVPQRPYMTLG-T 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIMAILETRKELDREGRRKELESLLQEFHISHI-RDNLGMS--------LSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:TIGR00954 531 LRDQIIYPDSSEDMKRRGLSDKDLEQILDNVQLTHIlEREGGWSavqdwmdvLSGGEKQRIAMARLFYHKPQFAILDECT 610
|
170 180 190
....*....|....*....|....*....|....*..
gi 820872358 166 AGVDPisvgDIKQ-IIHHLKAKGIGVLITDHnvRETL 201
Cdd:TIGR00954 611 SAVSV----DVEGyMYRLCREFGITLFSVSH--RKSL 641
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
18-228 |
2.50e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 66.15 E-value: 2.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 18 VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgIGYLPQEASIFRKlSVAD 97
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV-LSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 98 NIMAILETRKeldregrrkelESLLQEFHISHIRDNL--------------GMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PLN03232 1329 NIDPFSEHND-----------ADLWEALERAHIKDVIdrnpfgldaevsegGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 164 PFAGVDPISVGDIKQIIHHlKAKGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGDAQTILANE 228
Cdd:PLN03232 1398 ATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-219 |
2.76e-12 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 65.14 E-value: 2.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTcfymivGLVQADqgrvlIDNLDVSHQP-------MHGRA 76
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAH-----V*GPDAGRRPwrf*twcANRRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 77 -RAGIG-YLPQEASIFRKLSVADNIMAIlETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALAT 154
Cdd:NF000106 83 lRRTIG*HRPVR*GRRESFSGRENLYMI-GR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEG 219
Cdd:NF000106 162 RPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-169 |
7.61e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.80 E-value: 7.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTcfymivgLVQAdqgrvLIDNLDVSHqpmhGR--ARAGIGYLPQEASIFRKl 93
Cdd:PTZ00243 673 KVLLRDVSVSVPRGKLTVVLGATGSGKST-------LLQS-----LLSQFEISE----GRvwAERSIAYVPQQAWIMNA- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 94 SVADNIMAILETRKE-LDREGRRKELESLLQ------EFHISHirdnLGMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:PTZ00243 736 TVRGNILFFDEEDAArLADAVRVSQLEADLAqlggglETEIGE----KGVNLSGGQKARVSLARAVYANRDVYLLDDPLS 811
|
...
gi 820872358 167 GVD 169
Cdd:PTZ00243 812 ALD 814
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
12-164 |
2.19e-11 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 63.05 E-value: 2.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLI-DNLDVSHQPMHgraRAGIGylPQEasif 90
Cdd:PRK11147 328 QIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgTKLEVAYFDQH---RAELD--PEK---- 398
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 91 rklSVADNIMailETRKELDREGRRKELESLLQEFHISHIRdnlGMS----LSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PRK11147 399 ---TVMDNLA---EGKQEVMVNGRPRHVLGYLQDFLFHPKR---AMTpvkaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-227 |
2.84e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 61.64 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKT-TCFYMIVGL---VQADQGRVLIDNLDVSHQPMHGRARAGIGYLPQEAsiFR 91
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILpagVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPRSA--FN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KL-SVADNImaiLETRKELDREGRRKELESLLQEFHISHIRDNLGM---SLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:PRK10418 94 PLhTMHTHA---RETCLALGKPADDATLTAALEAVGLENAARVLKLypfEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 820872358 168 VDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK10418 171 LDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
19-215 |
3.81e-11 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 62.05 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAGIGYLPQE---ASIFRKLSV 95
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEErrsTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 ADN-IMAILETRKE----LDREGRRKELESLLQEFHI---SHiRDNLGmSLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:PRK10982 344 GFNsLISNIRNYKNkvglLDNSRMKSDTQWVIDSMRVktpGH-RTQIG-SLSGGNQQKVIIGRWLLTQPEILMLDEPTRG 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 820872358 168 VDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQL 215
Cdd:PRK10982 422 IDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-227 |
5.10e-11 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.80 E-value: 5.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVL-----IDNLDVSH-QPMhgraRAGIGYLPQE--ASIF 90
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqrIDTLSPGKlQAL----RRDIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKLSVADNIMAILETRKELDREGRRKELESLLQE--------FHISHirdnlgmSLSGGERRRVEIARALATAPKFILLD 162
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERvgllpehaWRYPH-------EFSGGQRQRICIARALALNPKVIIAD 488
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 163 EPFAGVDpisVGDIKQIIHHL----KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:PRK10261 489 EAVSALD---VSIRGQIINLLldlqRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFEN 554
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-219 |
7.12e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.92 E-value: 7.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVG-LVQADQGRVLIdnldvshqpmhgraRAGIGYLPQEASIFRKlSVADNI 99
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGeLSHAETSSVVI--------------RGSVAYVPQVSWIFNA-TVRENI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 100 MaiLETRKELDREGRRKELESLLQEFHISHIRD-----NLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVG 174
Cdd:PLN03232 700 L--FGSDFESERYWRAIDVTALQHDLDLLPGRDlteigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 820872358 175 DI--KQIIHHLKAKgIGVLITdhNVRETLDICETAYIVNDGQLIAEG 219
Cdd:PLN03232 778 QVfdSCMKDELKGK-TRVLVT--NQLHFLPLMDRIILVSEGMIKEEG 821
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
21-220 |
7.58e-11 |
|
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: 60.04 E-value: 7.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPM---HGRARAGIGYLPQEASIFRKlSVAD 97
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFeatRSRNRYSVAYAAQKPWLLNA-TVEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 98 NImaILETRKELDREGRRKELESLLQEFHISHIRDNL-----GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDpIS 172
Cdd:cd03290 98 NI--TFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQTeigerGINLSGGQRQRICVARALYQNTNIVFLDDPFSALD-IH 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 820872358 173 VGDikqiihHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGD 220
Cdd:cd03290 175 LSD------HLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKD 216
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
12-176 |
9.05e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 61.46 E-value: 9.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVlidnldvSHQpmhGRaragIGYLPQEASIFR 91
Cdd:TIGR01271 435 SLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI-------KHS---GR----ISFSPQTSWIMP 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KlSVADNIMAIL---ETR-KELDREGRRKELESLLQEfhishiRDNL-----GMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:TIGR01271 501 G-TIKDNIIFGLsydEYRyTSVIKACQLEEDIALFPE------KDKTvlgegGITLSGGQRARISLARAVYKDADLYLLD 573
|
170
....*....|....
gi 820872358 163 EPFAGVDPISVGDI 176
Cdd:TIGR01271 574 SPFTHLDVVTEKEI 587
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
17-224 |
1.13e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRV-------------LIDNLDVSHQPMHGRARAGIGYL 83
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllrrrsrqVIELSEQSAAQMRHVRGADMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQE--ASIFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGM---SLSGGERRRVEIARALATAPKF 158
Cdd:PRK10261 110 FQEpmTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRyphQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 159 ILLDEPFAGVDPISVGDIKQIIHHLKAK-GIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:PRK10261 190 LIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-196 |
1.42e-10 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 59.69 E-value: 1.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 28 SGQIVGLLGPNGAGKTTCFYMIVGLVQADQGR-------------------------VLIDNLDVSHQPMHgraragIGY 82
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKfddppdwdeildefrgselqnyftkLLEGDVKVIVKPQY------VDL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQeasifrklSVADNIMAILETRKEldregrRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:cd03236 99 IPK--------AVKGKVGELLKKKDE------RGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 820872358 163 EpfagvdPISVGDIKQ------IIHHLKAKGIGVLITDHN 196
Cdd:cd03236 165 E------PSSYLDIKQrlnaarLIRELAEDDNYVLVVEHD 198
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-224 |
1.71e-10 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 59.74 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVqADQGRV----LIDNLDVSHQPMH--GRARAgigylPQEASIFRK 92
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIggsaTFNGREILNLPEKelNKLRA-----EQISMIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 93 --------LSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGM---SLSGGERRRVEIARALATAPKFILL 161
Cdd:PRK09473 106 pmtslnpyMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMyphEFSGGMRQRVMIAMALLCRPKLLIA 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 162 DEPFAGVDPISVGDIKQIIHHLKAK---GIgVLITdHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREfntAI-IMIT-HDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-183 |
2.07e-10 |
|
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: 58.43 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 11 KSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD---QGRVLIDNLDVshQPMHGRARAGIGYLPQEa 87
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPY--KEFAEKYPGEIIYVSEE- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 88 sifrklsvaDNIMAILETRKELDregrrkelesllqeFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAG 167
Cdd:cd03233 92 ---------DVHFPTLTVRETLD--------------FALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRG 148
|
170
....*....|....*.
gi 820872358 168 VDPISVGDIKQIIHHL 183
Cdd:cd03233 149 LDSSTALEILKCIRTM 164
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-195 |
4.55e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLV--QADQGRVLIDNLDvshqpmhgraragigyLPQEASIFRKL 93
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ----------------FGREASLIDAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 94 SVADNIMAILETrkeLDREG-------RRKELEsllqefhishirdnlgmsLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:COG2401 107 GRKGDFKDAVEL---LNAVGlsdavlwLRRFKE------------------LSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|
gi 820872358 167 GVDPISVGDIKQIIHHL-KAKGIGVLITDH 195
Cdd:COG2401 166 HLDRQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
18-228 |
4.95e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 59.37 E-value: 4.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 18 VVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHqpmHGRA--RAGIGYLPQEASIFRKlsv 95
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISK---FGLMdlRKVLGIIPQAPVLFSG--- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 adnimailETRKELD--REGRRKELESLLQEFHISHI--RDNLGM---------SLSGGERRRVEIARALATAPKFILLD 162
Cdd:PLN03130 1328 --------TVRFNLDpfNEHNDADLWESLERAHLKDVirRNSLGLdaevseageNFSVGQRQLLSLARALLRRSKILVLD 1399
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 163 EPFAGVDPISVGDIKQIIHHlKAKGIGVLITDHNVRETLDiCETAYIVNDGQLIAEGDAQTILANE 228
Cdd:PLN03130 1400 EATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNE 1463
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
15-169 |
7.51e-10 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 57.56 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 15 GRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRvlidnldVSHQpmhGRaragIGYLPQEASIFRKlS 94
Cdd:cd03291 49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGK-------IKHS---GR----ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIMAILETrkeldREGRRKELESLLQ-EFHISHI--RDNL-----GMSLSGGERRRVEIARALATAPKFILLDEPFA 166
Cdd:cd03291 114 IKENIIFGVSY-----DEYRYKSVVKACQlEEDITKFpeKDNTvlgegGITLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
...
gi 820872358 167 GVD 169
Cdd:cd03291 189 YLD 191
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
16-226 |
1.01e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSH-QPMHGRARAGIgyLPQEASIFRKlS 94
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAV--VSQTPFLFSD-T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNImAILE---TRKELDREGRrkeleslLQEFHISHIR---------DNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:PRK10789 405 VANNI-ALGRpdaTQQEIEHVAR-------LASVHDDILRlpqgydtevGERGVMLSGGQKQRISIARALLLNAEILILD 476
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 163 EPFAGVDpisvGDIK-QIIHHLKAKGIG--VLITDHNVRETLDICETaYIVNDGQLIAEGDAQTILA 226
Cdd:PRK10789 477 DALSAVD----GRTEhQILHNLRQWGEGrtVIISAHRLSALTEASEI-LVMQHGHIAQRGNHDQLAQ 538
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
7-226 |
1.49e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 1.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 7 QHLAKSY-KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVShQPMHGRARAGIGYLPQ 85
Cdd:PRK10790 344 DNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLS-SLSHSVLRQGVAMVQQ 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 86 EASIfrklsVADNIMAILETRKELDREGRRKELESL-LQEFhISHIRDNL-------GMSLSGGERRRVEIARALATAPK 157
Cdd:PRK10790 423 DPVV-----LADTFLANVTLGRDISEEQVWQALETVqLAEL-ARSLPDGLytplgeqGNNLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 158 FILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVRETLDiCETAYIVNDGQLIAEGDAQTILA 226
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLSTIVE-ADTILVLHRGQAVEQGTHQQLLA 563
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-226 |
1.54e-09 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 57.65 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 22 VSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIdnldvshqpmhgraRAGIGYLPQEASIfRKLSVADNIMa 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM--------------KGSVAYVPQQAWI-QNDSLRENIL- 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 102 ileTRKELDREGRRKELES--LLQEFHISHIRDNL-----GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPiSVG 174
Cdd:TIGR00957 721 ---FGKALNEKYYQQVLEAcaLLPDLEILPSGDRTeigekGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDA-HVG 796
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 175 diKQIIHH-------LKAKgIGVLITdHNVrETLDICETAYIVNDGQLIAEGDAQTILA 226
Cdd:TIGR00957 797 --KHIFEHvigpegvLKNK-TRILVT-HGI-SYLPQVDVIIVMSGGKISEMGSYQELLQ 850
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-224 |
1.75e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.06 E-value: 1.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAdQGRVLIDNLDVSH---QPMHGRAR-----AGIGYLPQEA--S 88
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDY-PGRVMAEKLEFNGqdlQRISEKERrnlvgAEVAMIFQDPmtS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 89 IFRKLSVADNIMAILETRKELDREGRRKELESLLQEFHISHIRDNLGM---SLSGGERRRVEIARALATAPKFILLDEPF 165
Cdd:PRK11022 102 LNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVyphQLSGGMSQRVMIAMAIACRPKLLIADEPT 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 820872358 166 AGVDpisVGDIKQIIHHL----KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTI 224
Cdd:PRK11022 182 TALD---VTIQAQIIELLlelqQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-169 |
3.50e-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: 3.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMI----VGLVQADQGRVLIDNLdvSHQPMHGRARAGIGYLPQEASIFR 91
Cdd:TIGR00956 74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYDGI--TPEEIKKHYRGDVVYNAETDVHFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 92 KLSVADNI-----MAILETR-KELDREGRRKELESL-LQEFHISHIRD-NLGMSL----SGGERRRVEIARALATAPKFI 159
Cdd:TIGR00956 152 HLTVGETLdfaarCKTPQNRpDGVSREEYAKHIADVyMATYGLSHTRNtKVGNDFvrgvSGGERKRVSIAEASLGGAKIQ 231
|
170
....*....|
gi 820872358 160 LLDEPFAGVD 169
Cdd:TIGR00956 232 CWDNATRGLD 241
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
16-195 |
4.68e-09 |
|
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: 54.56 E-value: 4.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTcfYMIVgLVQADQGRVLIDNLDVSHQPMHGRARAGIGYLPQEASIFRKLSV 95
Cdd:cd03232 20 RQLLNNISGYVKPGTLTALMGESGAGKTT--LLDV-LAGRKTAGVITGEILINGRPLDKNFQRSTGYVEQQDVHSPNLTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 adnimailetrkeldregrrkeLESLlqEFHiSHIRDnlgmsLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGD 175
Cdd:cd03232 97 ----------------------REAL--RFS-ALLRG-----LSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYN 146
|
170 180
....*....|....*....|
gi 820872358 176 IKQIIHHLKAKGIGVLITDH 195
Cdd:cd03232 147 IVRFLKKLADSGQAILCTIH 166
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-164 |
5.22e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 55.67 E-value: 5.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRV-LIDNldvshqpmhgrarAGIGY 82
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSEN-------------ANIGY 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQE-ASIFrklsvaDNIMAILE----TRKELDREGR-RKELESLLqeFHISHIRDNLGmSLSGGERRRVEIARALATAP 156
Cdd:PRK15064 387 YAQDhAYDF------ENDLTLFDwmsqWRQEGDDEQAvRGTLGRLL--FSQDDIKKSVK-VLSGGEKGRMLFGKLMMQKP 457
|
....*...
gi 820872358 157 KFILLDEP 164
Cdd:PRK15064 458 NVLVMDEP 465
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-216 |
6.47e-09 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 55.57 E-value: 6.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQAD--QGRVLIDNLDVSHQPMHGRARAGIG 81
Cdd:NF040905 2 LEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCRFKDIRDSEALGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKLSVADNIMAILETRKE--LDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFI 159
Cdd:NF040905 82 IIHQELALIPYLSIAENIFLGNERAKRgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 160 LLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLI 216
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
17-227 |
1.39e-08 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 54.14 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGL------VQADqgRVLIDNLDVSHQPMHGRaRAGIG--------- 81
Cdd:COG4170 21 KAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkdnwhVTAD--RFRWNGIDLLKLSPRER-RKIIGreiamifqe 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 ---YLPQEASIFRKLSvaDNIMAILETRKELDREG-RRKELESLLQEFHI---SHIRDNLGMSLSGGERRRVEIARALAT 154
Cdd:COG4170 98 pssCLDPSAKIGDQLI--EAIPSWTFKGKWWQRFKwRKKRAIELLHRVGIkdhKDIMNSYPHELTEGECQKVMIAMAIAN 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 155 APKFILLDEPFAGVDPISVGDIKQIIHHL-KAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN 227
Cdd:COG4170 176 QPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
56-193 |
1.45e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.04 E-value: 1.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 56 DQGRVLIDNLDVSHQPMHGrARAGIGYLPQEASIFrKLSVADNIMAILE--TRKELDREGRRKELESLLQEFHISHIRD- 132
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKD-LRNLFSIVSQEPMLF-NMSIYENIKFGKEdaTREDVKRACKFAAIDEFIESLPNKYDTNv 1352
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 133 -NLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLIT 193
Cdd:PTZ00265 1353 gPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-195 |
1.71e-08 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 54.43 E-value: 1.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 29 GQIVGLLGPNGAGKTTCFYMIVGLvqadqgrvLIDNL-DVSHQPM------HGRARAGIGYlpqeasiFRKLSvADNIMA 101
Cdd:PRK13409 99 GKVTGILGPNGIGKTTAVKILSGE--------LIPNLgDYEEEPSwdevlkRFRGTELQNY-------FKKLY-NGEIKV 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 102 IL--------------ETRKELDREGRRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEpfag 167
Cdd:PRK13409 163 VHkpqyvdlipkvfkgKVRELLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDE---- 238
|
170 180 190
....*....|....*....|....*....|....
gi 820872358 168 vdPISVGDIKQ------IIHHLkAKGIGVLITDH 195
Cdd:PRK13409 239 --PTSYLDIRQrlnvarLIREL-AEGKYVLVVEH 269
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-164 |
2.05e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.19 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 24 LSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLID-NLDVSH-QPMHGRARAGigylpqeaSIFRklSVADNIMA 101
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEqDLIVARlQQDPPRNVEG--------TVYD--FVAEGIEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 102 ILETRKE-------LDREGRRKELESL--LQEfHISH---------IRDNLGM----------SLSGGERRRVEIARALA 153
Cdd:PRK11147 94 QAEYLKRyhdishlVETDPSEKNLNELakLQE-QLDHhnlwqlenrINEVLAQlgldpdaalsSLSGGWLRKAALGRALV 172
|
170
....*....|.
gi 820872358 154 TAPKFILLDEP 164
Cdd:PRK11147 173 SNPDVLLLDEP 183
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-195 |
2.10e-08 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 54.02 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 28 SGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRV------------------------LIDN-LDVSHQPMHgraragIGY 82
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkrfrgtelqdyfkkLANGeIKVAHKPQY------VDL 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 LPQeasiFRKLSVADnimaILETRKEldregrRKELESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLD 162
Cdd:COG1245 172 IPK----VFKGTVRE----LLEKVDE------RGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFD 237
|
170 180 190
....*....|....*....|....*....|....*....
gi 820872358 163 EPFagvdpiSVGDIKQ------IIHHLKAKGIGVLITDH 195
Cdd:COG1245 238 EPS------SYLDIYQrlnvarLIRELAEEGKYVLVVEH 270
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
137-219 |
2.49e-08 |
|
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: 53.86 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 137 SLSGGERRRVEIARAL---ATAPKFILLDEPFAGvdpISVGDIKQ---IIHHLKAKGIGVLITDHNvretLDICETA-YI 209
Cdd:TIGR00630 829 TLSGGEAQRIKLAKELskrSTGRTLYILDEPTTG---LHFDDIKKlleVLQRLVDKGNTVVVIEHN----LDVIKTAdYI 901
|
90
....*....|....*...
gi 820872358 210 V--------NDGQLIAEG 219
Cdd:TIGR00630 902 IdlgpeggdGGGTVVASG 919
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
19-170 |
3.58e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 50.36 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgraragiGYLPQEASIFRKLSVADN 98
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPE-------DYRKLFSAVFTDFHLFDQ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 99 IM---------AILEtrKELDREGRRKELEslLQEFHISHIRdnlgmsLSGGERRRVEIARALATAPKFILLDEPFAGVD 169
Cdd:PRK10522 412 LLgpegkpanpALVE--KWLERLKMAHKLE--LEDGRISNLK------LSKGQKKRLALLLALAEERDILLLDEWAADQD 481
|
.
gi 820872358 170 P 170
Cdd:PRK10522 482 P 482
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
137-219 |
3.85e-07 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 49.54 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 137 SLSGGERRRVEIARAL---ATAPKFILLDEPFAGvdpISVGDIKQ---IIHHLKAKGIGVLITDHNvretLDICETA-YI 209
Cdd:cd03271 169 TLSGGEAQRIKLAKELskrSTGKTLYILDEPTTG---LHFHDVKKlleVLQRLVDKGNTVVVIEHN----LDVIKCAdWI 241
|
90
....*....|....*...
gi 820872358 210 V--------NDGQLIAEG 219
Cdd:cd03271 242 IdlgpeggdGGGQVVASG 259
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-228 |
6.65e-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: 48.75 E-value: 6.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKG--RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHG-RARAGI 80
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 gylpqeasifrklSVADNIMAILETRKELDREGRRKElESLLQEFHISHIRDNL--------------GMSLSGGERRRV 146
Cdd:cd03288 100 -------------ILQDPILFSGSIRFNLDPECKCTD-DRLWEALEIAQLKNMVkslpggldavvtegGENFSVGQRQLF 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 147 EIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITdHNVRETLDiCETAYIVNDGQLIAEGDAQTILA 226
Cdd:cd03288 166 CLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFADRTVVTIA-HRVSTILD-ADLVLVLSRGILVECDTPENLLA 243
|
..
gi 820872358 227 NE 228
Cdd:cd03288 244 QE 245
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-173 |
7.40e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.19 E-value: 7.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSY-------KGRQVVR---DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMH 73
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfKPERLVKaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 74 GRARagigyLPQEASIfrklsVADNIMAILETRK--------------ELDREGRRKELESLLQ------EFHishirDN 133
Cdd:PRK11308 86 AQKL-----LRQKIQI-----VFQNPYGSLNPRKkvgqileepllintSLSAAERREKALAMMAkvglrpEHY-----DR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 820872358 134 LGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDpISV 173
Cdd:PRK11308 151 YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD-VSV 189
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-205 |
1.18e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 49.07 E-value: 1.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 17 QVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGlvqADQGRVLIDNLDVSHQPMHGRARAGI-GYLPQEASIFRKLSV 95
Cdd:PLN03140 894 QLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG---RKTGGYIEGDIRISGFPKKQETFARIsGYCEQNDIHSPQVTV 970
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 96 ADNIM--AILETRKELDREGRRKELESLLQEFHISHIRDNL----GMS-LSGGERRRVEIARALATAPKFILLDEPFAGV 168
Cdd:PLN03140 971 RESLIysAFLRLPKEVSKEEKMMFVDEVMELVELDNLKDAIvglpGVTgLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
|
170 180 190
....*....|....*....|....*....|....*..
gi 820872358 169 DPISVGDIKQIIHHLKAKGIGVLITDHnvRETLDICE 205
Cdd:PLN03140 1051 DARAAAIVMRTVRNTVDTGRTVVCTIH--QPSIDIFE 1085
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
16-195 |
2.19e-06 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 48.18 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVqaDQGRVLIDNLDVSHQPMHGRARAGIGY------------- 82
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERV--TTGVITGGDRLVNGRPLDSSFQRSIGYvqqqdlhlptstv 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 83 -----------LPQEASIFRKLSVADNIMAILETRKELDRegrrkelesllqefhishIRDNLGMSLSGGERRRVEIARA 151
Cdd:TIGR00956 854 reslrfsaylrQPKSVSKSEKMEYVEEVIKLLEMESYADA------------------VVGVPGEGLNVEQRKRLTIGVE 915
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 820872358 152 LATAPKFIL-LDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDH 195
Cdd:TIGR00956 916 LVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
138-219 |
2.23e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 48.10 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 138 LSGGERRRVEIARALA---TAPKFILLDEP-----FAgvdpisvgDIKQ---IIHHLKAKGIGVLITDHNvretLDICET 206
Cdd:COG0178 827 LSGGEAQRVKLASELSkrsTGKTLYILDEPttglhFH--------DIRKlleVLHRLVDKGNTVVVIEHN----LDVIKT 894
|
90 100
....*....|....*....|..
gi 820872358 207 A-YIV--------NDGQLIAEG 219
Cdd:COG0178 895 AdWIIdlgpeggdGGGEIVAEG 916
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-169 |
2.55e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 48.20 E-value: 2.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 16 RQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVG-LVQADQGRVLIdnldvshqpmhgraRAGIGYLPQEASIFRKlS 94
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVI--------------RGTVAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 95 VADNIMAILE---TR--KELDREGRRKELEsLLQEFHISHIRDNlGMSLSGGERRRVEIARALATAPKFILLDEPFAGVD 169
Cdd:PLN03130 695 VRDNILFGSPfdpERyeRAIDVTALQHDLD-LLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-184 |
3.22e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 47.72 E-value: 3.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 14 KGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNldvSHQPMHGRA---RAGIGYLPQEASIF 90
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIND---SHNLKDINLkwwRSKIGVVSQDPLLF 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 91 RKlSVADNIMAILETRKEL----------------DREGR--------------------------RKELES-------- 120
Cdd:PTZ00265 473 SN-SIKNNIKYSLYSLKDLealsnyynedgndsqeNKNKRnscrakcagdlndmsnttdsneliemRKNYQTikdsevvd 551
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 820872358 121 -----LLQEFhISHIRDNL-------GMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLK 184
Cdd:PTZ00265 552 vskkvLIHDF-VSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLK 626
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
138-219 |
4.56e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 46.99 E-value: 4.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 138 LSGGERRRVEIARAL---ATAPKFILLDEPFAGvdpISVGDIKQ---IIHHLKAKGIGVLITDHNvretLDICETA-YIV 210
Cdd:PRK00349 831 LSGGEAQRVKLAKELskrSTGKTLYILDEPTTG---LHFEDIRKlleVLHRLVDKGNTVVVIEHN----LDVIKTAdWII 903
|
90
....*....|....*..
gi 820872358 211 --------NDGQLIAEG 219
Cdd:PRK00349 904 dlgpeggdGGGEIVATG 920
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-187 |
5.72e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.55 E-value: 5.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGlvqaD--QGRVlidnldvSHQPMHGRARAG---------- 79
Cdd:PRK10938 269 SYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG----DhpQGYS-------NDLTLFGRRRGSgetiwdikkh 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 80 IGYLPQE----------------------ASIFRKLSVADNIMAiletRKELDREGRRKELESllQEFHishirdnlgmS 137
Cdd:PRK10938 338 IGYVSSSlhldyrvstsvrnvilsgffdsIGIYQAVSDRQQKLA----QQWLDILGIDKRTAD--APFH----------S 401
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 820872358 138 LSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKG 187
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEG 451
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
4-220 |
7.90e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.55 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGL--VQADQGRVLIDNLDVSHQPMHGRARAGI- 80
Cdd:PRK09580 2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIf 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 ---GYLPQEASIFRKLSVADNIMAILETRKE--LDREGRRKELESLLQEFHISH--IRDNLGMSLSGGERRRVEIARALA 153
Cdd:PRK09580 82 mafQYPVEIPGVSNQFFLQTALNAVRSYRGQepLDRFDFQDLMEEKIALLKMPEdlLTRSVNVGFSGGEKKRNDILQMAV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 820872358 154 TAPKFILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVReTLDICETAY--IVNDGQLIAEGD 220
Cdd:PRK09580 162 LEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQR-ILDYIKPDYvhVLYQGRIVKSGD 229
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-197 |
1.09e-05 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 44.49 E-value: 1.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 26 IDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHgraragigylpqeasifrklsvadnimailet 105
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKPQY-------------------------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 106 rkeldregrrkelesllqefhishirdnlgMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIHHLKA 185
Cdd:cd03222 70 ------------------------------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSE 119
|
170
....*....|...
gi 820872358 186 KGI-GVLITDHNV 197
Cdd:cd03222 120 EGKkTALVVEHDL 132
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
4-215 |
1.86e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 45.16 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 4 LKAQHLAKSYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVlidnldvshqpmhGRARaGI--G 81
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEI-------------GLAK-GIklG 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 82 YLPQEASIFRKlsvADNimailETRKELDREGRRkELESLLQE------FHISHIRDNLGmSLSGGERRRVEIARALATA 155
Cdd:PRK10636 379 YFAQHQLEFLR---ADE-----SPLQHLARLAPQ-ELEQKLRDylggfgFQGDKVTEETR-RFSGGEKARLVLALIVWQR 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 820872358 156 PKFILLDEPFAGVDPisvgDIKQIIHHLKAKGIGVLIT----DHNVRETLDiceTAYIVNDGQL 215
Cdd:PRK10636 449 PNLLLLDEPTNHLDL----DMRQALTEALIDFEGALVVvshdRHLLRSTTD---DLYLVHDGKV 505
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
21-163 |
1.89e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 44.09 E-value: 1.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVS--HQPMHGRARAGIGyLPQEASIFRKLSVADN 98
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINniAKPYCTYIGHNLG-LKLEMTVFENLKFWSE 96
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 99 IMAILETrkeldregrrkeLESLLQEFHISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDE 163
Cdd:PRK13541 97 IYNSAET------------LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
136-196 |
2.50e-05 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 43.12 E-value: 2.50e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 136 MSLSGGERRRVEIARALATAPK----FILLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHN 196
Cdd:cd03227 76 LQLSGGEKELSALALILALASLkprpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHL 140
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
19-213 |
3.13e-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: 43.08 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 19 VRDVSLSIDSGQIVGLLGPNGAGKTT----CFY-----MIVGLVQA---------DQGRVLIDNldvshqpmhgraraGI 80
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTlvneGLYasgkaRLISFLPKfsrnklifiDQLQFLIDV--------------GL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 81 GYLPQEasifRKLSvadnimailetrkeldregrrkelesllqefhishirdnlgmSLSGGERRRVEIARALATAPK--F 158
Cdd:cd03238 77 GYLTLG----QKLS------------------------------------------TLSGGELQRVKLASELFSEPPgtL 110
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 820872358 159 ILLDEPFAGVDPIsvgDIKQIIHHLKA---KGIGVLITDHNVREtldICETAYIVNDG 213
Cdd:cd03238 111 FILDEPSTGLHQQ---DINQLLEVIKGlidLGNTVILIEHNLDV---LSSADWIIDFG 162
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
14-164 |
4.69e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.01 E-value: 4.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 14 KGRQVVRD-VSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDN---LDVSHQPMHGRARAGIGYLPQEASI 89
Cdd:PRK10636 11 RGVRVLLDnATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqLAWVNQETPALPQPALEYVIDGDRE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 90 FRKLSVADNIM-------AILETRKELDREGR---RKELESLLQEFHISHIR-DNLGMSLSGGERRRVEIARALATAPKF 158
Cdd:PRK10636 91 YRQLEAQLHDAnerndghAIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQlERPVSDFSGGWRMRLNLAQALICRSDL 170
|
....*.
gi 820872358 159 ILLDEP 164
Cdd:PRK10636 171 LLLDEP 176
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-202 |
1.77e-04 |
|
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: 40.82 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 28 SGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIDNLDVSHQPMHGRARAgigylpqeasifrklsvadnimailetrk 107
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLL----------------------------- 51
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 108 eldregrrkelesllqefhisHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDIKQIIH------ 181
Cdd:smart00382 52 ---------------------IIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllll 110
|
170 180
....*....|....*....|.
gi 820872358 182 HLKAKGIGVLITDHNVRETLD 202
Cdd:smart00382 111 LKSEKNLTVILTTNDEKDLGP 131
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-197 |
2.54e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.12 E-value: 2.54e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 137 SLSGGERRRVEIARALATA---PKFILLDEPFAGvdpISVGDIKQIIHHLKA---KGIGVLITDHNV 197
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTG---LHTHDIKALIYVLQSlthQGHTVVIIEHNM 872
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-225 |
2.76e-04 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 40.95 E-value: 2.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVlidnldvshqPMHGRaragIGYLPQEASIFRKLSVADNIm 100
Cdd:PRK13546 42 DISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKV----------DRNGE----VSVIAISAGLSGQLTGIENI- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 101 aileTRKELDREGRRKELESLLQEF-HISHIRDNLGMSL---SGGERRRVEIARALATAPKFILLDEpfagvdPISVGDI 176
Cdd:PRK13546 107 ----EFKMLCMGFKRKEIKAMTPKIiEFSELGEFIYQPVkkySSGMRAKLGFSINITVNPDILVIDE------ALSVGDQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 820872358 177 K------QIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTIL 225
Cdd:PRK13546 177 TfaqkclDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
214-238 |
2.93e-04 |
|
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: 37.23 E-value: 2.93e-04
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-232 |
3.75e-04 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 41.03 E-value: 3.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 21 DVSLSIDSGQIVGLLGPNGAGKTTCFYMIVGLVQADQGRVLIdnldvshqpmhgraRAGIGYLPQEASIFRKLSVADNI- 99
Cdd:PRK13545 42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI--------------KGSAALIAISSGLNGQLTGIENIe 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 100 -----MAIleTRKELdregrrKELESLLQEF-HISHIRDNLGMSLSGGERRRVEIARALATAPKFILLDEpfagvdPISV 173
Cdd:PRK13545 108 lkglmMGL--TKEKI------KEIIPEIIEFaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDE------ALSV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 820872358 174 GDIK------QIIHHLKAKGIGVLITDHNVRETLDICETAYIVNDGQLIAEGDAQTILAN--ELVKE 232
Cdd:PRK13545 174 GDQTftkkclDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDHydEFLKK 240
|
|
| ABC_MutS2 |
cd03280 |
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS ... |
5-195 |
3.98e-04 |
|
ATP-binding cassette domain of MutS2; MutS2 homologs in bacteria and eukaryotes. The MutS protein initiates DNA mismatch repair by recognizing mispaired and unpaired bases embedded in duplex DNA and activating endo- and exonucleases to remove the mismatch. Members of the MutS family also possess a conserved ATPase activity that belongs to the ATP binding cassette (ABC) superfamily. MutS homologs (MSH) have been identified in most prokaryotic and all eukaryotic organisms examined. Prokaryotes have two homologs (MutS1 and MutS2), whereas seven MSH proteins (MSH1 to MSH7) have been identified in eukaryotes. The homodimer MutS1 and heterodimers MSH2-MSH3 and MSH2-MSH6 are primarily involved in mitotic mismatch repair, whereas MSH4-MSH5 is involved in resolution of Holliday junctions during meiosis. All members of the MutS family contain the highly conserved Walker A/B ATPase domain, and many share a common mechanism of action. MutS1, MSH2-MSH3, MSH2-MSH6, and MSH4-MSH5 dimerize to form sliding clamps, and recognition of specific DNA structures or lesions results in ADP/ATP exchange.
Pssm-ID: 213247 [Multi-domain] Cd Length: 200 Bit Score: 40.31 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 5 KAQHLAKSYKGRQVVrDVSLSIDSG-QIVGLLGPNGAGKTTCFyMIVGLVQAdqgrvlidnldvshqpMhgrARAGIgYL 83
Cdd:cd03280 4 EARHPLLPLQGEKVV-PLDIQLGENkRVLVITGPNAGGKTVTL-KTLGLLTL----------------M---AQSGL-PI 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 84 PQEASifRKLSVADNIMAILetrkeldreGRRKELESLLQEF--HISHIRdnlgmslsggerrrvEIARAlATAPKFILL 161
Cdd:cd03280 62 PAAEG--SSLPVFENIFADI---------GDEQSIEQSLSTFssHMKNIA---------------RILQH-ADPDSLVLL 114
|
170 180 190
....*....|....*....|....*....|....*
gi 820872358 162 DEPFAGVDPISVGDIKQ-IIHHLKAKGIGVLITDH 195
Cdd:cd03280 115 DELGSGTDPVEGAALAIaILEELLERGALVIATTH 149
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-238 |
5.36e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 5.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 137 SLSGGERRRVEIARALATAPKFI--LLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHNVR------ETLDICETAY 208
Cdd:PRK00635 476 TLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQmisladRIIDIGPGAG 555
|
90 100 110
....*....|....*....|....*....|.
gi 820872358 209 IVNdGQLIAEGDAQTILAN-ELVKEVYLGHE 238
Cdd:PRK00635 556 IFG-GEVLFNGSPREFLAKsDSLTAKYLRQE 585
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
12-164 |
5.29e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 37.92 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 12 SYKGRQVVRDVSLSIDSGQIVGLLGPNGAGKTTCF-YM----IVGL------------VQADQGRVL--IDNLDVSH-QP 71
Cdd:PLN03073 186 SVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrYMamhaIDGIpkncqilhveqeVVGDDTTALqcVLNTDIERtQL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 72 MHGRAR-------------AGIGYLPQEASIfRKLSVADNIMAILETRKELDREGRRKELESLLQEFHIS-HIRDNLGMS 137
Cdd:PLN03073 266 LEEEAQlvaqqrelefeteTGKGKGANKDGV-DKDAVSQRLEEIYKRLELIDAYTAEARAASILAGLSFTpEMQVKATKT 344
|
170 180
....*....|....*....|....*..
gi 820872358 138 LSGGERRRVEIARALATAPKFILLDEP 164
Cdd:PLN03073 345 FSGGWRMRIALARALFIEPDLLLLDEP 371
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
11-184 |
5.37e-03 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 36.91 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 11 KSYKGRQVVRdvslsIDSGqIVGLLGPNGAGKTT-------CFY--------MIVGLVQADQGRVLIDnLDVSHQP---- 71
Cdd:COG0419 11 RSYRDTETID-----FDDG-LNLIVGPNGAGKSTileairyALYgkarsrskLRSDLINVGSEEASVE-LEFEHGGkryr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 72 ---MHGRARAGIGYLPQE-ASIFRKLSVADNIMAILETRKELDREGRRK-----ELESLLQE-FHISHIRDNLGmSLSGG 141
Cdd:COG0419 84 ierRQGEFAEFLEAKPSErKEALKRLLGLEIYEELKERLKELEEALESAleelaELQKLKQEiLAQLSGLDPIE-TLSGG 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 820872358 142 ERRRVEIARALAtapkfILLDepFAGVDPISVGDIKQIIHHLK 184
Cdd:COG0419 163 ERLRLALADLLS-----LILD--FGSLDEERLERLLDALEELA 198
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
136-195 |
6.66e-03 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 36.85 E-value: 6.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 136 MSLSGGERRRVEIARALATAPKFIL--LDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDH 195
Cdd:cd03270 136 PTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEH 197
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
132-226 |
7.92e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.13 E-value: 7.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 820872358 132 DNLGMSLSGGERRRVEIARALATAPKFILLDEPFAGVDPISVGDI----KQIIHHLKAKGIGVLItdHNVRETLDICETA 207
Cdd:PLN03140 331 DEMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIvkclQQIVHLTEATVLMSLL--QPAPETFDLFDDI 408
|
90
....*....|....*....
gi 820872358 208 YIVNDGQLIAEGDAQTILA 226
Cdd:PLN03140 409 ILLSEGQIVYQGPRDHILE 427
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-196 |
8.36e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 37.12 E-value: 8.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 820872358 137 SLSGGERRRVEIARALATAPKFI--LLDEPFAGVDPISVGDIKQIIHHLKAKGIGVLITDHN 196
Cdd:PRK00635 1387 TLSDGEHYRLHLAKKISSNLTDIiyLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRS 1448
|
|
| |
