|
Name |
Accession |
Description |
Interval |
E-value |
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-236 |
4.80e-146 |
|
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: 406.68 E-value: 4.80e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGL 80
Cdd:COG0410 1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTVMENLEMGAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLL 160
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELFPRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 161 DEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAYLGG 236
Cdd:COG0410 161 DEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLGV 236
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-225 |
7.46e-126 |
|
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: 355.20 E-value: 7.46e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQV 83
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMGAFLKKnREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARR-RAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 164 SMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:cd03224 160 SEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-236 |
5.17e-98 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 285.62 E-value: 5.17e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGL 80
Cdd:PRK11614 3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREAV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTVMENLEMGAFLKKnREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLL 160
Cdd:PRK11614 83 AIVPEGRRVFSRMTVEENLAMGGFFAE-RDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 161 DEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAYLGG 236
Cdd:PRK11614 162 DEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLGG 237
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-236 |
1.34e-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: 229.15 E-value: 1.34e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGL 80
Cdd:COG0411 2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 S---QVPegrHVFPGLTVMENLEMGAF-------------LKKNREENQANLKKVFS--RFPRLEERKNQDAATLSGGEQ 142
Cdd:COG0411 82 ArtfQNP---RLFPELTVLENVLVAAHarlgrgllaallrLPRARREEREARERAEEllERVGLADRADEPAGNLSYGQQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 143 QMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGK 221
Cdd:COG0411 159 RRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPA 238
|
250
....*....|....*
gi 444285220 222 ELASSEEVRKAYLGG 236
Cdd:COG0411 239 EVRADPRVIEAYLGE 253
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-229 |
6.83e-69 |
|
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: 211.53 E-value: 6.83e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLS-- 81
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGrt 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 -QVPEgrhVFPGLTVMENLEMGA--------FLKKNREENQANLKKVFS--RFPRLEERKNQDAATLSGGEQQMLAMGRA 150
Cdd:cd03219 81 fQIPR---LFPELTVLENVMVAAqartgsglLLARARREEREARERAEEllERVGLADLADRPAGELSYGQQRRLEIARA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 151 LMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEV 229
Cdd:cd03219 158 LATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-235 |
3.19e-63 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 197.17 E-value: 3.19e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMP----AQKiv 76
Cdd:COG1137 1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrARL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 agGLSQVPEGRHVFPGLTVMEN----LEMgafLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALM 152
Cdd:COG1137 79 --GIGYLPQEASIFRKLTVEDNilavLEL---RKLSKKEREERLEELLEEF-GITHLRKSKAYSLSGGERRRVEIARALA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 153 STPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKA 232
Cdd:COG1137 153 TNPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKV 232
|
...
gi 444285220 233 YLG 235
Cdd:COG1137 233 YLG 235
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-229 |
2.73e-62 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 194.51 E-value: 2.73e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA---QKIvagGL 80
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAevrRRI---GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 sqVPEGRHVFPGLTVMENLE-MGAFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:COG1131 78 --VPQEPALYPDLTVRENLRfFARLYGLPRKEARERIDELLELF-GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLI 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 160 LDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASS--EEV 229
Cdd:COG1131 155 LDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARllEDV 226
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
4-235 |
3.77e-62 |
|
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: 193.91 E-value: 3.77e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQV 83
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMGA-FLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLeIRGLSKKEREEKLEELLEEF-HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDE 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAYLG 235
Cdd:cd03218 160 PFAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
4-235 |
2.08e-57 |
|
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: 182.09 E-value: 2.08e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQV 83
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLE-----MGAFLKKNREENQANLKKVFSrfprLEERKNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMavleiRKDLDRAEREERLEALLEEFQ----ISHLRDNKAMSLSGGERRRVEIARALATNPKFI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 159 LLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAYLG 235
Cdd:TIGR04406 158 LLDEPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLG 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
3-234 |
6.19e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 178.51 E-value: 6.19e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkiVAGGLSQ 82
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE--ARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEM-GAFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYfAELYGLFDEELKKRIEELIELL-GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLD 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASS---EEVRKAYL 234
Cdd:COG4555 158 EPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEigeENLEDAFV 233
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-233 |
2.74e-52 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 169.45 E-value: 2.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvAGGLSQ 82
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL-ARRIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMG-----AFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKL 157
Cdd:COG1120 80 VPQEPPAPFGLTVRELVALGryphlGLFGRPSAEDREAVEEALERT-GLEHLADRPVDELSGGERQRVLIARALAQEPPL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 158 LLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAY 233
Cdd:COG1120 159 LLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY 235
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-214 |
1.13e-51 |
|
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: 165.26 E-value: 1.13e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkiVAGGLSQV 83
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEE--VKRRIGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEmgaflkknreenqanlkkvfsrfprleerknqdaatLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 444285220 164 SMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
3-235 |
3.61e-51 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 166.70 E-value: 3.61e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQ 82
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENL-----------------EMGAFLKKNRE--ENQAN-LKKVfsrfpRLEERKNQDAATLSGGEQ 142
Cdd:PRK11300 85 TFQHVRLFREMTVIENLlvaqhqqlktglfsgllKTPAFRRAESEalDRAATwLERV-----GLLEHANRQAGNLAYGQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 143 QMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGK 221
Cdd:PRK11300 160 RRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPE 239
|
250
....*....|....
gi 444285220 222 ELASSEEVRKAYLG 235
Cdd:PRK11300 240 EIRNNPDVIKAYLG 253
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-233 |
2.17e-50 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 164.49 E-value: 2.17e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKmPAQKIvaGGL 80
Cdd:COG1121 4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-ARRRI--GYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPgLTVMENLEMG------AFLKKNREENQA---NLKKVfsrfpRLEERKNQDAATLSGGEQQ--MLAmgR 149
Cdd:COG1121 81 PQRAEVDWDFP-ITVRDVVLMGrygrrgLFRRPSRADREAvdeALERV-----GLEDLADRPIGELSGGQQQrvLLA--R 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 150 ALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLEtGKIVLSGTGKELASSEEV 229
Cdd:COG1121 153 ALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPENL 231
|
....
gi 444285220 230 RKAY 233
Cdd:COG1121 232 SRAY 235
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-232 |
7.45e-50 |
|
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: 162.50 E-value: 7.45e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVagglsq 82
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 vpegRHV-----FP-----GLTVMENLemgAF----LKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMG 148
Cdd:COG1122 75 ----RKVglvfqNPddqlfAPTVEEDV---AFgpenLGLPREEIRERVEEALELV-GLEHLADRPPHELSGGQKQRVAIA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 149 RALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEE 228
Cdd:COG1122 147 GVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226
|
....
gi 444285220 229 VRKA 232
Cdd:COG1122 227 LLEE 230
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-218 |
2.30e-48 |
|
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: 158.07 E-value: 2.30e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaGGLSQV 83
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER---RNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMG-AFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGlKLRGVPKAEIRARVRELLELV-GLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03259 157 PLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
5-213 |
7.25e-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: 156.86 E-value: 7.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 5 KVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKI--VAGGL 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELrrKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEgrHVFPGLTVMENLemgAF----LKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPK 156
Cdd:cd03225 81 FQNPD--DQFFGPTVEEEV---AFglenLGLPEEEIEERVEEALELV-GLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 157 LLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGK 213
Cdd:cd03225 155 ILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-214 |
3.54e-47 |
|
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: 155.34 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGM----IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQK---IV 76
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaaFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 AGGLSQVPEGRHVFPGLTVMENLEMGAFL-KKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLaGVPKKERRERAEELLERV-GLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 156 KLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKAlAISDRGYVLETGKI 214
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-213 |
4.87e-46 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 151.19 E-value: 4.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM----PAQKIVAGG 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLedelPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPEgrhVFPGLTVMENLEMGaflkknreenqanlkkvfsrfprleerknqdaatLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:cd03229 81 VFQDFA---LFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLL 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 160 LDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGK 213
Cdd:cd03229 124 LDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
5-218 |
1.50e-45 |
|
ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.
Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 151.15 E-value: 1.50e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 5 KVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkivAGGLSQVP 84
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 85 EGRHVFPgLTVMENLEMGAFLKKN---------REENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:cd03235 78 SIDRDFP-ISVRDVVLMGLYGHKGlfrrlskadKAKVDEALERV-----GLSELADRQIGELSGGQQQRVLLARALVQDP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 156 KLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRgYVLETGKIVLSG 218
Cdd:cd03235 152 DLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-233 |
1.87e-45 |
|
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: 151.57 E-value: 1.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG-MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA----- 77
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrqi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQvpeGRHVFPGLTVMENLEMGAFLKKNreenqaNLKKVFSRFPR--------------LEERKNQDAATLSGGEQQ 143
Cdd:cd03256 81 GMIFQ---QFNLIERLSVLENVLSGRLGRRS------TWRSLFGLFPKeekqralaalervgLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 144 MLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKE 222
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
250
....*....|.
gi 444285220 223 LaSSEEVRKAY 233
Cdd:cd03256 232 L-TDEVLDEIY 241
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-223 |
2.18e-45 |
|
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: 150.73 E-value: 2.18e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG--MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkiVAGGLS 81
Cdd:cd03263 1 LQIRNLTKTYKkgTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKA--ARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGLTVMENLEMGAFLK-KNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLL 160
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKgLPKSEIKEEVELLLRVL-GLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 161 DEPSMGLAPIFIQEIFDIIQDIqKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03263 158 DEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
2-215 |
3.06e-45 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 150.58 E-value: 3.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHYGM----IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKiva 77
Cdd:COG1136 3 PLLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERE--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 ggLSQVpegR-----------HVFPGLTVMENLEMGAFL-KKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQML 145
Cdd:COG1136 80 --LARL---RrrhigfvfqffNLLPELTALENVALPLLLaGVSRKERRERARELLERV-GLGDRLDHRPSQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 146 AMGRALMSTPKLLLLDEPS------MGlapifiQEIFDIIQDIQKQ-GTTVLLIEQNaNKALAISDRGYVLETGKIV 215
Cdd:COG1136 154 AIARALVNRPKLILADEPTgnldskTG------EEVLELLRELNRElGTTIVMVTHD-PELAARADRVIRLRDGRIV 223
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-223 |
3.28e-45 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 154.10 E-value: 3.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaggl 80
Cdd:COG3842 3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 sqvpegRHV---------FPGLTVMEN----LEMGAFLKKNREE--NQAnLKKVfsrfpRLEERKNQDAATLSGGEQQML 145
Cdd:COG3842 77 ------RNVgmvfqdyalFPHLTVAENvafgLRMRGVPKAEIRArvAEL-LELV-----GLEGLADRYPHQLSGGQQQRV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 146 AMGRALMSTPKLLLLDEP----------SMglapifIQEIFDIiqdIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:COG3842 145 ALARALAPEPRVLLLDEPlsaldaklreEM------REELRRL---QRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
....*...
gi 444285220 216 LSGTGKEL 223
Cdd:COG3842 216 QVGTPEEI 223
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
4-218 |
4.58e-45 |
|
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: 149.67 E-value: 4.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQV 83
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEgrhVFPGLTVMENLEMGAFLKKNREENQANLKKVFSrfprLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:cd03268 81 PG---FYPNLTARENLRLLARLLGIRKKRIDEVLDVVG----LKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEP 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 164 SMGLAPIFIQEIFDIIQDIQKQGTTVLL-------IEQnankalaISDRGYVLETGKIVLSG 218
Cdd:cd03268 154 TNGLDPDGIKELRELILSLRDQGITVLIsshllseIQK-------VADRIGIINKGKLIEEG 208
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-215 |
1.08e-44 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 149.05 E-value: 1.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGM-IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAqkivagglS 81
Cdd:COG2884 1 MIRFENVSKRYPGgREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKR--------R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRH----VF------PGLTVMENLemgAF----LKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAM 147
Cdd:COG2884 73 EIPYLRRrigvVFqdfrllPDRTVYENV---ALplrvTGKSRKEIRRRVREVLDLV-GLSDKAKALPHELSGGEQQRVAI 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 148 GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVL-------LIEQNANKALAISDrgyvletGKIV 215
Cdd:COG2884 149 ARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLiathdleLVDRMPKRVLELED-------GRLV 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-233 |
1.86e-44 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 150.64 E-value: 1.86e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvaGGLsq 82
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRI--GYL-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 vPEGRHVFPGLTVMENLEMGAFLK-KNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:COG4152 77 -PEERGLYPKMKVGEQLVYLARLKgLSKAEAKRRADEWLERL-GLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIQKQGTTVL-------LIEQnankalaISDRGYVLETGKIVLSGTgkelasSEEVRKAY 233
Cdd:COG4152 155 EPFSGLDPVNVELLKDVIRELAAKGTTVIfsshqmeLVEE-------LCDRIVIINKGRKVLSGS------VDEIRRQF 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-218 |
3.84e-44 |
|
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.
Pssm-ID: 213233 [Multi-domain] Cd Length: 218 Bit Score: 147.51 E-value: 3.84e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkiVAG 78
Cdd:cd03266 1 MITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAE--ARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQVPEGRHVFPGLTVMENLE-MGAFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKL 157
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEyFAGLYGLKGDELTARLEELADRL-GMEELLDRRVGGFSTGMRQKVAIARALVHDPPV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285220 158 LLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03266 158 LLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-214 |
6.46e-44 |
|
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: 146.91 E-value: 6.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQ-KIVAGGLSQ 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNiNELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMG--AFLKKNREENQAN----LKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTPK 156
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLApiKVKGMSKAEAEERalelLEKV-----GLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 157 LLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:cd03262 156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-215 |
7.27e-44 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 147.27 E-value: 7.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA--QKIV 76
Cdd:cd03257 1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 AGGLSQVP-EGRHVF-PGLTVMENLE---MGAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRAL 151
Cdd:cd03257 81 RKEIQMVFqDPMSSLnPRMTIGEQIAeplRIHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
4-218 |
7.71e-44 |
|
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: 146.66 E-value: 7.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvaGGLsqv 83
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRI--GYL--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMGAFLKK-NREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGlKKEEARRRIDEWLERL-ELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03269 155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-227 |
9.56e-44 |
|
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: 147.05 E-value: 9.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA----- 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYElrrri 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 ------GGLsqvpegrhvFPGLTVMENLEMG--AFLKKNREE---------NQANLKKVFSRFPrleerknqdaATLSGG 140
Cdd:COG1127 85 gmlfqgGAL---------FDSLTVFENVAFPlrEHTDLSEAEirelvleklELVGLPGAADKMP----------SELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 141 EQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGT 219
Cdd:COG1127 146 MRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
....*...
gi 444285220 220 GKELASSE 227
Cdd:COG1127 226 PEELLASD 233
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-235 |
2.31e-43 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 146.42 E-value: 2.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLS 81
Cdd:COG4674 9 PILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 ---QVPEgrhVFPGLTVMENLEM---------GAFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGR 149
Cdd:COG4674 89 rkfQKPT---VFEELTVFENLELalkgdrgvfASLFARLTAEERDRIEEVLETI-GLTDKADRLAGLLSHGQKQWLEIGM 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 150 ALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIqKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEV 229
Cdd:COG4674 165 LLAQDPKLLLLDEPVAGMTDAETERTAELLKSL-AGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPRV 243
|
....*.
gi 444285220 230 RKAYLG 235
Cdd:COG4674 244 IEVYLG 249
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
3-223 |
4.05e-43 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 145.52 E-value: 4.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkivaggLSQ 82
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKD------INK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VpeGRHV---------FPGLTVMENLEMG--AFLKKNREENQAN----LKKVfsrfpRLEERKNQDAATLSGGEQQMLAM 147
Cdd:COG1126 75 L--RRKVgmvfqqfnlFPHLTVLENVTLApiKVKKMSKAEAEERamelLERV-----GLADKADAYPAQLSGGQQQRVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 148 GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:COG1126 148 ARALAMEPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEF 223
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
5-218 |
5.57e-43 |
|
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: 143.34 E-value: 5.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 5 KVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvAGGLSQVP 84
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL-ARKIAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 85 egrhvfpglTVMENLEMGAFlkknreenqanlkkvfsrfprleerKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:cd03214 80 ---------QALELLGLAHL-------------------------ADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 165 MGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03214 126 SHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
6-223 |
2.40e-42 |
|
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: 142.89 E-value: 2.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkiVAGGLSQVPE 85
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPRE--VRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 86 GRHVFPGLTVMENLEMGAFL----KKNREENQANLKKVFSrfprLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLygvpGAERRERIDELLDFVG----LLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLD 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIQK-QGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03265 157 EPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-232 |
3.76e-42 |
|
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: 143.41 E-value: 3.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGM----IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKmPAQKIVAG 78
Cdd:COG1124 1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTR-RRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLS---QVPEGRhVFPGLTVMENLE--MGAFLKKNREENQANL-------KKVFSRFPRleerknqdaaTLSGGEQQMLA 146
Cdd:COG1124 80 RVQmvfQDPYAS-LHPRHTVDRILAepLRIHGLPDREERIAELleqvglpPSFLDRYPH----------QLSGGQRQRVA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 147 MGRALMSTPKLLLLDEPSMGLAPIfIQ-EIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVlsgtgkELA 224
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVS-VQaEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV------EEL 221
|
....*...
gi 444285220 225 SSEEVRKA 232
Cdd:COG1124 222 TVADLLAG 229
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
1-235 |
1.06e-41 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 141.95 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGL 80
Cdd:PRK10895 1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTVMENLEMGAFLKK--NREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMAVLQIRDdlSAEQREDRANELMEEF-HIEHLRDSMGQSLSGGERRRVEIARALAANPKFI 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 159 LLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAYLG 235
Cdd:PRK10895 160 LLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLG 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-228 |
1.41e-41 |
|
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: 141.49 E-value: 1.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM-PAQKIVA----GGL 80
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLsEAELYRLrrrmGML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQvpeGRHVFPGLTVMENleMGAFLKKNREENQANLKKVFS---RFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKL 157
Cdd:cd03261 83 FQ---SGALFDSLTVFEN--VAFPLREHTRLSEEEIREIVLeklEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 158 LLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEE 228
Cdd:cd03261 158 LLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD 229
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-214 |
2.99e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 139.95 E-value: 2.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA----QKIVAgg 79
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPpewrRQVAY-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPegrHVFPGlTVMENLEMgAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:COG4619 79 VPQEP---ALWGG-TVRDNLPF-PFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 160 LDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-223 |
3.02e-41 |
|
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: 140.45 E-value: 3.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaGGLSQV 83
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHK---RPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMGAFLKK-NREENQANLKKVFsRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKlPKAEIKERVAEAL-DLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
5-213 |
4.01e-41 |
|
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: 137.76 E-value: 4.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 5 KVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaqkivagglsqvp 84
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 85 egrhvfpgltvmenlemgaflkknreeNQANLKKVFSRFprleerknQdaatLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:cd00267 68 ---------------------------LEELRRRIGYVP--------Q----LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 444285220 165 MGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGK 213
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
4-235 |
1.09e-40 |
|
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: 139.39 E-value: 1.09e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQaVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaGGLSQV 83
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEK---RDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMGafLKKNREENQANLKKV--FSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYG--LKKRKVDKKEIERKVleIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLD 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL---ASSEEVRKaYLG 235
Cdd:cd03299 155 EPFSALDVRTKEKLREELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVfkkPKNEFVAE-FLG 231
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-214 |
1.25e-40 |
|
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: 137.18 E-value: 1.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYgmiqAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQ 82
Cdd:cd03215 4 VLEVRGLSVKG----AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRH---VFPGLTVMENLEMGAFLkknreenqanlkkvfsrfprleerknqdaatlSGGEQQMLAMGRALMSTPKLLL 159
Cdd:cd03215 80 VPEDRKregLVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLI 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 160 LDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:cd03215 128 LDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-223 |
1.38e-40 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 145.43 E-value: 1.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MS-MLKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPS---SGKIEFLGQEIQKMPAQK 74
Cdd:COG1123 1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 75 I--VAGGLSQVPEGRhvFPGLTVMENLEMGAFLKK-NREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRAL 151
Cdd:COG1123 81 RgrRIGMVFQDPMTQ--LNPVTVGDQIAEALENLGlSRAEARARVLELLEAV-GLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
3-191 |
1.68e-40 |
|
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: 138.00 E-value: 1.68e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkiVAGGLSQ 82
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED--YRRRLAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMGAFLkKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAAL-YGLRADREAIDEALEAV-GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180
....*....|....*....|....*....
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQGTTVLL 191
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLL 186
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-223 |
3.37e-40 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 144.01 E-value: 3.37e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQ 82
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAGIAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMGAFLKK----NREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:COG1129 84 IHQELNLVPNLSVAENIFLGREPRRggliDWRAMRRRARELLARL-GLDIDPDTPVGDLSVAQQQLVEIARALSRDARVL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 159 LLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLI-----EqnankALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:COG1129 163 ILDEPTASLTEREVERLFRIIRRLKAQGVAIIYIshrldE-----VFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-223 |
1.10e-39 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 142.73 E-value: 1.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGM-----IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA 77
Cdd:COG1123 260 LLEVRNLSKRYPVrgkggVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 gglsqvpEGRHV-----------FPGLTVMENLEMG--AFLKKNREENQAN----LKKV------FSRFPRleerknqda 134
Cdd:COG1123 340 -------LRRRVqmvfqdpysslNPRMTVGDIIAEPlrLHGLLSRAERRERvaelLERVglppdlADRYPH--------- 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 135 aTLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGK 213
Cdd:COG1123 404 -ELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGR 482
|
250
....*....|
gi 444285220 214 IVLSGTGKEL 223
Cdd:COG1123 483 IVEDGPTEEV 492
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-217 |
1.35e-39 |
|
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: 134.09 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQ-KMPAQKIVAGglsq 82
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSfASPRDARRAG---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 vpegrhvfpgltvmenLEMgaflkknreenqanlkkVFsrfprleerknQdaatLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:cd03216 77 ----------------IAM-----------------VY-----------Q----LSVGERQMVEIARALARNARLLILDE 108
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLS 217
Cdd:cd03216 109 PTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVGT 163
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
19-163 |
3.26e-39 |
|
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: 132.77 E-value: 3.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAqKIVAGGLSQVPEGRHVFPGLTVMEN 98
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDER-KSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 99 LEMGAFLKKN-REENQANLKKVFSRFPRLEERKN---QDAATLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:pfam00005 80 LRLGLLLKGLsKREKDARAEEALEKLGLGDLADRpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-223 |
2.15e-38 |
|
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: 133.07 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLV-----RPSSGKIEFLGQEIQKMPAQKIV-- 76
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 --AGGLSQVPegrHVFPGlTVMENLEMGAFL--KKNREENQANLKKVFSRFPRLEERKNQ-DAATLSGGEQQMLAMGRAL 151
Cdd:cd03260 81 rrVGMVFQKP---NPFPG-SIYDNVAYGLRLhgIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQgTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-215 |
3.21e-38 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 133.68 E-value: 3.21e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIV 76
Cdd:COG1116 5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 agglsqVPEGRHVFPGLTVMENLEMGA-FLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:COG1116 85 ------VFQEPALLPWLTVLDNVALGLeLRGVPKAERRERARELLELV-GLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 156 KLLLLDEP----------SMGlapifiQEIFDIiqdIQKQGTTVLLIEQNANKALAISDRGYVLET--GKIV 215
Cdd:COG1116 158 EVLLMDEPfgaldaltreRLQ------DELLRL---WQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-209 |
3.50e-38 |
|
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: 132.21 E-value: 3.50e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG----MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVagg 79
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRGY--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 lsqVPEGRHVFPGLTVMENLEMGAFLKKN-----REENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMST 154
Cdd:cd03293 78 ---VFQQDALLPWLTVLDNVALGLELQGVpkaeaRERAEELLELV-----GLSGFENAYPHQLSGGMRQRVALARALAVD 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVL 209
Cdd:cd03293 150 PDVLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-236 |
9.58e-37 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 134.76 E-value: 9.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHygmiQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQ-KMPAQKIvAGGLS 81
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRiRSPRDAI-RAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRH---VFPGLTVMENLEMGA--------FLKKNREENQAN--LKKVFSRFPRLEerknQDAATLSGGEQQMLAMG 148
Cdd:COG1129 331 YVPEDRKgegLVLDLSIRENITLASldrlsrggLLDRRRERALAEeyIKRLRIKTPSPE----QPVGNLSGGNQQKVVLA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 149 RALMSTPKLLLLDEPSMGlapifI-----QEIFDIIQDIQKQGTTVLLI-----EqnankALAISDRGYVLETGKIVLSG 218
Cdd:COG1129 407 KWLATDPKVLILDEPTRG-----IdvgakAEIYRLIRELAAEGKAVIVIsselpE-----LLGLSDRILVMREGRIVGEL 476
|
250
....*....|....*...
gi 444285220 219 TGKElASSEEVRKAYLGG 236
Cdd:COG1129 477 DREE-ATEEAIMAAATGG 493
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-223 |
1.18e-36 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 131.81 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSmLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQ-KMPAQKivagg 79
Cdd:COG1118 1 MS-IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLPPRE----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 lsqvpegRHV---------FPGLTVMENLemgAF----LKKNREENQAN----LKKVfsrfpRLEERKNQDAATLSGGEQ 142
Cdd:COG1118 75 -------RRVgfvfqhyalFPHMTVAENI---AFglrvRPPSKAEIRARveelLELV-----QLEGLADRYPSQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 143 QMLAMGRALMSTPKLLLLDEPsMG-----LAPIFIQEIFDIIQDIqkQGTTVL----LIEqnankALAISDRGYVLETGK 213
Cdd:COG1118 140 QRVALARALAVEPEVLLLDEP-FGaldakVRKELRRWLRRLHDEL--GGTTVFvthdQEE-----ALELADRVVVMNQGR 211
|
250
....*....|
gi 444285220 214 IVLSGTGKEL 223
Cdd:COG1118 212 IEQVGTPDEV 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-219 |
3.65e-36 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 127.82 E-value: 3.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSmLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQE--IQKMPAQKIVAG 78
Cdd:PRK11124 1 MS-IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 gLSQ----VPEGRHVFPGLTVMENLeMGA---FLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRAL 151
Cdd:PRK11124 80 -LRRnvgmVFQQYNLWPHLTVQQNL-IEApcrVLGLSKDQALARAEKLLERL-RLKPYADRFPLHLSGGQQQRVAIARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGT 219
Cdd:PRK11124 157 MMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
4-224 |
4.61e-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: 133.74 E-value: 4.61e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKI--VAGG 79
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLrrRIAV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPegrHVFPGlTVMENL----------EMGAFLKknreenQANLKKVFSRFP-----RLEErknqDAATLSGGEQQM 144
Cdd:COG4987 414 VPQRP---HLFDT-TLRENLrlarpdatdeELWAALE------RVGLGDWLAALPdgldtWLGE----GGRRLSGGERRR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 145 LAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDiQKQGTTVLLIEQNANkALAISDRGYVLETGKIVLSGTGKELA 224
Cdd:COG4987 480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLA-GLERMDRILVLEDGRIVEQGTHEELL 557
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
3-233 |
4.97e-36 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 127.97 E-value: 4.97e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA--GGL 80
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARrrAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPegrHV-FPgLTVMENLEMGA-----FLKKNREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALM-- 152
Cdd:PRK13548 82 PQHS---SLsFP-FTVEEVVAMGRaphglSRAEDDALVAAALAQV-----DLAHLAGRDYPQLSGGEQQRVQLARVLAql 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 153 ----STPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSE 227
Cdd:PRK13548 153 wepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPE 232
|
....*.
gi 444285220 228 EVRKAY 233
Cdd:PRK13548 233 TLRRVY 238
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-223 |
5.55e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.81 E-value: 5.55e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaGGL 80
Cdd:COG3839 1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---RNI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTVMENLEMGAFLKK-NREENQANLKKVfSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:COG3839 78 AMVFQSYALYPHMTVYENIAFPLKLRKvPKAEIDRRVREA-AELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 160 LDEP----------SMglapifIQEIFDIIQDIqkqGTTVLL-----IEqnankALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:COG3839 157 LDEPlsnldaklrvEM------RAEIKRLHRRL---GTTTIYvthdqVE-----AMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
6-215 |
5.65e-36 |
|
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: 126.22 E-value: 5.65e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYG-MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKiVAGGLSQVP 84
Cdd:cd03226 2 IENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAKERRK-SIGYVMQDV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 85 eGRHVFpGLTVMENLEMGAFLKKNREENQANLKKVFSrfprLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:cd03226 81 -DYQLF-TDSVREELLLGLKELDAGNEQAETVLKDLD----LYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 444285220 165 MGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-227 |
6.22e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 133.34 E-value: 6.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvAGGL 80
Cdd:COG4988 335 PSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW-RRQI 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGlTVMENLEMGAFlKKNREE-----NQANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRALMST 154
Cdd:COG4988 414 AWVPQNPYLFAG-TIRENLRLGRP-DASDEEleaalEAAGLDEFVAALPDgLDTPLGEGGRGLSGGQAQRLALARALLRD 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDIqKQGTTVLLI---EQNANKAlaisDRGYVLETGKIVLSGTGKELASSE 227
Cdd:COG4988 492 APLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILIthrLALLAQA----DRILVLDDGRIVEQGTHEELLAKN 562
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
3-223 |
8.20e-36 |
|
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ABC-type transporter encoded by metN of the metNPQ operon in Bacillus subtilis that is involved in methionine transport. Other members of this system include the MetP permease and the MetQ substrate binding protein. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213225 [Multi-domain] Cd Length: 233 Bit Score: 126.54 E-value: 8.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYG----MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA- 77
Cdd:cd03258 1 MIELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 ----GGLSQvpeGRHVFPGLTVMEN----LEMGAFLKKNREENQANLKKvfsrFPRLEERKNQDAATLSGGEQQMLAMGR 149
Cdd:cd03258 81 rrriGMIFQ---HFNLLSSRTVFENvalpLEIAGVPKAEIEERVLELLE----LVGLEDKADAYPAQLSGGQKQRVGIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 150 ALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03258 154 ALANNPKVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
3-233 |
1.25e-35 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 126.77 E-value: 1.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaggLSQ 82
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWE-----LAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VpegRHVFP-------GLTVMENLEMGAF-LKKNREENQANLKKVFSRF--PRLEERKNQdaaTLSGGEQQMLAMGRAL- 151
Cdd:COG4559 76 R---RAVLPqhsslafPFTVEEVVALGRApHGSSAAQDRQIVREALALVglAHLAGRSYQ---TLSGGEQQRVQLARVLa 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 152 ------MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:COG4559 150 qlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
|
....*...
gi 444285220 226 SEEVRKAY 233
Cdd:COG4559 230 DELLERVY 237
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-223 |
2.01e-35 |
|
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: 125.91 E-value: 2.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSmLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGL 80
Cdd:cd03296 1 MS-IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQvpegrH--VFPGLTVMENLEMGAFLKKNREENQANL--KKVFS--RFPRLEERKNQDAATLSGGEQQMLAMGRALMST 154
Cdd:cd03296 80 FQ-----HyaLFRHMTVFDNVAFGLRVKPRSERPPEAEirAKVHEllKLVQLDWLADRYPAQLSGGQRQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 155 PKLLLLDEPSMGL-API------FIQEIFDiiqdiqKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03296 155 PKVLLLDEPFGALdAKVrkelrrWLRRLHD------ELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
2.55e-35 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 125.51 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSmLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEI---QKMPAQKIVA 77
Cdd:COG4161 1 MS-IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 --GGLSQVPEGRHVFPGLTVMENLEMGA--FLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMS 153
Cdd:COG4161 80 lrQKVGMVFQQYNLWPHLTVMENLIEAPckVLGLSKEQAREKAMKLLARL-RLTDKADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 154 TPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGT 219
Cdd:COG4161 159 EPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-222 |
4.57e-35 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 125.58 E-value: 4.57e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSV--HYGMI---QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvA 77
Cdd:COG1101 1 MLELKNLSKtfNPGTVnekRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKR-A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVpegrhvF--------PGLTVMENLEMG-----------AFLKKNREENQANLKkvfsRFPR-LEERKNQDAATL 137
Cdd:COG1101 80 KYIGRV------FqdpmmgtaPSMTIEENLALAyrrgkrrglrrGLTKKRRELFRELLA----TLGLgLENRLDTKVGLL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 138 SGGEQQMLAMGRALMSTPKLLLLDEPSMGLAP---IFIQEIFDIIqdIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPktaALVLELTEKI--VEENNLTTLMVTHNMEQALDYGNRLIMMHEGRI 227
|
....*...
gi 444285220 215 VLSGTGKE 222
Cdd:COG1101 228 ILDVSGEE 235
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-229 |
3.71e-34 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 124.40 E-value: 3.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRP---SSGKIEFLGQEIQKMPAQKi 75
Cdd:COG0444 1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 76 vaggLSQVpEGRH---VF--------PGLTV----MENLEmgAFLKKNREENQANLKKVFSR--FPRLEERKNQDAATLS 138
Cdd:COG0444 80 ----LRKI-RGREiqmIFqdpmtslnPVMTVgdqiAEPLR--IHGGLSKAEARERAIELLERvgLPDPERRLDRYPHELS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 139 GGEQQ--MLAMgrALMSTPKLLLLDEPSMGLAPIfIQ-EIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:COG0444 153 GGMRQrvMIAR--ALALEPKLLIADEPTTALDVT-IQaQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229
|
250
....*....|....*
gi 444285220 215 VlsgtgkELASSEEV 229
Cdd:COG0444 230 V------EEGPVEEL 238
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
3-204 |
8.15e-34 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 120.82 E-value: 8.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGM-IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA--GG 79
Cdd:TIGR02673 1 MIEFHNVSKAYPGgVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLlrRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPEGRHVFPGLTVMENLEM-----GAFLKKNREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMST 154
Cdd:TIGR02673 81 IGVVFQDFRLLPDRTVYENVALplevrGKKEREIQRRVGAALRQV-----GLEHKADAFPEQLSGGEQQRVAIARAIVNS 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVL-------LIEQNANKALAISD 204
Cdd:TIGR02673 156 PPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIvathdlsLVDRVAHRVIILDD 212
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-215 |
1.14e-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: 120.44 E-value: 1.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaGGLSQV 83
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD---RDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMGAFLKKNREENQAnlKKVFS--RFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEID--ERVREvaELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 162 EPSMGL-APIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:cd03301 156 EPLSNLdAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
4-213 |
3.01e-33 |
|
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: 117.87 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG--MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIVAGGLS 81
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD-LESLRKNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLemgaflkknreenqanlkkvfsrfprleerknqdaatLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:cd03228 80 YVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIqKQGTTVLLIEQNANkALAISDRGYVLETGK 213
Cdd:cd03228 122 EATSALDPETEALILEALRAL-AKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
18-223 |
4.00e-33 |
|
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: 120.44 E-value: 4.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA---QKIVAGGLSQVPEGRHVFPGLT 94
Cdd:cd03294 39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelRELRRKKISMVFQSFALLPHRT 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 95 VMEN----LEMGAFLKKNREENQAN-LKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAP 169
Cdd:cd03294 119 VLENvafgLEVQGVPRAEREERAAEaLELV-----GLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 170 IFIQEIFDIIQDIQ-KQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03294 194 LIRREMQDELLRLQaELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-215 |
5.01e-33 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 124.75 E-value: 5.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVH-YGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQ 82
Cdd:COG3845 258 LEVENLSVRdDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAY 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRH---VFPGLTVMENLEMGAFLKK--------NREENQANLKKVFSRF----PRLEERknqdAATLSGGEQQMLAM 147
Cdd:COG3845 338 IPEDRLgrgLVPDMSVAENLILGRYRRPpfsrggflDRKAIRAFAEELIEEFdvrtPGPDTP----ARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285220 148 GRALMSTPKLLLLDEPSMGL---ApifIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLdvgA---IEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
3-235 |
6.67e-33 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 119.09 E-value: 6.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYG--MIQAvrdvSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM-PAQKIVAGg 79
Cdd:COG3840 1 MLRLDDLTYRYGdfPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALpPAERPVSM- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQvpEGrHVFPGLTVMENLEMG--AFLKKNREENQA--------NLKKVFSRFPrleerknqdaATLSGGEQQMLAMGR 149
Cdd:COG3840 76 LFQ--EN-NLFPHLTVAQNIGLGlrPGLKLTAEQRAQveqalervGLAGLLDRLP----------GQLSGGQRQRVALAR 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 150 ALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQK-QGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSE- 227
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEp 222
|
....*....
gi 444285220 228 -EVRKAYLG 235
Cdd:COG3840 223 pPALAAYLG 231
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
4-169 |
7.40e-33 |
|
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: 118.06 E-value: 7.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGeVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIvAGGLSQV 83
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQP-QKL-RRRIGYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMGAFLK-----KNREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:cd03264 78 PQEFGVYPNFTVREFLDYIAWLKgipskEVKARVDEVLELV-----NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
|
170
....*....|.
gi 444285220 159 LLDEPSMGLAP 169
Cdd:cd03264 153 IVDEPTAGLDP 163
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-223 |
3.48e-32 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 119.94 E-value: 3.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVE--NLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIqkmPAQKIVA- 77
Cdd:PRK13536 37 MSTVAIDlaGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPV---PARARLAr 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRHVFPGLTVMENLEM-GAFLKKNREENQANLKKVFSrFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPK 156
Cdd:PRK13536 114 ARIGVVPQFDNLDLEFTVRENLLVfGRYFGMSTREIEAVIPSLLE-FARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 157 LLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-222 |
4.61e-32 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 120.05 E-value: 4.61e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaggl 80
Cdd:PRK09452 12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 sqvpegRHV---------FPGLTVMENLEMGAFLKKNREENQAnlKKVFS--RFPRLEERKNQDAATLSGGEQQMLAMGR 149
Cdd:PRK09452 86 ------RHVntvfqsyalFPHMTVFENVAFGLRMQKTPAAEIT--PRVMEalRMVQLEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285220 150 ALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKE 222
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPRE 231
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
4-223 |
9.81e-32 |
|
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: 122.25 E-value: 9.81e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG--MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkIVAGGLS 81
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPA-SLRRQIG 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEMGAfLKKNREE-----NQANLKKVFSRFP-----RLEERknqdAATLSGGEQQMLAMGRAL 151
Cdd:COG2274 553 VVLQDVFLFSG-TIRENITLGD-PDATDEEiieaaRLAGLHDFIEALPmgydtVVGEG----GSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIqKQGTTVLLIeqnANK--ALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:COG2274 627 LRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIII---AHRlsTIRLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
21-218 |
2.75e-31 |
|
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: 114.31 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEgEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQK------MPAQKIVAGGLSQvpeGRHVFPGLT 94
Cdd:cd03297 16 KIDFDLNE-EVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDsrkkinLPPQQRKIGLVFQ---QYALFPHLN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 95 VMENLEMGAFLKKNREENQAnLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQE 174
Cdd:cd03297 92 VRENLAFGLKRKRNREDRIS-VDELLDLL-GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 444285220 175 IFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03297 170 LLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-223 |
3.98e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 114.42 E-value: 3.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIqKMPAQKIV-----A 77
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERlirqeA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GglsQVPEGRHVFPGLTVMENLEMGAF----LKKNREENQAN--LKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRAL 151
Cdd:PRK09493 80 G---MVFQQFYLFPHLTALENVMFGPLrvrgASKEEAEKQARelLAKV-----GLAERAHHYPSELSGGQQQRVAIARAL 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK09493 152 AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-219 |
6.47e-31 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 116.33 E-value: 6.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA------ 72
Cdd:COG1135 1 MIELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSErelraa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 -QKIvagG--------LSQvpegRhvfpglTVMEN----LEMgafLKKNREENQanlKKVFS--RFPRLEERKNQDAATL 137
Cdd:COG1135 81 rRKI---GmifqhfnlLSS----R------TVAENvalpLEI---AGVPKAEIR---KRVAEllELVGLSDKADAYPSQL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 138 SGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLI--EQNANKALAisDRGYVLETGKI 214
Cdd:COG1135 142 SGGQKQRVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDInRELGLTIVLIthEMDVVRRIC--DRVAVLENGRI 219
|
....*
gi 444285220 215 VLSGT 219
Cdd:COG1135 220 VEQGP 224
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-227 |
3.17e-30 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.75 E-value: 3.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLsqV 83
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV--V 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEM-GAFLKKNREENQANLKKVFsRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:PRK13537 86 PQFDNLDPDFTVRENLLVfGRYFGLSAAAARALVPPLL-EFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSE 227
Cdd:PRK13537 165 PTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESE 229
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-215 |
6.56e-30 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 115.89 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQ-KMPAQKIVAG-G- 79
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRiRSPRDAIALGiGm 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQvpegrH--VFPGLTVMENLEMGA----FLKKNREENQANLKKVFSRFPrLEERKNQDAATLSGGEQQMLAMGRALMS 153
Cdd:COG3845 85 VHQ-----HfmLVPNLTVAENIVLGLeptkGGRLDRKAARARIRELSERYG-LDVDPDAKVEDLSVGEQQRVEILKALYR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 154 TPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:COG3845 159 GARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVV 220
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
4-223 |
8.81e-30 |
|
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: 111.24 E-value: 8.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQ-AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQK-------- 74
Cdd:cd03295 1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVElrrkigyv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 75 IVAGGLsqvpegrhvFPGLTVMENLEMGAFLKKNREENQANLKKVFSRFPRLEERKNQD--AATLSGGEQQMLAMGRALM 152
Cdd:cd03295 81 IQQIGL---------FPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEFADryPHELSGGQQQRVGVARALA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 153 STPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03295 152 ADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEI 223
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
14-214 |
1.04e-29 |
|
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: 110.19 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 14 GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKI--VAGGLSQVPEGRHVFP 91
Cdd:cd03292 12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIpyLRRKIGVVFQDFRLLP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 92 GLTVMEN--LEMGAFLKKNREENqanlKKVFSRFPR--LEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGL 167
Cdd:cd03292 92 DRNVYENvaFALEVTGVPPREIR----KRVPAALELvgLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 444285220 168 APIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:cd03292 168 DPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
2-215 |
1.27e-29 |
|
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: 110.60 E-value: 1.27e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIVA 77
Cdd:COG4181 7 PIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALD-EDARA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLsqvpeGRH---VF------PGLTVMEN----LEMgAFLKKNREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQM 144
Cdd:COG4181 86 RLR-----ARHvgfVFqsfqllPTLTALENvmlpLEL-AGRRDARARARALLERV-----GLGHRLDHYPAQLSGGEQQR 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 145 LAMGRALMSTPKLLLLDEPSMGL-----APIfIQEIFDIIQDiqkQGTTVLLIEQNANKAlAISDRGYVLETGKIV 215
Cdd:COG4181 155 VALARAFATEPAILFADEPTGNLdaatgEQI-IDLLFELNRE---RGTTLVLVTHDPALA-ARCDRVLRLRAGRLV 225
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-227 |
1.41e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 115.15 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQ 82
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMGafLKKnreeNQANLKKVFSRFPRLEERKNQD--AATLSGGEQQMLAMGRALMSTPKLLLL 160
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFG--LPK----RQASMQKMKQLLAALGCQLDLDssAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 161 DEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSE 227
Cdd:PRK15439 165 DEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDD 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-214 |
1.73e-29 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 114.76 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSvhyGmiQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQV 83
Cdd:PRK15439 269 LTVEDLT---G--EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVYL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFpGL-----------TVMENlEMGAFLKKNREenqanlKKVFSRFPRLE----ERKNQDAATLSGGEQQMLAMG 148
Cdd:PRK15439 344 PEDRQSS-GLyldaplawnvcALTHN-RRGFWIKPARE------NAVLERYRRALnikfNHAEQAARTLSGGNQQKVLIA 415
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 149 RALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:PRK15439 416 KCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
6-195 |
3.79e-29 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 108.47 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM---PAQKIVAGGLSQ 82
Cdd:TIGR03608 1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLnskKASKFRREKLGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMG-AFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:TIGR03608 81 LFQNFALIENETVEENLDLGlKYKKLSKKEKREKKKEALEKV-GLNLKLKQKIYELSGGEQQRVALARAILKPPPLILAD 159
|
170 180 190
....*....|....*....|....*....|....
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQN 195
Cdd:TIGR03608 160 EPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHD 193
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-223 |
6.56e-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: 6.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEI---QKMPAQKIVA 77
Cdd:PRK11264 1 MSAIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtaRSLSQQKGLI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQ----VPEGRHVFPGLTVMENLEMGAFLKKN--REENQANLKKVFSRFPrLEERKNQDAATLSGGEQQMLAMGRAL 151
Cdd:PRK11264 81 RQLRQhvgfVFQNFNLFPHRTVLENIIEGPVIVKGepKEEATARARELLAKVG-LAGKETSYPRRLSGGQQQRVAIARAL 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK11264 160 AMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-234 |
6.71e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 109.70 E-value: 6.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHYGMIQ--AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA-- 77
Cdd:PRK13632 6 VMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKki 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRhvFPGLTVMENLemgAFLKKNREENQANLKKVFSRFPR---LEERKNQDAATLSGGEQQMLAMGRALMST 154
Cdd:PRK13632 86 GIIFQNPDNQ--FIGATVEDDI---AFGLENKKVPPKKMKDIIDDLAKkvgMEDYLDKEPQNLSGGQKQRVAIASVLALN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGT-TVLLIEQNANKALaISDRGYVLETGKIVLSGTGKE-LASSEEVRKA 232
Cdd:PRK13632 161 PEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEiLNNKEILEKA 239
|
..
gi 444285220 233 YL 234
Cdd:PRK13632 240 KI 241
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
7.01e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 109.78 E-value: 7.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQK-----MPAQKIV 76
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYdkkslLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 aGGLSQVPEGRHVFPglTVMENLEMGAF-LKKNREENQANLKKVFSRFPrLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:PRK13639 81 -GIVFQNPDDQLFAP--TVEEDVAFGPLnLGLSKEEVEKRVKEALKAVG-MEGFENKPPHHLSGGQKKRVAIAGILAMKP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 156 KLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEE-VRKAYL 234
Cdd:PRK13639 157 EIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIEtIRKANL 236
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-218 |
1.23e-28 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 108.41 E-value: 1.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYG----MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIV 76
Cdd:COG4525 1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 agglsqvpegrhVF------PGLTVMENLEMGAFLKK-----NREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQML 145
Cdd:COG4525 81 ------------VFqkdallPWLNVLDNVAFGLRLRGvpkaeRRARAEELLALV-----GLADFARRRIWQLSGGMRQRV 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 146 AMGRALMSTPKLLLLDEPsMGLAPIF----IQEIfdIIQDIQKQGTTVLLIEQNANKALaisdrgyVLETGKIVLSG 218
Cdd:COG4525 144 GIARALAADPRFLLMDEP-FGALDALtreqMQEL--LLDVWQRTGKGVFLITHSVEEAL-------FLATRLVVMSP 210
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-236 |
1.56e-28 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 108.08 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVR--PS---SGKIEFLGQEIQKMPAQKI 75
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 76 V--AGGLSQVPegrHVFPGLTVMENLEMGAFLK---KNREENQANLKKVFSRFPRLEERKNQ---DAATLSGGEQQMLAM 147
Cdd:PRK14247 81 RrrVQMVFQIP---NPIPNLSIFENVALGLKLNrlvKSKKELQERVRWALEKAQLWDEVKDRldaPAGKLSGGQQQRLCI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 148 GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQgTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASS- 226
Cdd:PRK14247 158 ARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNp 236
|
250
....*....|.
gi 444285220 227 -EEVRKAYLGG 236
Cdd:PRK14247 237 rHELTEKYVTG 247
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-223 |
1.69e-28 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 107.31 E-value: 1.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 5 KVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIVAGGLSQV 83
Cdd:cd03254 4 EFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS-RKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGlTVMENLEMGAFLKKNREENQANLKKVFSRFPR-----LEERKNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:cd03254 83 LQDTFLFSG-TIMENIRLGRPNATDEEVIEAAKEAGAHDFIMklpngYDTVLGENGGNLSQGERQLLAIARAMLRDPKIL 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 159 LLDEPSMGLAPIFIQEIFDIIQDIQKQGTTV-----LLIEQNANKALaisdrgyVLETGKIVLSGTGKEL 223
Cdd:cd03254 162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIiiahrLSTIKNADKIL-------VLDDGKIIEEGTHDEL 224
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-230 |
2.65e-28 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.80 E-value: 2.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQ 82
Cdd:PRK09700 5 YISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMGAFL------------KKNREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRA 150
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLtkkvcgvniidwREMRVRAAMMLLRV-----GLKVDLDEKVANLSISHKQMLEIAKT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 151 LMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVR 230
Cdd:PRK09700 160 LMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR 239
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
3-163 |
2.96e-28 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 106.41 E-value: 2.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRP---SSGKIEFLGQEIQKMPAQKIVAGG 79
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPegrHVFPGLTVMENLEMG---AFLKKNREE------NQANLKKVFSRFPrleerknqdaATLSGGEQQMLAMGRA 150
Cdd:COG4136 81 LFQDD---LLFPHLSVGENLAFAlppTIGRAQRRArveqalEEAGLAGFADRDP----------ATLSGGQRARVALLRA 147
|
170
....*....|...
gi 444285220 151 LMSTPKLLLLDEP 163
Cdd:COG4136 148 LLAEPRALLLDEP 160
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-223 |
4.13e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 107.79 E-value: 4.13e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA-- 77
Cdd:PRK13635 4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRqv 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRhvFPGLTVMENLEMGafLKKN---REEN----QANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRA 150
Cdd:PRK13635 84 GMVFQNPDNQ--FVGATVQDDVAFG--LENIgvpREEMvervDQALRQV-----GMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285220 151 LMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGT-TVLLIEQNANKAlAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEI 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-234 |
4.45e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 106.70 E-value: 4.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MS-MLKVENLSVHY----------------------GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSS 57
Cdd:COG1134 1 MSsMIEVENVSKSYrlyhepsrslkelllrrrrtrrEEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 58 GKIEFLGqeiqkmpaqKI-----VAGGLsqVPEgrhvfpgLTVMENLEM-GAFLKKNREENQANLKKV--FSrfpRLEER 129
Cdd:COG1134 81 GRVEVNG---------RVsalleLGAGF--HPE-------LTGRENIYLnGRLLGLSRKEIDEKFDEIveFA---ELGDF 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 130 KNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEpsmGLA---PIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRG 206
Cdd:COG1134 140 IDQPVKTYSSGMRARLAFAVATAVDPDILLVDE---VLAvgdAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRA 216
|
250 260
....*....|....*....|....*...
gi 444285220 207 YVLETGKIVLSGTgkelasSEEVRKAYL 234
Cdd:COG1134 217 IWLEKGRLVMDGD------PEEVIAAYE 238
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
1-215 |
5.37e-28 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 110.77 E-value: 5.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGL 80
Cdd:PRK11288 2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTVMENLEMGAFLKKNREENQANLKK-VFSRFPRLEERKNQDA--ATLSGGEQQMLAMGRALMSTPKL 157
Cdd:PRK11288 82 AIIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYeAREQLEHLGVDIDPDTplKYLSIGQRQMVEIAKALARNARV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 158 LLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:PRK11288 162 IAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-223 |
8.70e-28 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 108.77 E-value: 8.70e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQ 82
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 vpeGRHVFPGLTVMENLEMGafLKKNR---EENQANLKKVFSrFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:PRK11607 99 ---SYALFPHMTVEQNIAFG--LKQDKlpkAEIASRVNEMLG-LVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 160 LDEPsMG-----LAPIFIQEIFDIIQDIqkqGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK11607 173 LDEP-MGaldkkLRDRMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-216 |
1.13e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 105.92 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIeflgqeiqkmpaqkiVAGG--LS 81
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------------LAGTapLA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEG-RHVF------PGLTVMENLEMGafLKKN-REENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMS 153
Cdd:PRK11247 78 EAREDtRLMFqdarllPWKKVIDNVGLG--LKGQwRDAALQALAAV-----GLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285220 154 TPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVL 216
Cdd:PRK11247 151 RPGLLLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGL 214
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
3-212 |
1.18e-27 |
|
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: 105.21 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGM-------IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQE----IQKMP 71
Cdd:COG4778 4 LLEVENLSKTFTLhlqggkrLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQAS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 72 AQKIVA------GGLSQVpegRHVFPGLT----VMENL-EMGAflkkNREENQANLKKVFSRFpRLEERKNQDA-ATLSG 139
Cdd:COG4778 84 PREILAlrrrtiGYVSQF---LRVIPRVSaldvVAEPLlERGV----DREEARARARELLARL-NLPERLWDLPpATFSG 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 140 GEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETG 212
Cdd:COG4778 156 GEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
13-223 |
1.65e-27 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 107.10 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 13 YGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLG---QEIQKMPAQKI--VAGGLSQvpegr 87
Cdd:COG4586 32 YREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGyvpFKRRKEFARRIgvVFGQRSQ----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 88 hVFPGLTVMENLEMgafLKK----NREENQANLKKVFSRFpRLEERKNQDAATLSGGeQQM---LAMgrALMSTPKLLLL 160
Cdd:COG4586 107 -LWWDLPAIDSFRL---LKAiyriPDAEYKKRLDELVELL-DLGELLDTPVRQLSLG-QRMrceLAA--ALLHRPKILFL 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285220 161 DEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLL-------IEqnankalAISDRGYVLETGKIVLSGTGKEL 223
Cdd:COG4586 179 DEPTIGLDVVSKEAIREFLKEYnRERGTTILLtshdmddIE-------ALCDRVIVIDHGRIIYDGSLEEL 242
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-224 |
4.77e-27 |
|
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: 102.99 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGL--VRPSSGKIEFLGQEIQKMPAQKIVAGGL- 80
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 --SQVPEGrhvFPGLTVMEnlemgaFLkknREENqanlkkvfsrfprleerknqdaATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:cd03217 81 laFQYPPE---IPGVKNAD------FL---RYVN----------------------EGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 159 LLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAI-SDRGYVLETGKIVLSGtGKELA 224
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG-DKELA 192
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
4-218 |
4.92e-27 |
|
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: 103.34 E-value: 4.92e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEvnEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM-PAQKIVagglSQ 82
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAApPADRPV----SM 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMGAF--LKKNREENQAnLKKVFSRFPrLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLL 160
Cdd:cd03298 75 LFQENNLFAHLTVEQNVGLGLSpgLKLTAEDRQA-IEVALARVG-LAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 161 DEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03298 153 DEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
13-218 |
6.89e-27 |
|
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: 103.57 E-value: 6.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 13 YGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLG-----QEIQKMPAQKIVAGGLSQVPEGR 87
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlvpwkRRKKFLRRIGVVFGQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 88 HVFPGLTVME---NLEMGAFlKKNREEnqanlkkvFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:cd03267 111 PVIDSFYLLAaiyDLPPARF-KKRLDE--------LSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 165 MGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03267 182 IGLDVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
2-233 |
6.99e-27 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 103.94 E-value: 6.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvAGGLS 81
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQL-ARRLA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEgRHVFP-GLTVMENLEMG-----AFLKKNREENQANLKKVFSRfPRLEERKNQDAATLSGGEQQ--MLAMGRAlMS 153
Cdd:PRK11231 80 LLPQ-HHLTPeGITVRELVAYGrspwlSLWGRLSAEDNARVNQAMEQ-TRINHLADRRLTDLSGGQRQraFLAMVLA-QD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 154 TPkLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAY 233
Cdd:PRK11231 157 TP-VVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVF 235
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-199 |
8.61e-27 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 102.97 E-value: 8.61e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHY--GMIQA--VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQ---K 74
Cdd:PRK11629 4 ILLQCDNLCKRYqeGSVQTdvLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAakaE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 75 IVAGGLSQVPEGRHVFPGLTVMENLEMGAFL-KKNREENQANLKKVFSRFPrLEERKNQDAATLSGGEQQMLAMGRALMS 153
Cdd:PRK11629 84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIgKKKPAEINSRALEMLAAVG-LEHRANHRPSELSGGERQRVAIARALVN 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 444285220 154 TPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKA 199
Cdd:PRK11629 163 NPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTHDLQLA 209
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-234 |
1.00e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 104.16 E-value: 1.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYG-MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQK-----MPAQKIV 76
Cdd:PRK13636 5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYsrkglMKLRESV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 aGGLSQVPEgrHVFPGLTVMENLEMGAF-LKKNREENQANLKKVFSRfPRLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:PRK13636 85 -GMVFQDPD--NQLFSASVYQDVSFGAVnLKLPEDEVRKRVDNALKR-TGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 156 KLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL-ASSEEVRKAY 233
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVfAEKEMLRKVN 240
|
.
gi 444285220 234 L 234
Cdd:PRK13636 241 L 241
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
21-226 |
1.63e-26 |
|
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: 104.80 E-value: 1.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMpaqkivAGGLSQVPEGRHV---------FP 91
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDS------ARGIFLPPHRRRIgyvfqearlFP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 92 GLTVMENLEMGafLKKNREENQAnlkkvfSRFPR---------LEERKnqdAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:COG4148 91 HLSVRGNLLYG--RKRAPRAERR------ISFDEvvellgighLLDRR---PATLSGGERQRVAIGRALLSSPRLLLMDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 163 P--SMGLApiFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASS 226
Cdd:COG4148 160 PlaALDLA--RKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
21-226 |
1.68e-26 |
|
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: 104.81 E-value: 1.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQK------MPAQKIVAGGLSQvpEGRhVFPGLT 94
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDsrkgifLPPEKRRIGYVFQ--EAR-LFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 95 VMENLEMGafLKKNR-EENQANLKKVFSRF---PRLEERKNqdaaTLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPI 170
Cdd:TIGR02142 92 VRGNLRYG--MKRARpSERRISFERVIELLgigHLLGRLPG----RLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 171 FIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASS 226
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWAS 222
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
17-234 |
1.83e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 103.37 E-value: 1.83e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 17 QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIV------AGGLSQVPEGRhVF 90
Cdd:PRK13641 21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLkklrkkVSLVFQFPEAQ-LF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 91 PGlTVMENLE-----MGAFLKKNREENQANLKKVFSRfprlEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSM 165
Cdd:PRK13641 100 EN-TVLKDVEfgpknFGFSEDEAKEKALKWLKKVGLS----EDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 166 GLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEE-VRKAYL 234
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKEwLKKHYL 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-233 |
2.17e-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: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGK-IEFLGQ--------EIQKmp 71
Cdd:COG1119 1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLFGErrggedvwELRK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 72 aqKIvagGLSQvPEGRHVFP-GLTVMENLEMGAF----LKKNREENQANL-KKVFSRFpRLEERKNQDAATLSGGEQQML 145
Cdd:COG1119 79 --RI---GLVS-PALQLRFPrDETVLDVVLSGFFdsigLYREPTDEQRERaRELLELL-GLAHLADRPFGTLSQGEQRRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 146 AMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELA 224
Cdd:COG1119 152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVL 231
|
....*....
gi 444285220 225 SSEEVRKAY 233
Cdd:COG1119 232 TSENLSEAF 240
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-219 |
2.77e-26 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 104.11 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAg 78
Cdd:PRK11153 1 MIELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRK- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 glsqvpEGRHV------FPGL---TVMEN----LEMGaflKKNREENQanlKKVFSRFPR--LEERKNQDAATLSGGEQQ 143
Cdd:PRK11153 80 ------ARRQIgmifqhFNLLssrTVFDNvalpLELA---GTPKAEIK---ARVTELLELvgLSDKADRYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 144 MLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLI--EQNANKALAisDRGYVLETGKIVLSGT 219
Cdd:PRK11153 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRElGLTIVLIthEMDVVKRIC--DRVAVIDAGRLVEQGT 224
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-233 |
3.62e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.54 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAqKIVAGGL 80
Cdd:PRK09536 1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSA-RAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTVMENLEMGAFLKKNR--EENQANLKKVFSRFPRLEERK--NQDAATLSGGEQQMLAMGRALMSTPK 156
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGRTPHRSRfdTWTETDRAAVERAMERTGVAQfaDRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 157 LLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAY 233
Cdd:PRK09536 160 VLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAF 236
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
4-229 |
4.32e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 103.27 E-value: 4.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY-----------GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA 72
Cdd:COG4608 8 LEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 QKivagglsQVPEGRH---VF--------PGLTVMENLE-----MGAFLKKNREEN-QANLKKV------FSRFPRleer 129
Cdd:COG4608 88 RE-------LRPLRRRmqmVFqdpyaslnPRMTVGDIIAeplriHGLASKAERRERvAELLELVglrpehADRYPH---- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 130 knqdaaTLSGGEQQMLAMGRALMSTPKLLLLDEP------SmglapifIQ-EIFDIIQDIQKQ-GTTVLLIEQNankaLA 201
Cdd:COG4608 157 ------EFSGGQRQRIGIARALALNPKLIVCDEPvsaldvS-------IQaQVLNLLEDLQDElGLTYLFISHD----LS 219
|
250 260 270
....*....|....*....|....*....|..
gi 444285220 202 ----ISDRGYVLETGKIVlsgtgkELASSEEV 229
Cdd:COG4608 220 vvrhISDRVAVMYLGKIV------EIAPRDEL 245
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-222 |
5.58e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 5.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSmLKVENLSVHY--GM---IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQ----KMP 71
Cdd:PRK13637 1 MS-IKIENLTHIYmeGTpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 72 AQKIVAGGLSQVPEgrHVFPGLTVMENLemgAFLKKNREENQANLKKVFSRFPRL-----EERKNQDAATLSGGEQQMLA 146
Cdd:PRK13637 80 DIRKKVGLVFQYPE--YQLFEETIEKDI---AFGPINLGLSEEEIENRVKRAMNIvgldyEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 147 MGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKE 222
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPRE 231
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
2-223 |
6.08e-26 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 101.63 E-value: 6.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLV---RPSSGKIEFLGQEIQKmpaqkivAG 78
Cdd:PRK09984 3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQR-------EG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQVPEGRHVFPG-----------LTVMENLEMGAFlkknreENQANLKKVFSRFPRLEERK--------------NQD 133
Cdd:PRK09984 76 RLARDIRKSRANTGyifqqfnlvnrLSVLENVLIGAL------GSTPFWRTCFSWFTREQKQRalqaltrvgmvhfaHQR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 134 AATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETG 212
Cdd:PRK09984 150 VSTLSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDInQNDGITVVVTLHQVDYALRYCERIVALRQG 229
|
250
....*....|.
gi 444285220 213 KIVLSGTGKEL 223
Cdd:PRK09984 230 HVFYDGSSQQF 240
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
4-192 |
1.10e-25 |
|
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: 104.29 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA---QKIVAgG 79
Cdd:TIGR02857 322 LEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADAdswRDQIA-W 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPegrHVFPGlTVMENLEMG------AFLKknREENQANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRALM 152
Cdd:TIGR02857 401 VPQHP---FLFAG-TIAENIRLArpdasdAEIR--EALERAGLDEFVAALPQgLDTPIGEGGAGLSGGQAQRLALARAFL 474
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 444285220 153 STPKLLLLDEPSMGLAPIFIQEIFDIIQDIqKQGTTVLLI 192
Cdd:TIGR02857 475 RDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLV 513
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
3-235 |
1.32e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 100.83 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQ---EIQKMPAQKIVAG 78
Cdd:PRK13644 1 MIRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIdtgDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQVPEGRhvFPGLTVMENLemgAFLKKNREENQANLKKVFSRF---PRLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:PRK13644 81 IVFQNPETQ--FVGRTVEEDL---AFGPENLCLPPIEIRKRVDRAlaeIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 156 KLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKaLAISDRGYVLETGKIVLSGTGKELASSEEVRkaYLG 235
Cdd:PRK13644 156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQ--TLG 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
4-218 |
1.79e-25 |
|
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: 99.14 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY----------------------GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIE 61
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 62 flgqeiqkmpaqkiVAGGLSQVPEGRHVF-PGLTVMENLEM-GAFLKKNREENQANLKKVFSrFPRLEERKNQDAATLSG 139
Cdd:cd03220 81 --------------VRGRVSSLLGLGGGFnPELTGRENIYLnGRLLGLSRKEIDEKIDEIIE-FSELGDFIDLPVKTYSS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 140 GEQQMLAMGRALMSTPKLLLLDEpsmGLA---PIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVL 216
Cdd:cd03220 146 GMKARLAFAIATALEPDILLIDE---VLAvgdAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRF 222
|
..
gi 444285220 217 SG 218
Cdd:cd03220 223 DG 224
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-223 |
1.82e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.11 E-value: 1.82e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaGGLSQV 83
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ---RDICMV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEMG-AFLKKNREENQANLKKVFSrFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:PRK11432 84 FQSYALFPHMSLGENVGYGlKMLGVPKEERKQRVKEALE-LVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
4-223 |
2.55e-25 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 103.32 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIVAGGLSQ 82
Cdd:COG1132 340 IEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT-LESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGlTVMENLEMGAfLKKNREE-----NQANLKKVFSRFP-----RLEERknqdAATLSGGEQQMLAMGRALM 152
Cdd:COG1132 419 VPQDTFLFSG-TIRENIRYGR-PDATDEEveeaaKAAQAHEFIEALPdgydtVVGER----GVNLSGGQRQRIAIARALL 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 153 STPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKqGTTVLLIeqnANK--ALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:COG1132 493 KDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVI---AHRlsTIRNADRILVLDDGRIVEQGTHEEL 561
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
19-212 |
3.76e-25 |
|
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: 98.69 E-value: 3.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVagglsqVPEGRHVFPGLTVMEN 98
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV------VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 99 --LEMGAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIF 176
Cdd:TIGR01184 75 iaLAVDRVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 444285220 177 DIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETG 212
Cdd:TIGR01184 155 EELMQIwEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-215 |
5.13e-25 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 98.96 E-value: 5.13e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGL------VRpSSGKIEFLGQEIqkmpaqkiVA 77
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndlipgAR-VEGEILLDGEDI--------YD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRHV---------FPgLTVMENLEMGafLKKNREENQANLKKvfsrfpRLEE-------------RKNQDAA 135
Cdd:COG1117 83 PDVDVVELRRRVgmvfqkpnpFP-KSIYDNVAYG--LRLHGIKSKSELDE------IVEEslrkaalwdevkdRLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 136 TLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQgTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
4-192 |
9.38e-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: 101.67 E-value: 9.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAV-RDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIVAGGLSQ 82
Cdd:TIGR02868 335 LELRDLSAGYPGAPPVlDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLD-QDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFpGLTVMENL----------EMGAFLKknreenQANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRAL 151
Cdd:TIGR02868 414 CAQDAHLF-DTTVRENLrlarpdatdeELWAALE------RVGLADWLRALPDgLDTVLGEGGARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQkQGTTVLLI 192
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLI 526
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-230 |
1.58e-24 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 99.39 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSmLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGL 80
Cdd:PRK10851 1 MS-IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQvpegrH--VFPGLTVMENLEMG-AFLKKNREENQANLKKVFSRF---PRLEERKNQDAATLSGGEQQMLAMGRALMST 154
Cdd:PRK10851 80 FQ-----HyaLFRHMTVFDNIAFGlTVLPRRERPNAAAIKAKVTQLlemVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVR 230
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEElKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-218 |
2.30e-24 |
|
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: 96.50 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY-GM-IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAgGLS 81
Cdd:cd03245 3 IEFRNVSFSYpNQeIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRR-NIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEMGAFLKKNRE----ENQANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRALMSTPK 156
Cdd:cd03245 82 YVPQDVTLFYG-TLRDNITLGAPLADDERilraAELAGVTDFVNKHPNgLDLQIGERGRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 157 LLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNAnkALAISDRGYVLETGKIVLSG 218
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPS--LLDLVDRIIVMDSGRIVADG 220
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-214 |
2.32e-24 |
|
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: 94.98 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQA--VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMpAQKIVAGGLS 81
Cdd:cd03246 1 LEVENVSFRYPGAEPpvLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQW-DPNELGDHVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLemgaflkknreenqanlkkvfsrfprleerknqdaatLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:cd03246 80 YLPQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANkALAISDRGYVLETGKI 214
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
2-233 |
3.65e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 96.98 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMpAQKIVA---G 78
Cdd:PRK10253 6 ARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHY-ASKEVArriG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQvpegRHVFPG-LTVMENLEMGAF-----LKKNREENQANLKKVFsRFPRLEERKNQDAATLSGGEQQMLAMGRALM 152
Cdd:PRK10253 85 LLAQ----NATTPGdITVQELVARGRYphqplFTRWRKEDEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMVLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 153 STPKLLLLDEPSMGLAPIFIQEIFDIIQDIQK-QGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRK 231
Cdd:PRK10253 160 QETAIMLLDEPTTWLDISHQIDLLELLSELNReKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIER 239
|
..
gi 444285220 232 AY 233
Cdd:PRK10253 240 IY 241
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-163 |
3.78e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 3.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGkieflgqEIQKMPAQKIvaGGLSQVPE 85
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVSIPKGLRI--GYLPQEPP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 86 grhVFPGLTVMENLEMG----AFLKKNREENQANL---KKVFSRFPRLEER--------------------------KNQ 132
Cdd:COG0488 72 ---LDDDLTVLDTVLDGdaelRALEAELEELEAKLaepDEDLERLAELQEEfealggweaearaeeilsglgfpeedLDR 148
|
170 180 190
....*....|....*....|....*....|.
gi 444285220 133 DAATLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:COG0488 149 PVSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-235 |
3.85e-24 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 96.19 E-value: 3.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMiQAVRdVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM-PAQKIVagglS 81
Cdd:PRK10771 1 MLKLTDITWLYHH-LPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTpPSRRPV----S 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGLTVMENLEMGAF--LKKNREE--------NQANLKKVFSRFPrleerknqdaATLSGGEQQMLAMGRAL 151
Cdd:PRK10771 75 MLFQENNLFSHLTVAQNIGLGLNpgLKLNAAQreklhaiaRQMGIEDLLARLP----------GQLSGGQRQRVALARCL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 152 MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVR 230
Cdd:PRK10771 145 VREQPILLLDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKASA 224
|
....*
gi 444285220 231 KAYLG 235
Cdd:PRK10771 225 SALLG 229
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-223 |
5.06e-24 |
|
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: 99.76 E-value: 5.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYG----MIQAVRDVSFEVNEGEVVSLIGANGAGKT----TILRTLSGLVRPSSGKIEFLGQEIQKMPA 72
Cdd:COG4172 4 MPLLSVEDLSVAFGqgggTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 QKivaggLSQVpEGRH---VF--------PGLTV----MENLE----MGAflKKNREENQANLKKVfsRFPRLEERKNQD 133
Cdd:COG4172 84 RE-----LRRI-RGNRiamIFqepmtslnPLHTIgkqiAEVLRlhrgLSG--AAARARALELLERV--GIPDPERRLDAY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 134 AATLSGGEQQ--MLAMgrALMSTPKLLLLDEPSMGLaPIFIQ-EIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVL 209
Cdd:COG4172 154 PHQLSGGQRQrvMIAM--ALANEPDLLIADEPTTAL-DVTVQaQILDLLKDLQRElGMALLLITHDLGVVRRFADRVAVM 230
|
250
....*....|....
gi 444285220 210 ETGKIVLSGTGKEL 223
Cdd:COG4172 231 RQGEIVEQGPTAEL 244
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
4-218 |
6.36e-24 |
|
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: 93.92 E-value: 6.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG--MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKmpAQKIVAGGLS 81
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSD--LEKALSSLIS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLemgaflkknreenqanlkkvfsrfprleerknqdAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:cd03247 79 VLNQRPYLFDT-TLRNNL----------------------------------GRRFSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIQKqGTTVLLIEQNAnKALAISDRGYVLETGKIVLSG 218
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-214 |
6.55e-24 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 99.31 E-value: 6.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVhygmiQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQV 83
Cdd:PRK10762 258 LKVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRH---VFPGLTVMENLEMGA---FLKKNREENQANLKKVFSRFPRLEERK----NQDAATLSGGEQQMLAMGRALMS 153
Cdd:PRK10762 333 SEDRKrdgLVLGMSVKENMSLTAlryFSRAGGSLKHADEQQAVSDFIRLFNIKtpsmEQAIGLLSGGNQQKVAIARGLMT 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285220 154 TPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:PRK10762 413 RPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-225 |
7.16e-24 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 99.11 E-value: 7.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY-----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEF-LGQEIQKMPAQKIV 76
Cdd:TIGR03269 279 IIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 AGG-----LSQVPEGRHVFPGLTVMENL--EMGAFLKKNREENQA--NLKKVFSRFPRLEERKNQDAATLSGGEQQMLAM 147
Cdd:TIGR03269 359 GRGrakryIGILHQEYDLYPHRTVLDNLteAIGLELPDELARMKAviTLKMVGFDEEKAEEILDKYPDELSEGERHRVAL 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 148 GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:TIGR03269 439 AQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVE 517
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-219 |
8.83e-24 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 99.70 E-value: 8.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKmpAQKIVAGGLSQVPEGRHVFPGLTVME 97
Cdd:TIGR01257 945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET--NLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 98 NLEMGAFLK-KNREENQANLKKVFSRfPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIF 176
Cdd:TIGR01257 1023 HILFYAQLKgRSWEEAQLEMEAMLED-TGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 444285220 177 DIIQDIqKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGT 219
Cdd:TIGR01257 1102 DLLLKY-RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
4-223 |
9.09e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.81 E-value: 9.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQ---------- 73
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadkn 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 74 --KIVAGGLSQVPEGRHVFPGLTVMENLeMGA---FLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMG 148
Cdd:PRK10619 86 qlRLLRTRLTMVFQHFNLWSHMTVLENV-MEApiqVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 149 RALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-213 |
1.22e-23 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 98.46 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGlVRPS---SGKIEFLGQEIQkmpAQKIV--- 76
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEELQ---ASNIRdte 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 AGGLSQVPEGRHVFPGLTVMENLEMGAFLKKNreeNQANLKKVFSRFPRL--EERKNQDAAT----LSGGEQQMLAMGRA 150
Cdd:PRK13549 81 RAGIAIIHQELALVKELSVLENIFLGNEITPG---GIMDYDAMYLRAQKLlaQLKLDINPATpvgnLGLGQQQLVEIAKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 151 LMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGK 213
Cdd:PRK13549 158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
16-229 |
1.93e-23 |
|
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: 94.14 E-value: 1.93e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 16 IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA--GGLSQVPegrHVFPGl 93
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSqiGLVSQEP---VLFDG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 94 TVMENLEMGAFLKKNREE----NQANLKKVFSRFP-RLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGL- 167
Cdd:cd03249 92 TIAENIRYGKPDATDEEVeeaaKKANIHDFIMSLPdGYDTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALd 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 168 --APIFIQEIFDIIqdiqKQGTTVLLIeqnANKALAI--SDRGYVLETGKIVLSGTGKELASSEEV 229
Cdd:cd03249 172 aeSEKLVQEALDRA----MKGRTTIVI---AHRLSTIrnADLIAVLQNGQVVEQGTHDELMAQKGV 230
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-225 |
2.16e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 95.18 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQ---AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA----Q 73
Cdd:PRK13650 2 SNIIEVKNLTFKYKEDQekyTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdirH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 74 KIvaGGLSQVPEGRhvFPGLTVMENLEMGAflkknreENQA-NLKKVFSR------FPRLEERKNQDAATLSGGEQQMLA 146
Cdd:PRK13650 82 KI--GMVFQNPDNQ--FVGATVEDDVAFGL-------ENKGiPHEEMKERvnealeLVGMQDFKEREPARLSGGQKQRVA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 147 MGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKaLAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:PRK13650 151 IAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELFS 229
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
1-229 |
2.32e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 94.87 E-value: 2.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKI--VA 77
Cdd:PRK13652 1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVrkFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRHVFPglTVMENLEMGAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKL 157
Cdd:PRK13652 81 GLVFQNPDDQIFSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 158 LLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEV 229
Cdd:PRK13652 159 LVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDL 231
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-222 |
2.69e-23 |
|
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];
Pssm-ID: 443660 [Multi-domain] Cd Length: 563 Bit Score: 97.51 E-value: 2.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvaggls 81
Cdd:COG4618 331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREEL------ 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 qvpeGRHV---------FPGlTVMENLemgaflkknreenqanlkkvfSRFPRLEERKNQDAA----------------- 135
Cdd:COG4618 405 ----GRHIgylpqdvelFDG-TIAENI---------------------ARFGDADPEKVVAAAklagvhemilrlpdgyd 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 136 --------TLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANkALAISDRGY 207
Cdd:COG4618 459 trigeggaRLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLL 537
|
250
....*....|....*
gi 444285220 208 VLETGKIVLSGTGKE 222
Cdd:COG4618 538 VLRDGRVQAFGPRDE 552
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
3-191 |
2.72e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 93.09 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA--QKivagGL 80
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCtyQK----QL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTVMENLEMGA-FLKKNREENQanLKKVFSrfprLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:PRK13540 77 CFVGHRSGINPYLTLRENCLYDIhFSPGAVGITE--LCRLFS----LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWL 150
|
170 180 190
....*....|....*....|....*....|..
gi 444285220 160 LDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLL 191
Cdd:PRK13540 151 LDEPLVALDELSLLTIITKIQEHRAKGGAVLL 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
4-190 |
2.79e-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: 2.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEI---QKMPAQKIV-AGG 79
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaeqRDEPHENILyLGH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPegrhvfPGLTVMENLE-MGAFLKKNREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:TIGR01189 81 LPGLK------PELSALENLHfWAAIHGGAQRTIEDALAAV-----GLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLW 149
|
170 180 190
....*....|....*....|....*....|...
gi 444285220 159 LLDEPSMGLAPIFIQEIFDIIQD-IQKQGTTVL 190
Cdd:TIGR01189 150 ILDEPTTALDKAGVALLAGLLRAhLARGGIVLL 182
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-232 |
3.83e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 94.38 E-value: 3.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY------GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMP-AQKI 75
Cdd:PRK13633 4 MIKCKNVSYKYesneesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnLWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 76 --VAGGLSQVPEGRHVfpgLTVMEnlEMGAFLKKN--------REENQANLKKVfsrfpRLEERKNQDAATLSGGEQQML 145
Cdd:PRK13633 84 rnKAGMVFQNPDNQIV---ATIVE--EDVAFGPENlgippeeiRERVDESLKKV-----GMYEYRRHAPHLLSGGQKQRV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 146 AMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKAlAISDRGYVLETGKIVLSGTGKELA 224
Cdd:PRK13633 154 AIAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIF 232
|
....*...
gi 444285220 225 SSEEVRKA 232
Cdd:PRK13633 233 KEVEMMKK 240
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-223 |
4.90e-23 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 93.69 E-value: 4.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLS--GLVRPS---SGKIEFLGQEIQKmPAQKIVA 77
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEvtiTGSIVYNGHNIYS-PRTDTVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 -----GGLSQVPegrHVFPgLTVMENLEMGafLKKNREENQANLKKVFSR-------FPRLEERKNQDAATLSGGEQQML 145
Cdd:PRK14239 84 lrkeiGMVFQQP---NPFP-MSIYENVVYG--LRLKGIKDKQVLDEAVEKslkgasiWDEVKDRLHDSALGLSGGQQQRV 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 146 AMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQgTTVLLIEQNANKALAISDR-GYVLEtGKIVLSGTGKEL 223
Cdd:PRK14239 158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRtGFFLD-GDLIEYNDTKQM 234
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-215 |
6.79e-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: 96.43 E-value: 6.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGlVRPS---SGKIEFLGQEIQKMPAQKIVAGG 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPEGRHVFPGLTVMENLEMG--AFLKKNREENQANLKKVFSRFPRLEERKNQDA---ATLSGGEQQMLAMGRALMST 154
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGneITLPGGRMAYNAMYLRAKNLLRELQLDADNVTrpvGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-215 |
7.17e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 96.13 E-value: 7.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLsvhygMIQAVR-DVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQ-KMPAQKIVAgGLS 81
Cdd:PRK11288 258 LRLDGL-----KGPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDiRSPRDAIRA-GIM 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRH---VFPGLTVMENLEMGA---------FLKKNREENQAN--LKKVFSRFPRLEerknQDAATLSGGEQQMLAM 147
Cdd:PRK11288 332 LCPEDRKaegIIPVHSVADNINISArrhhlragcLINNRWEAENADrfIRSLNIKTPSRE----QLIMNLSGGNQQKAIL 407
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 148 GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA 475
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-204 |
8.35e-23 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 92.25 E-value: 8.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKI--VAGG 79
Cdd:PRK10908 1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVpfLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPEGRHVFPGLTVMENLEM-----GAFLKKNREENQANLKKVfsrfPRLEERKNQdAATLSGGEQQMLAMGRALMST 154
Cdd:PRK10908 81 IGMIFQDHHLLMDRTVYDNVAIpliiaGASGDDIRRRVSAALDKV----GLLDKAKNF-PIQLSGGEQQRVGIARAVVNK 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVL-------LIEQNANKALAISD 204
Cdd:PRK10908 156 PAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLmathdigLISRRSYRMLTLSD 212
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-226 |
1.34e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 92.79 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSS-----GKIEFLGQEI-QKMPAQKIVA 77
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyERRVNLNRLR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRHVFPgLTVMENLEMGAFL-----KKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALM 152
Cdd:PRK14258 88 RQVSMVHPKPNLFP-MSVYDNVAYGVKIvgwrpKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 153 STPKLLLLDEPSMGLAPIFIQEIFDIIQDIQ-KQGTTVLLIEQNANKALAISD-----RGYVLETGKIVLSGTGKELASS 226
Cdd:PRK14258 167 VKPKVLLMDEPCFGLDPIASMKVESLIQSLRlRSELTMVIVSHNLHQVSRLSDftaffKGNENRIGQLVEFGLTKKIFNS 246
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-235 |
1.38e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 93.02 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAgglsQVPEGRHV---FPGLt 94
Cdd:PRK15056 22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVA----YVPQSEEVdwsFPVL- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 95 VMENLEMG-----AFLKKNREENQANLKKVFSRFPRLEERKNQdAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAP 169
Cdd:PRK15056 97 VEDVVMMGryghmGWLRRAKKRDRQIVTAALARVDMVEFRHRQ-IGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 170 IFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGyVLETGKIVLSGTGKELASSEEVRKAYLG 235
Cdd:PRK15056 176 KTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTETTFTAENLELAFSG 240
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-224 |
2.26e-22 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 91.67 E-value: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGL--VRPSSGKIEFLGQEIQKMPAQKIVAGGLS 81
Cdd:COG0396 1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 ---QVPEgrhVFPGLTVMEnlemgaFLK----KNREEN---QANLKKVFSRFPRLEerKNQDAAT------LSGGEQ--- 142
Cdd:COG0396 81 lafQYPV---EIPGVSVSN------FLRtalnARRGEElsaREFLKLLKEKMKELG--LDEDFLDryvnegFSGGEKkrn 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 143 ---QMLAMGralmstPKLLLLDEPSMGL---ApifIQEIFDIIQDIQKQGTTVLLIEQNAN-----KAlaisDRGYVLET 211
Cdd:COG0396 150 eilQMLLLE------PKLAILDETDSGLdidA---LRIVAEGVNKLRSPDRGILIITHYQRildyiKP----DFVHVLVD 216
|
250
....*....|...
gi 444285220 212 GKIVLSGtGKELA 224
Cdd:COG0396 217 GRIVKSG-GKELA 228
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-224 |
2.37e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKivaGGL 80
Cdd:PRK11000 1 MASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE---RGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTVMENLEMGAFL-KKNREENQANLKKVFS--RFPRLEERKNQDaatLSGGEQQMLAMGRALMSTPKL 157
Cdd:PRK11000 78 GMVFQSYALYPHLSVAENMSFGLKLaGAKKEEINQRVNQVAEvlQLAHLLDRKPKA---LSGGQRQRVAIGRTLVAEPSV 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 158 LLLDEPSMGL-APIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIvlSGTGKELA 224
Cdd:PRK11000 155 FLLDEPLSNLdAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV--AQVGKPLE 220
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-215 |
2.45e-22 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 90.55 E-value: 2.45e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG--MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKiVAGGLS 81
Cdd:cd03369 7 IEVENLSVRYApdLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLED-LRSSLT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEMgaflkknreENQANLKKVFSRFPRLEERKNqdaatLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:cd03369 86 IIPQDPTLFSG-TIRSNLDP---------FDEYSDEEIYGALRVSEGGLN-----LSQGQRQLLCLARALLKRPRVLVLD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 162 EPSmglAPIfiqeifDIIQD--IQK------QGTTVLLIEQNAnKALAISDRGYVLETGKIV 215
Cdd:cd03369 151 EAT---ASI------DYATDalIQKtireefTNSTILTIAHRL-RTIIDYDKILVMDAGEVK 202
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-223 |
2.98e-22 |
|
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: 94.78 E-value: 2.98e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG--MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGgLS 81
Cdd:TIGR02203 331 VEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ-VA 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEMGAFLKKNREE-----NQANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:TIGR02203 410 LVSQDVVLFND-TIANNIAYGRTEQADRAEieralAAAYAQDFVDKLPLgLDTPIGENGVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 156 KLLLLDEPSMGLAPIFIQEIFDIIQDIQkQGTTVLLIeqnANKALAI--SDRGYVLETGKIVLSGTGKEL 223
Cdd:TIGR02203 489 PILILDEATSALDNESERLVQAALERLM-QGRTTLVI---AHRLSTIekADRIVVMDDGRIVERGTHNEL 554
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-219 |
4.07e-22 |
|
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: 90.25 E-value: 4.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvAGGLS 81
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL-RSRIS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEmgAFLKKNREE-----NQANLKKVFSRFP-RLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:cd03244 82 IIPQDPVLFSG-TIRSNLD--PFGEYSDEElwqalERVGLKEFVESLPgGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285220 156 KLLLLDEPSMGLAPIFIQEIFDIIQDIQKqGTTVLLIEQNANkALAISDRGYVLETGKIVLSGT 219
Cdd:cd03244 159 KILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHRLD-TIIDSDRILVLDKGRVVEFDS 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-163 |
5.46e-22 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 93.59 E-value: 5.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlgqeiqkmpAQKIVAGGLSQ 82
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETVKIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 vpEGRHVFPGLTVMENLEMGAflkknREENQANLKKVFSR--FPRleERKNQDAATLSGGEQQMLAMGRALMSTPKLLLL 160
Cdd:COG0488 386 --HQEELDPDKTVLDELRDGA-----PGGTEQEVRGYLGRflFSG--DDAFKPVGVLSGGEKARLALAKLLLSPPNVLLL 456
|
...
gi 444285220 161 DEP 163
Cdd:COG0488 457 DEP 459
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
4-224 |
6.76e-22 |
|
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: 90.40 E-value: 6.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSG--LVRPSSGKIEFLGQEIQKMPAQKIVAGGL- 80
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPDERARAGLf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 --SQVPEGrhvFPGLTVMENLEmgAFLKKNREENQANLKKVFSRFPRLEE---RKNQDAATL--------SGGEQQMLAM 147
Cdd:TIGR01978 81 laFQYPEE---IPGVSNLEFLR--SALNARRSARGEEPLDLLDFEKLLKEklaLLDMDEEFLnrsvnegfSGGEKKRNEI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 148 GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAIS-DRGYVLETGKIVLSGtGKELA 224
Cdd:TIGR01978 156 LQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSG-DVELA 232
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
3-191 |
9.68e-22 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 89.16 E-value: 9.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIqkmpaqkivagGLSQ 82
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI-----------DDPD 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRH-------VFPGLTVMENLEMGAFLKKNREEN-QANLKKVfsRFPRLEERKnqdAATLSGGEQQMLAMGRALMST 154
Cdd:PRK13539 71 VAEACHylghrnaMKPALTVAENLEFWAAFLGGEELDiAAALEAV--GLAPLAHLP---FGYLSAGQKRRVALARLLVSN 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 444285220 155 PKLLLLDEPSMGLaPIFIQEIF-DIIQDIQKQGTTVLL 191
Cdd:PRK13539 146 RPIWILDEPTAAL-DAAAVALFaELIRAHLAQGGIVIA 182
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-234 |
1.16e-21 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 92.97 E-value: 1.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGM---IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGlVRPS--SGKIEFLGQEIQKMPAQKIVA 77
Cdd:TIGR02633 257 ILEARNLTCWDVInphRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGkfEGNVFINGKPVDIRNPAQAIR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRH---VFPGLTVMENLEMGA---FLKKNREENQANLKKVFSRFPRLEERKNQD---AATLSGGEQQMLAMG 148
Cdd:TIGR02633 336 AGIAMVPEDRKrhgIVPILGVGKNITLSVlksFCFKMRIDAAAELQIIGSAIQRLKVKTASPflpIGRLSGGNQQKAVLA 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 149 RALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELaSSEE 228
Cdd:TIGR02633 416 KMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDFVNHAL-TQEQ 494
|
....*.
gi 444285220 229 VRKAYL 234
Cdd:TIGR02633 495 VLAAAL 500
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
17-223 |
1.88e-21 |
|
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: 88.83 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 17 QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMpAQKIVAGGLSQVPEGRHVFPGlTVM 96
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREV-TLDSLRRAIGVVPQDTVLFND-TIG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 97 ENLEMGAfLKKNREE-----NQANLKKVFSRFP-----RLEERknqdAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMG 166
Cdd:cd03253 93 YNIRYGR-PDATDEEvieaaKAAQIHDKIMRFPdgydtIVGER----GLKLSGGEKQRVAIARAILKNPPILLLDEATSA 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 167 LAPIFIQEIFDIIQDIQKQGTTVLLieqnANKALAI--SDRGYVLETGKIVLSGTGKEL 223
Cdd:cd03253 168 LDTHTEREIQAALRDVSKGRTTIVI----AHRLSTIvnADKIIVLKDGRIVERGTHEEL 222
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-236 |
2.81e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 89.13 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPS-----SGKIEFLGQEIQKMPAQKI--- 75
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIYSPDVDPIevr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 76 -VAGGLSQVPegrHVFPGLTVMENLEMGAFLK---KNREENQANLK---KVFSRFPRLEERKNQDAATLSGGEQQMLAMG 148
Cdd:PRK14267 85 rEVGMVFQYP---NPFPHLTIYDNVAIGVKLNglvKSKKELDERVEwalKKAALWDEVKDRLNDYPSNLSGGQRQRLVIA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 149 RALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNAnKALAISDRGYVLETGKIVLSGTGKELASS-- 226
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPA-QAARVSDYVAFLYLGKLIEVGPTRKVFENpe 240
|
250
....*....|
gi 444285220 227 EEVRKAYLGG 236
Cdd:PRK14267 241 HELTEKYVTG 250
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
18-223 |
3.80e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.03 E-value: 3.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIV------AGGLSQVPEGRhVFP 91
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIkqirkkVGLVFQFPESQ-LFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 92 GlTVMENLemgAFLKKN----REENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGL 167
Cdd:PRK13649 101 E-TVLKDV---AFGPQNfgvsQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 168 APIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK13649 177 DPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
4-223 |
4.12e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.42 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGgLS 81
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQA-IS 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEMGAFlKKNREENQANLKKV-FSRFprLEERKNQDAAT------LSGGEQQMLAMGRALMST 154
Cdd:PRK11160 418 VVSQRVHLFSA-TLRDNLLLAAP-NASDEALIEVLQQVgLEKL--LEDDKGLNAWLgeggrqLSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDIQkQGTTVLLIEQNANkALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-218 |
4.66e-21 |
|
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: 87.71 E-value: 4.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 17 QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPS---SGKIEFLGQEIQKMPAQKIVAgglsQVPEGRHVFPGL 93
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQPRKPDQFQKCVA----YVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 94 TVMENLEMGAFLKKNREENQANLKKVfSRFPRLEERKNQDAA-----TLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLA 168
Cdd:cd03234 97 TVRETLTYTAILRLPRKSSDAIRKKR-VEDVLLRDLALTRIGgnlvkGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 444285220 169 PIFIQEIFDIIQDIQKQGTTVLL-IEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03234 176 SFTALNLVSTLSQLARRNRIVILtIHQPRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-223 |
5.37e-21 |
|
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: 91.34 E-value: 5.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGM-IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMpAQKIVAGGLSQ 82
Cdd:TIGR01193 474 IVINDVSYSYGYgSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDI-DRHTLRQFINY 552
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGlTVMENLEMGAflKKNREENQ-------ANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRALMST 154
Cdd:TIGR01193 553 LPQEPYIFSG-SILENLLLGA--KENVSQDEiwaaceiAEIKDDIENMPLgYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 155 PKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQgtTVLLIEQNANKAlAISDRGYVLETGKIVLSGTGKEL 223
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK--TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
4-204 |
5.58e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 88.30 E-value: 5.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGL--VRPS---SGKIEFLGQEIQkmpaqkivAG 78
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLY--------AP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQVPEGRHV---------FPGlTVMENLEMGAFLKKNreenQANLKKVFSRFPR-------LEERKNQDAATLSGGEQ 142
Cdd:PRK14243 83 DVDPVEVRRRIgmvfqkpnpFPK-SIYDNIAYGARINGY----KGDMDELVERSLRqaalwdeVKDKLKQSGLSLSGGQQ 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 143 QMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQgTTVLLIEQNANKALAISD 204
Cdd:PRK14243 158 QRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
16-218 |
6.06e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 88.99 E-value: 6.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 16 IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFL--GQEIQKMPA-----------QKIVAGGLSQ 82
Cdd:PRK13651 20 LKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkDEKNKKKTKekekvleklviQKTRFKKIKK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRH----VFP-------GLTVMENLEMGAF-LKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRA 150
Cdd:PRK13651 100 IKEIRRrvgvVFQfaeyqlfEQTIEKDIIFGPVsMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAGI 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 151 LMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDG 247
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-219 |
8.51e-21 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 87.48 E-value: 8.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEflgqeiqKMPAQKIvaggl 80
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-------RNGKLRI----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGLTvmenLEMGAFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLL 160
Cdd:PRK09544 70 GYVPQKLYLDTTLP----LTVNRFLRLRPGTKKEDILPALKRV-QAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 161 DEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLeTGKIVLSGT 219
Cdd:PRK09544 145 DEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGT 203
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
3-200 |
1.18e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.45 E-value: 1.18e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVagglsq 82
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAERGV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPEGRHVFPGLTVMENLEMGAFL----KKNREEN-QANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKL 157
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLagveKMQRLEIaHQMLKKV-----GLEGAEKRYIWQLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 444285220 158 LLLDEPsMGLAPIFIQEIFD--IIQDIQKQGTTVLLIEQNANKAL 200
Cdd:PRK11248 150 LLLDEP-FGALDAFTREQMQtlLLKLWQETGKQVLLITHDIEEAV 193
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-219 |
1.26e-20 |
|
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: 89.74 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY-----------GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVrPSSGKIEFLGQEIQKMPA 72
Cdd:COG4172 276 LEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSR 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 QK---------IV----AGGLSQ-------VPEGRHV-FPGLTvmenlemgaflKKNREEN-QANLKKV------FSRFP 124
Cdd:COG4172 355 RAlrplrrrmqVVfqdpFGSLSPrmtvgqiIAEGLRVhGPGLS-----------AAERRARvAEALEEVgldpaaRHRYP 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 125 rleerknqdaATLSGGEQQMLAMGRALMSTPKLLLLDEP------SmglapifIQ-EIFDIIQDIQKQ-GTTVLLIEQNA 196
Cdd:COG4172 424 ----------HEFSGGQRQRIAIARALILEPKLLVLDEPtsaldvS-------VQaQILDLLRDLQREhGLAYLFISHDL 486
|
250 260
....*....|....*....|...
gi 444285220 197 NKALAISDRGYVLETGKIVLSGT 219
Cdd:COG4172 487 AVVRALAHRVMVMKDGKVVEQGP 509
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
4-227 |
1.65e-20 |
|
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: 86.52 E-value: 1.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG--MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA--GG 79
Cdd:cd03251 1 VEFKNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRqiGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPegrHVFPGlTVMENLEMGAFlKKNREE-----NQANLKKVFSRFP-----RLEERknqdAATLSGGEQQMLAMGR 149
Cdd:cd03251 81 VSQDV---FLFND-TVAENIAYGRP-GATREEveeaaRAANAHEFIMELPegydtVIGER----GVKLSGGQRQRIAIAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 150 ALMSTPKLLLLDEPSMGLApifiQEIFDIIQD-IQK--QGTTVLLIeqnANKALAI--SDRGYVLETGKIVLSGTGKELA 224
Cdd:cd03251 152 ALLKDPPILILDEATSALD----TESERLVQAaLERlmKNRTTFVI---AHRLSTIenADRIVVLEDGKIVERGTHEELL 224
|
...
gi 444285220 225 SSE 227
Cdd:cd03251 225 AQG 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-227 |
1.69e-20 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 86.68 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMP----AQKIvag 78
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPsrelAKRL--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 glsqvpegrhvfpgltvmenlemgAFLkknREENQANLK-KV-----FSRFP----RL--EERKNQDAA----------- 135
Cdd:COG4604 78 ------------------------AIL---RQENHINSRlTVrelvaFGRFPyskgRLtaEDREIIDEAiayldledlad 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 136 ----TLSGGEQQM--LAMgrALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYV 208
Cdd:COG4604 131 ryldELSGGQRQRafIAM--VLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVA 208
|
250
....*....|....*....
gi 444285220 209 LETGKIVLSGTGKELASSE 227
Cdd:COG4604 209 MKDGRVVAQGTPEEIITPE 227
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
3-214 |
1.85e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 89.22 E-value: 1.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGM---IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGlVRP--SSGKIEFLGQEIQ-KMPAQKIv 76
Cdd:PRK13549 259 ILEVRNLTAWDPVnphIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKiRNPQQAI- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 77 AGGLSQVPEGRH---VFPGLTVMENLEMGA---FLKKNREENQANLKKVFSRFPRLEERKN---QDAATLSGGEQQMLAM 147
Cdd:PRK13549 337 AQGIAMVPEDRKrdgIVPVMGVGKNITLAAldrFTGGSRIDDAAELKTILESIQRLKVKTAspeLAIARLSGGNQQKAVL 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 148 GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:PRK13549 417 AKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
18-231 |
2.04e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 87.16 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRP---SSGKIEFLGQEIQKMPAQKI--VAGGLSQVPEGRhvFPG 92
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIreKVGIVFQNPDNQ--FVG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 93 LTVMENLemgAFLKKN----REENQANLKKVFSRFPRLEERKNQdAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLA 168
Cdd:PRK13640 100 ATVGDDV---AFGLENravpRPEMIKIVRDVLADVGMLDYIDSE-PANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285220 169 PIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKAlAISDRGYVLETGKIVLSGTGKELASSEEVRK 231
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSKVEMLK 238
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
19-234 |
2.56e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 89.07 E-value: 2.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQVPEGRH---VFPGLTV 95
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITESRRdngFFPNFSI 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 96 MENLEMGAFLKKNReenqanLKKVFSRFPRLEERK----------------NQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:PRK09700 359 AQNMAISRSLKDGG------YKGAMGLFHEVDEQRtaenqrellalkchsvNQNITELSGGNQQKVLISKWLCCCPEVII 432
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 160 LDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAYL 234
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEEEIMAWAL 507
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-218 |
2.91e-20 |
|
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: 84.91 E-value: 2.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPS--SGKIEFLGQEIQKMPAQKIVAgglsQVPEGRHVFPGLTVM 96
Cdd:cd03213 25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKIIG----YVPQDDILHPTLTVR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 97 ENLEMGAFLKKnreenqanlkkvfsrfprleerknqdaatLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIF 176
Cdd:cd03213 101 ETLMFAAKLRG-----------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVM 151
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 444285220 177 DIIQDIQKQGTTVLL-IEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03213 152 SLLRRLADTGRTIICsIHQPSSEIFELFDKLLLLSQGRVIYFG 194
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
2-215 |
3.10e-20 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 89.01 E-value: 3.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA 77
Cdd:PRK10535 3 ALLELKDIRRSYpsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 ------GGLSQvpeGRHVFPGLTVMENLEMGA-FLKKNREENQANLKKVFSRFPrLEERKNQDAATLSGGEQQMLAMGRA 150
Cdd:PRK10535 83 lrrehfGFIFQ---RYHLLSHLTAAQNVEVPAvYAGLERKQRLLRAQELLQRLG-LEDRVEYQPSQLSGGQQQRVSIARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 151 LMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKAlAISDRGYVLETGKIV 215
Cdd:PRK10535 159 LMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVA-AQAERVIEIRDGEIV 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-236 |
3.48e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 86.25 E-value: 3.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVR------PSSGKIEFLGQEIQKMPAQKI--VAGGLSQVPegrHVF 90
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKLrkEVGMVFQQP---NPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 91 PGLTVMENLEMGafLKKNREENQANLKKVFSRFPR-------LEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:PRK14246 103 PHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRkvglwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 164 SMGLAPIFIQEIFDIIQDIQKQgTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASS--EEVRKAYLGG 236
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSpkNELTEKYVIG 254
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
13-192 |
4.66e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 84.21 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 13 YGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEflgqeiqkmpaqkiVAGG--LSQVPEGRHV- 89
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVR--------------RAGGarVAYVPQRSEVp 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 90 --FPgLTVMENLEMGAF-----LKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:NF040873 68 dsLP-LTVRDLVAMGRWarrglWRRLTRDDRAAVDDALERV-GLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQGTTVLLI 192
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARGATVVVV 175
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
14-223 |
5.09e-20 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 87.78 E-value: 5.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 14 GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMP---AQKIVAGGLSQVPEGRHVF 90
Cdd:PRK10070 39 GLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALM 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 91 PGLTVMENLEMGAFL-----KKNREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSM 165
Cdd:PRK10070 119 PHMTVLDNTAFGMELaginaEERREKALDALRQV-----GLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 166 GLAPIFIQEIFDIIQDIQ-KQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQaKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEI 252
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-230 |
5.24e-20 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 85.97 E-value: 5.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKI--VAG 78
Cdd:PRK11831 5 ANLVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQVPEGRHVFPGLTVMENLemgAF-LKKNREENQANLKKVFsrFPRLEERKNQDAAT-----LSGGEQQMLAMGRALM 152
Cdd:PRK11831 85 RMSMLFQSGALFTDMNVFDNV---AYpLREHTQLPAPLLHSTV--MMKLEAVGLRGAAKlmpseLSGGMARRAALARAIA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 153 STPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVR 230
Cdd:PRK11831 160 LEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
2-214 |
6.74e-20 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 84.83 E-value: 6.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHYG----MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQ---K 74
Cdd:PRK10584 5 NIVEVHHLKKSVGqgehELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEaraK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 75 IVAGGLSQVPEGRHVFPGLTVMENLEMGAFLK-----KNREENQANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGR 149
Cdd:PRK10584 85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRgessrQSRNGAKALLEQL-----GLGKRLDHLPAQLSGGEQQRVALAR 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 150 ALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKAlAISDRGYVLETGKI 214
Cdd:PRK10584 160 AFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLA-ARCDRRLRLVNGQL 224
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
2-215 |
9.03e-20 |
|
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: 85.24 E-value: 9.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHY---------GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM-P 71
Cdd:TIGR02769 1 SLLEVRDVTHTYrtgglfgakQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 72 AQK---------IVAGGLSQVPEGRHVfpGLTVMENLEMGAFLKKNREEN--QANLKKVFSRFPRLEERKNQdaatLSGG 140
Cdd:TIGR02769 81 KQRrafrrdvqlVFQDSPSAVNPRMTV--RQIIGEPLRHLTSLDESEQKAriAELLDMVGLRSEDADKLPRQ----LSGG 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 141 EQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:TIGR02769 155 QLQRINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-229 |
1.45e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 84.79 E-value: 1.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKI--VAGGL 80
Cdd:PRK13647 5 IEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVrsKVGLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRhVFPGlTVME-------NLEMGAFLKKNREEnqANLKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMS 153
Cdd:PRK13647 85 FQDPDDQ-VFSS-TVWDdvafgpvNMGLDKDEVERRVE--EALKAV-----RMWDFRDKPPYHLSYGQKKRVAIAGVLAM 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 154 TPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGtGKELASSEEV 229
Cdd:PRK13647 156 DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEG-DKSLLTDEDI 230
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-229 |
1.95e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.14 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGM-------------IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQK 69
Cdd:PRK15079 8 LLEVADLKVHFDIkdgkqwfwqppktLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 70 MPA----------QKIVAGGLSQVPegrhvfPGLTV----MENLEMgAFLKKNREENQANLKKVFSRFPRLEERKNQDAA 135
Cdd:PRK15079 88 MKDdewravrsdiQMIFQDPLASLN------PRMTIgeiiAEPLRT-YHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 136 TLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLaPIFIQ-EIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGK 213
Cdd:PRK15079 161 EFSGGQCQRIGIARALILEPKLIICDEPVSAL-DVSIQaQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGH 239
|
250
....*....|....*.
gi 444285220 214 IVlsgtgkELASSEEV 229
Cdd:PRK15079 240 AV------ELGTYDEV 249
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
3-233 |
2.58e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 84.40 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYG-----MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEF-------LGQEIQKM 70
Cdd:PRK13643 1 MIKFEKVNYTYQpnspfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvssTSKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 71 PAQKIVaGGLSQVPEGRhVFPGlTVMENLEMG-AFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGR 149
Cdd:PRK13643 81 PVRKKV-GVVFQFPESQ-LFEE-TVLKDVAFGpQNFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 150 ALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEV 229
Cdd:PRK13643 158 ILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDF 237
|
....
gi 444285220 230 RKAY 233
Cdd:PRK13643 238 LKAH 241
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
3-163 |
3.12e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 82.16 E-value: 3.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVhygmiqaVRD-------VSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKmpaqki 75
Cdd:PRK13538 1 MLEARNLAC-------ERDerilfsgLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRR------ 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 76 vagglsqvpeGRHVF----------PG----LTVMENLemgAFLKK-----NREENQANLKKVfsrfpRLEERKNQDAAT 136
Cdd:PRK13538 68 ----------QRDEYhqdllylghqPGikteLTALENL---RFYQRlhgpgDDEALWEALAQV-----GLAGFEDVPVRQ 129
|
170 180
....*....|....*....|....*..
gi 444285220 137 LSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:PRK13538 130 LSAGQQRRVALARLWLTRAPLWILDEP 156
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
7-215 |
3.64e-19 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 85.55 E-value: 3.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 7 ENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQVPEG 86
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 87 RHVFPGLTVMENLEMGAFLKKNREENQANL----KKVFSRFPrLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKGMFVDQDKMyrdtKAIFDELD-IDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 444285220 163 PSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:PRK10982 161 PTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-215 |
3.87e-19 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 85.61 E-value: 3.87e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMI---QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLV--RPSSGKIEFLGQEIQKMPAQKIVA 77
Cdd:NF040905 257 VFEVKNWTVYHPLHperKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSygRNISGTVFKDGKEVDVSTVSDAID 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRHVFpGLTVMENLemgaflKKNreENQANLKKVFSRF--PRLEERK----------------NQDAATLSG 139
Cdd:NF040905 337 AGLAYVTEDRKGY-GLNLIDDI------KRN--ITLANLGKVSRRGviDENEEIKvaeeyrkkmniktpsvFQKVGNLSG 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 140 GEQQMLAMGRALMSTPKLLLLDEPSMGlapifIQ-----EIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:NF040905 408 GNQQKVVLSKWLFTDPDVLILDEPTRG-----IDvgakyEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI 482
|
.
gi 444285220 215 V 215
Cdd:NF040905 483 T 483
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-234 |
3.95e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 83.52 E-value: 3.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEI----QKMPAQKIVAG 78
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdyskRGLLALRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQVPEGRHVFPGLTV-----MENLEMGAFLKKNREENQANLKKVfSRFprleerKNQDAATLSGGEQQMLAMGRALMS 153
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDSdiafsLRNLGVPEAEITRRVDEALTLVDA-QHF------RHQPIQCLSHGQKKRVAIAGALVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 154 TPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGT-GKELASSEEVRKA 232
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGApGEVFACTEAMEQA 233
|
..
gi 444285220 233 YL 234
Cdd:PRK13638 234 GL 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-226 |
4.56e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 4.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 8 NLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSG-----KIEFLGQEI---QKMPAQKIVAGG 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnyRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQVPegrHVFPgLTVMENLEMGAFL------KKNREENQANLKKVfSRFPRLEERKNQDAATLSGGEQQMLAMGRALMS 153
Cdd:PRK14271 106 LFQRP---NPFP-MSIMDNVLAGVRAhklvprKEFRGVAQARLTEV-GLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAV 180
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 154 TPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQgTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASS 226
Cdd:PRK14271 181 NPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSS 252
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-163 |
7.14e-19 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 83.74 E-value: 7.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM-PAQKIVAg 78
Cdd:PRK11650 1 MAGLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELePADRDIA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 glsqvpegrHVF------PGLTVMENLEMGAflkKNReenqanlkkvfsRFPRLE-ERKNQDAAT--------------L 137
Cdd:PRK11650 80 ---------MVFqnyalyPHMSVRENMAYGL---KIR------------GMPKAEiEERVAEAARileleplldrkpreL 135
|
170 180
....*....|....*....|....*.
gi 444285220 138 SGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:PRK11650 136 SGGQRQRVAMGRAIVREPAVFLFDEP 161
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-229 |
1.59e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 82.59 E-value: 1.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYG-----MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSG-----------KIEFLGQE 66
Cdd:PRK13631 21 ILRVKNLYCVFDekqenELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGtiqvgdiyigdKKNNHELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 67 IQKMPaQKI--------VAGGLSQVPEgRHVFPGlTVMENLEMGAF-LKKNREENQANLKKVFSRFPRLEERKNQDAATL 137
Cdd:PRK13631 101 TNPYS-KKIknfkelrrRVSMVFQFPE-YQLFKD-TIEKDIMFGPVaLGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 138 SGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLS 217
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
|
250
....*....|..
gi 444285220 218 GTGKELASSEEV 229
Cdd:PRK13631 258 GTPYEIFTDQHI 269
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
31-230 |
2.93e-18 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 82.23 E-value: 2.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 31 VVSLIGANGAGKTTILRTLSGLVRPSSGKIEfLGQEIQKMPAQKIvagglSQVPEGRHV---------FPGLTVMENLEM 101
Cdd:PRK11144 26 ITAIFGRSGAGKTSLINAISGLTRPQKGRIV-LNGRVLFDAEKGI-----CLPPEKRRIgyvfqdarlFPHYKVRGNLRY 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 102 GafLKKNREENQANL------KKVFSRFPrleerknqdaATLSGGEQQMLAMGRALMSTPKLLLLDEPsmgLAPIFI--- 172
Cdd:PRK11144 100 G--MAKSMVAQFDKIvallgiEPLLDRYP----------GSLSGGEKQRVAIGRALLTAPELLLMDEP---LASLDLprk 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 173 QEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVR 230
Cdd:PRK11144 165 RELLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
3-214 |
3.08e-18 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 82.85 E-value: 3.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSvhyGMIQ-AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLS 81
Cdd:PRK10982 250 ILEVRNLT---SLRQpSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVfPGLTVMENLEMGAFLkknreenqANLKKVFSRFPRLEERKNQ-------DA------------ATLSGGEQ 142
Cdd:PRK10982 327 LVTEERRS-TGIYAYLDIGFNSLI--------SNIRNYKNKVGLLDNSRMKsdtqwviDSmrvktpghrtqiGSLSGGNQ 397
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 143 QMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKI 214
Cdd:PRK10982 398 QKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-215 |
3.26e-18 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 80.89 E-value: 3.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHY---------GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMP 71
Cdd:PRK10419 1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 72 AQKIVAGGLS-----QVPEGRhVFPGLTVMENLE--MGAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQM 144
Cdd:PRK10419 81 RAQRKAFRRDiqmvfQDSISA-VNPRKTVREIIRepLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQR 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 145 LAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:PRK10419 160 VCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
1-223 |
3.39e-18 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 81.71 E-value: 3.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYG----MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLV----RPSSGKIEFLGQEIQKMPA 72
Cdd:PRK11022 1 MALLNVDKLSVHFGdesaPFRAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 ---QKIVAGGLSQVPEG--RHVFPGLTV----MENLEM---GAflKKNREENQANLKKVFSrFPRLEERKNQDAATLSGG 140
Cdd:PRK11022 81 kerRNLVGAEVAMIFQDpmTSLNPCYTVgfqiMEAIKVhqgGN--KKTRRQRAIDLLNQVG-IPDPASRLDVYPHQLSGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 141 EQQ--MLAMgrALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVL-LIEQNANKALAISDRGYVLETGKIVLS 217
Cdd:PRK11022 158 MSQrvMIAM--AIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALvLITHDLALVAEAAHKIIVMYAGQVVET 235
|
....*.
gi 444285220 218 GTGKEL 223
Cdd:PRK11022 236 GKAHDI 241
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
6-190 |
4.28e-18 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 82.86 E-value: 4.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQK-------------MPa 72
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADarhrravcpriayMP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 QkivagGLsqvpeGRHVFPGLTVMENLEMGAFL----KKNREENQANLKKV--FSRFPrleERKnqdAATLSGGEQQMLA 146
Cdd:NF033858 83 Q-----GL-----GKNLYPTLSVFENLDFFGRLfgqdAAERRRRIDELLRAtgLAPFA---DRP---AGKLSGGMKQKLG 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 444285220 147 MGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ--GTTVL 190
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVL 192
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-225 |
8.03e-18 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.93 E-value: 8.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAG--KTTILRTLSGlvrPSSGKIEF-LGQEIQKMPAQKIVAGGL 80
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWrF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGR-HVFPGltvMENLEM-GAFLKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:NF000106 91 RPVR*GRrESFSG---RENLYMiGR*LDLSRKDARARADELLERF-SLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 159 LLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:NF000106 167 YLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKT 233
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
3-167 |
1.14e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.20 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQ-----EIQKMPAQKIVA 77
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 ------GGLSQVP-EG--RHVFPGLTVMENLeMGAFLK---KNREENQANLKKVFSRFPRLEERknqdAATLSGGEQQML 145
Cdd:PRK11701 86 llrtewGFVHQHPrDGlrMQVSAGGNIGERL-MAVGARhygDIRATAGDWLERVEIDAARIDDL----PTTFSGGMQQRL 160
|
170 180
....*....|....*....|..
gi 444285220 146 AMGRALMSTPKLLLLDEPSMGL 167
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGL 182
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-228 |
1.24e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.37 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY---GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEI--QKMPAQKIVA 77
Cdd:PRK13642 4 ILEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLtaENVWNLRRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLSQVPEGRhvFPGLTVMENLEMGAFLKK-NREENQANLKKVFSRFPRLeERKNQDAATLSGGEQQMLAMGRALMSTPK 156
Cdd:PRK13642 84 GMVFQNPDNQ--FVGATVEDDVAFGMENQGiPREEMIKRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 444285220 157 LLLLDEPSMGLAPIFIQEIFDIIQDIQ-KQGTTVLLIEQNANKAlAISDRGYVLETGKIVLSGTGKELASSEE 228
Cdd:PRK13642 161 IIILDESTSMLDPTGRQEIMRVIHEIKeKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELFATSE 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
21-225 |
1.59e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.86 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPS---SGKIEFLGQEIQKMPAQKIVAgglsQVPEGRHVFPGLTVME 97
Cdd:TIGR00955 43 NVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISA----YVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 98 NLEMGAFLKKNR----EENQANLKKVFSRfprLEERKNQDAAT--------LSGGEQQMLAMGRALMSTPKLLLLDEPSM 165
Cdd:TIGR00955 119 HLMFQAHLRMPRrvtkKEKRERVDEVLQA---LGLRKCANTRIgvpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285220 166 GLAPIFIQEIFDIIQDIQKQGTTVLL-IEQNANKALAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICtIHQPSSELFELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
7-226 |
3.18e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.01 E-value: 3.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 7 ENLSVHY-GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvagglsqvpe 85
Cdd:PRK13657 338 DDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL---------- 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 86 gRH----VF--PGL---TVMENLEMG------AFLKKNREENQAN---LKKVFSRFPRLEERKNQdaatLSGGEQQMLAM 147
Cdd:PRK13657 408 -RRniavVFqdAGLfnrSIEDNIRVGrpdatdEEMRAAAERAQAHdfiERKPDGYDTVVGERGRQ----LSGGERQRLAI 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 148 GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAisDRGYVLETGKIVLSGTGKELASS 226
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRNA--DRILVFDNGRVVESGSFDELVAR 559
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
17-235 |
3.25e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 78.67 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 17 QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIV------AGGLSQVPEGRhVF 90
Cdd:PRK13646 21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrpvrkrIGMVFQFPESQ-LF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 91 PGlTVMENLEMGAflkKNReenQANLKKVFSR---------FPRleERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:PRK13646 100 ED-TVEREIIFGP---KNF---KMNLDEVKNYahrllmdlgFSR--DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIQ-KQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL-ASSEEVRKAYLG 235
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELfKDKKKLADWHIG 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-232 |
4.75e-17 |
|
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: 79.46 E-value: 4.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGL--VRPSSGKI----------------EFLGQ 65
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 66 EIQK----MPAQKIVAGGLSQvPEGRHV--------------FPGLTVMENL-----EMGAFLKKNREENQANLKKVfsr 122
Cdd:TIGR03269 81 PCPVcggtLEPEEVDFWNLSD-KLRRRIrkriaimlqrtfalYGDDTVLDNVlealeEIGYEGKEAVGRAVDLIEMV--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 123 fpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALA- 201
Cdd:TIGR03269 157 --QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEd 234
|
250 260 270
....*....|....*....|....*....|....*.
gi 444285220 202 ISDRGYVLETGKIVLSGTGKE-----LASSEEVRKA 232
Cdd:TIGR03269 235 LSDKAIWLENGEIKEEGTPDEvvavfMEGVSEVEKE 270
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-223 |
4.79e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 78.14 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQK-------MPAQKIVaGGLSQVPEgrHVF 90
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgkknkklKPLRKKV-GIVFQFPE--HQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 91 PGLTVMENLemgAFLKKN----REENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMG 166
Cdd:PRK13634 99 FEETVEKDI---CFGPMNfgvsEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 167 LAPIFIQEIFDIIQDIQK-QGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
22-233 |
5.26e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 77.28 E-value: 5.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 22 VSFEVNEGEVVSLIGANGAGKTTILRTLSGLVrPSSGKIEFLGQEIQKMPA--QKIVAGGLSQ---VPEGRHVFPGLTvm 96
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAaeLARHRAYLSQqqtPPFAMPVFQYLT-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 97 enLEMGAflKKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQ-------MLAMGRALMSTPKLLLLDEPSMGLaP 169
Cdd:PRK03695 92 --LHQPD--KTRTEAVASALNEVAEAL-GLDDKLGRSVNQLSGGEWQrvrlaavVLQVWPDINPAGQLLLLDEPMNSL-D 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 170 IFIQEIFD-IIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRKAY 233
Cdd:PRK03695 166 VAQQAALDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
4-164 |
9.15e-17 |
|
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: 74.02 E-value: 9.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIeflgqeiqkmpaqkivagglsqv 83
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIV----------------------- 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 pegrhvfpglTVMENLEMGAFlkknreenqanlkkvfsrfprleerknqdaATLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:cd03221 58 ----------TWGSTVKIGYF------------------------------EQLSGGEKMRLALAKLLLENPNLLLLDEP 97
|
.
gi 444285220 164 S 164
Cdd:cd03221 98 T 98
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
4-167 |
1.01e-16 |
|
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: 75.61 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMpaQKIVAGGLSQV 83
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQ--RDSIARGLLYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLEmgaFLKKNREENQanlkkVFSRFPRLEERKNQD--AATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:cd03231 79 GHAPGIKTTLSVLENLR---FWHADHSDEQ-----VEEALARVGLNGFEDrpVAQLSAGQQRRVALARLLLSGRPLWILD 150
|
....*.
gi 444285220 162 EPSMGL 167
Cdd:cd03231 151 EPTTAL 156
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
18-227 |
1.35e-16 |
|
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: 75.99 E-value: 1.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGgLSQVPEGRHVFPGlTVME 97
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQ-VGVVLQENVLFNR-SIRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 98 NLEMG-AFLKKNREENQANLKKVFSRFPRLEERKNQ----DAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLApifI 172
Cdd:cd03252 95 NIALAdPGMSMERVIEAAKLAGAHDFISELPEGYDTivgeQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD---Y 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 173 QEIFDIIQDIQK--QGTTVLLIEQNANkALAISDRGYVLETGKIVLSGTGKELASSE 227
Cdd:cd03252 172 ESEHAIMRNMHDicAGRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
16-213 |
1.63e-16 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 77.74 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 16 IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQ-KMPAQKIVAgGLSQVPEGRHVFPGLT 94
Cdd:PRK10762 17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfNGPKSSQEA-GIGIIHQELNLIPQLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 95 VMENLEMGaflkknREENQA----NLKKVFSRFPRLEERKN------QDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:PRK10762 96 IAENIFLG------REFVNRfgriDWKKMYAEADKLLARLNlrfssdKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 444285220 165 MGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGK 213
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-227 |
2.11e-16 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 77.58 E-value: 2.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 22 VSFEVNEGEVVSLIGANGAGKTTILRTLSGLVrPSSGKIEFLGQEIQKMPA----QKIvaGGLSQVPegrHVFPGlTVME 97
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPeswrKHL--SWVGQNP---QLPHG-TLRD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 98 NLEMGaflKKNREE-------NQANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAP 169
Cdd:PRK11174 442 NVLLG---NPDASDeqlqqalENAWVSEFLPLLPQgLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDA 518
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 444285220 170 IFIQEIFDIIQDIQKQGTTVLL---IEQnankaLAISDRGYVLETGKIVLSGTGKELASSE 227
Cdd:PRK11174 519 HSEQLVMQALNAASRRQTTLMVthqLED-----LAQWDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-226 |
2.32e-16 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 76.48 E-value: 2.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPS----SGKIEFLGQEIQKMPA 72
Cdd:COG4170 1 MPLLDIRNLTIEIdtpqGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNwhvtADRFRWNGIDLLKLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 Q---KIVAGGLS---QVPEgRHVFPGLTVMENLEM--------GAF--LKKNREENQANL---------KKVFSRFPrle 127
Cdd:COG4170 81 RerrKIIGREIAmifQEPS-SCLDPSAKIGDQLIEaipswtfkGKWwqRFKWRKKRAIELlhrvgikdhKDIMNSYP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 128 erkNQdaatLSGGEQQ--MLAMgrALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISD 204
Cdd:COG4170 157 ---HE----LTEGECQkvMIAM--AIANQPRLLIADEPTNAMESTTQAQIFRLLARLnQLQGTSILLISHDLESISQWAD 227
|
250 260
....*....|....*....|..
gi 444285220 205 RGYVLETGKIVLSGTGKELASS 226
Cdd:COG4170 228 TITVLYCGQTVESGPTEQILKS 249
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
2-192 |
5.31e-16 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 76.38 E-value: 5.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSV---HYGMIqaVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGL--------VRPSSGKIEFLGQEIqKM 70
Cdd:COG4178 361 GALALEDLTLrtpDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwpygsgriARPAGARVLFLPQRP-YL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 71 PAqkivaGGLSQV---PEGRHVFPGLTVMENLEmgaflkknreenQANLkkvfsrfPRLEERKNQDAA---TLSGGEQQM 144
Cdd:COG4178 438 PL-----GTLREAllyPATAEAFSDAELREALE------------AVGL-------GHLAERLDEEADwdqVLSLGEQQR 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 444285220 145 LAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDiQKQGTTVLLI 192
Cdd:COG4178 494 LAFARLLLHKPDWLFLDEATSALDEENEAALYQLLRE-ELPGTTVISV 540
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-214 |
5.37e-16 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 74.89 E-value: 5.37e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRpSSGKIEFLGQEIQKMPAQKIvAGGLS 81
Cdd:cd03289 3 MTVKDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKW-RKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEmgAFLKKNREE-----NQANLKKVFSRFP-RLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNLD--PYGKWSDEEiwkvaEEVGLKSVIEQFPgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 156 KLLLLDEPSMGLAPIFIQeifdIIQDIQKQ---GTTVLLIEQNAnKALAISDRGYVLETGKI 214
Cdd:cd03289 158 KILLLDEPSAHLDPITYQ----VIRKTLKQafaDCTVILSEHRI-EAMLECQRFLVIEENKV 214
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
21-197 |
1.22e-15 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 73.21 E-value: 1.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMP--AQKIVAGGLSQVPegrhVFPGLTVMEN 98
Cdd:PRK10247 25 NISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKpeIYRQQVSYCAQTP----TLFGDTVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 99 LEMGAFLKKNREENQAnLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDI 178
Cdd:PRK10247 101 LIFPWQIRNQQPDPAI-FLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEI 179
|
170 180
....*....|....*....|
gi 444285220 179 I-QDIQKQGTTVLLIEQNAN 197
Cdd:PRK10247 180 IhRYVREQNIAVLWVTHDKD 199
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
17-214 |
1.50e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 72.89 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 17 QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQ----KMPAQKIVAggLSQVPegrhVFPG 92
Cdd:cd03248 28 LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISqyehKYLHSKVSL--VGQEP----VLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 93 LTVMENLEMG----AFLKKNREENQANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGL 167
Cdd:cd03248 102 RSLQDNIAYGlqscSFECVKEAAQKAHAHSFISELASgYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSAL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 444285220 168 APIFIQEIFDIIQDiQKQGTTVLLIEQNANkALAISDRGYVLETGKI 214
Cdd:cd03248 182 DAESEQQVQQALYD-WPERRTVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-204 |
2.19e-15 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 74.82 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 28 EGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIE-----------FLGQEIQKMpAQKIVAGGLS---------QVPEgr 87
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTELQDY-FKKLANGEIKvahkpqyvdLIPK-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 88 hVFPGlTVMEnlemgaFLKKNREENqaNLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS--- 164
Cdd:COG1245 175 -VFKG-TVRE------LLEKVDERG--KLDELAEKL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSsyl 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 444285220 165 -----MGLApifiqeifDIIQDIQKQGTTVLLIEQNankaLAISD 204
Cdd:COG1245 244 diyqrLNVA--------RLIRELAEEGKYVLVVEHD----LAILD 276
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-228 |
2.20e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.25 E-value: 2.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA--GGLSQVPEGRhvFPGLTV 95
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKhiGIVFQNPDNQ--FVGSIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 96 MENLEMGafLKKN---REENQANLKKVFSRFPRLeERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFI 172
Cdd:PRK13648 102 KYDVAFG--LENHavpYDEMHRRVSEALKQVDML-ERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDAR 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 173 QEIFDIIQDIQ-KQGTTVLLIEQNANKALAiSDRGYVLETGKIVLSGTGKELASSEE 228
Cdd:PRK13648 179 QNLLDLVRKVKsEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHAE 234
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
16-218 |
2.47e-15 |
|
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: 71.91 E-value: 2.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 16 IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPS---SGKIEFLGQEIQKMpaQKIVAGGLSQVPEGRHVFPG 92
Cdd:cd03233 20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEF--AEKYPGEIIYVSEEDVHFPT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 93 LTVMENLEMGAFLKKNReenqanlkkvFSRfprleerknqdaaTLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIfi 172
Cdd:cd03233 98 LTVRETLDFALRCKGNE----------FVR-------------GISGGERKRVSIAEALVSRASVLCWDNSTRGLDSS-- 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 444285220 173 qEIFDIIQDIQKQ-----GTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:cd03233 153 -TALEILKCIRTMadvlkTTTFVSLYQASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-232 |
2.96e-15 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 74.37 E-value: 2.96e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 17 QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA----QKIVAGGLSQVPEGRHVFP- 91
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHhylhRQVALVGQEPVLFSGSVREn 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 92 ---GLTVMENLEMGAFLKknreenQANLKKVFSRFPR-----LEERKNQdaatLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:TIGR00958 575 iayGLTDTPDEEIMAAAK------AANAHDFIMEFPNgydteVGEKGSQ----LSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 164 SMGLAPIFIQEIFdiiQDIQKQGTTVLLIE------QNANKALaisdrgyVLETGKIVLSGTGKELASSEEVRKA 232
Cdd:TIGR00958 645 TSALDAECEQLLQ---ESRSRASRTVLLIAhrlstvERADQIL-------VLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
3-233 |
3.98e-15 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 72.55 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSG----LVRPS----SGKIEFLGQEIQKMPAQK 74
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRgarvTGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 75 IvAGGLSQVPE-GRHVFPgLTVMENLEMGAFLKKNRE-ENQANLKKVFSRFPRL---EERKNQDAATLSGGEQQMLAMGR 149
Cdd:PRK13547 81 L-ARLRAVLPQaAQPAFA-FSAREIVLLGRYPHARRAgALTHRDGEIAWQALALagaTALVGRDVTTLSGGELARVQFAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 150 AL---------MSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSGT 219
Cdd:PRK13547 159 VLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238
|
250
....*....|....
gi 444285220 220 GKELASSEEVRKAY 233
Cdd:PRK13547 239 PADVLTPAHIARCY 252
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-218 |
6.71e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 73.35 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 16 IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVA-----GGLSQVP----EG 86
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQAlrrdiQFIFQDPyaslDP 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 87 RHVFpGLTVMENLEMGAFLkkNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMG 166
Cdd:PRK10261 417 RQTV-GDSIMEPLRVHGLL--PGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSA 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 444285220 167 LAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:PRK10261 494 LDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-194 |
9.34e-15 |
|
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: 73.02 E-value: 9.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRpSSGKIEFLGQEIQKMPAQKIvAGGLS 81
Cdd:TIGR01271 1218 MDVQGLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTW-RKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEmgAFLKKNREE-----NQANLKKVFSRFP-RLEERKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:TIGR01271 1296 VIPQKVFIFSG-TFRKNLD--PYEQWSDEEiwkvaEEVGLKSVIEQFPdKLDFVLVDGGYVLSNGHKQLMCLARSILSKA 1372
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 444285220 156 KLLLLDEPSMGLAPIFIQeifdIIQDIQKQG---TTVLLIEQ 194
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQ----IIRKTLKQSfsnCTVILSEH 1410
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
2-225 |
1.88e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.59 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLS---------VHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKI------------ 60
Cdd:PRK15112 3 TLLEVRNLSktfryrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELliddhplhfgdy 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 61 EFLGQEIQKM---------PAQKIvaGGLSQVPegrhvfpgltVMENLEMGAflkknrEENQANLKKVFSRFPRLEERKN 131
Cdd:PRK15112 83 SYRSQRIRMIfqdpstslnPRQRI--SQILDFP----------LRLNTDLEP------EQREKQIIETLRQVGLLPDHAS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 132 QDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQ-KQGTTVLLIEQNANKALAISDRGYVLE 210
Cdd:PRK15112 145 YYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVLVMH 224
|
250
....*....|....*.
gi 444285220 211 TGKIVLSG-TGKELAS 225
Cdd:PRK15112 225 QGEVVERGsTADVLAS 240
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
18-225 |
2.67e-14 |
|
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: 71.97 E-value: 2.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIqkMPAQKIVAGGLSQVPEGRHVFPGLTVME 97
Cdd:TIGR01257 1954 AVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNMGYCPQFDAIDDLLTGRE 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 98 NLEMGAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFD 177
Cdd:TIGR01257 2032 HLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWN 2111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 444285220 178 IIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:TIGR01257 2112 TIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKS 2159
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
16-215 |
2.70e-14 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 71.36 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 16 IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGlVRPS---SGKIEFLGQE-----IQKMPAQKIVA--GGLSQVPE 85
Cdd:NF040905 14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGEVcrfkdIRDSEALGIVIihQELALIPY 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 86 grhvfpgLTVMENLEMG------AFLKKNREENQAN--LKKVfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKL 157
Cdd:NF040905 93 -------LSIAENIFLGnerakrGVIDWNETNRRARelLAKV-----GLDESPDTLVTDIGVGKQQLVEIAKALSKDVKL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 158 LLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:NF040905 161 LILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
17-229 |
5.12e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 69.65 E-value: 5.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 17 QAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSG-------KIEFLGQEIQKMPAQKIVAGGLSQVPEgRHV 89
Cdd:PRK13645 25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEVKRLRKEIGLVFQFPE-YQL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 90 FPGlTVMENLEMGAF-LKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLA 168
Cdd:PRK13645 104 FQE-TIEKDIAFGPVnLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLD 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 169 PIFIQEIFDIIQDIQK-QGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELASSEEV 229
Cdd:PRK13645 183 PKGEEDFINLFERLNKeYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQEL 244
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
22-228 |
1.02e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 70.15 E-value: 1.02e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 22 VSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQK---MPAQKIvaggLSQVPEGRHVFPGlTVMEN 98
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfglMDLRKV----LGIIPQAPVLFSG-TVRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 99 LEmgAFLKKNREE-----NQANLKKVFSRFPR-LEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLapifi 172
Cdd:PLN03130 1333 LD--PFNEHNDADlweslERAHLKDVIRRNSLgLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAV----- 1405
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 444285220 173 qeifDIIQD--IQK------QGTTVLLIEQNANKALAiSDRGYVLETGKIVLSGTGKELASSEE 228
Cdd:PLN03130 1406 ----DVRTDalIQKtireefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLSNEG 1464
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-223 |
1.05e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.88 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAG 78
Cdd:PRK10261 12 VLAVENLNIAFmqeqQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKMLLRRRSRQVIELS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQVpEGRHVF----------------PGLTVMENLEMGAFLKK--NREENQANLKKVFS--RFPRLEERKNQDAATLS 138
Cdd:PRK10261 92 EQSAA-QMRHVRgadmamifqepmtslnPVFTVGEQIAESIRLHQgaSREEAMVEAKRMLDqvRIPEAQTILSRYPHQLS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 139 GGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTT-VLLIEQNANKALAISDRGYVLETGKIVLS 217
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGVVAEIADRVLVMYQGEAVET 250
|
....*.
gi 444285220 218 GTGKEL 223
Cdd:PRK10261 251 GSVEQI 256
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
7-170 |
1.07e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 69.77 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 7 ENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEI--QKMPAQKIVaGGLSQV- 83
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdaGDIATRRRV-GYMSQAf 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 ---PEgrhvfpgLTVMENLEMGAFL-KKNREENQANLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:NF033858 349 slyGE-------LTVRQNLELHARLfHLPAAEIAARVAEMLERF-DLADVADALPDSLPLGIRQRLSLAVAVIHKPELLI 420
|
170
....*....|.
gi 444285220 160 LDEPSMGLAPI 170
Cdd:NF033858 421 LDEPTSGVDPV 431
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
34-163 |
1.23e-13 |
|
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: 69.58 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 34 LIGANGAGKTTILRTLSGLVRPSSGKIeflgqeiqkMPAQKIVAGGLSQVPEgrhVFPGLTVMENLEMG-----AFLKKN 108
Cdd:TIGR03719 36 VLGLNGAGKSTLLRIMAGVDKDFNGEA---------RPQPGIKVGYLPQEPQ---LDPTKTVRENVEEGvaeikDALDRF 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 109 RE------ENQANLKKVFSRFPRLEER------------------------KNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:TIGR03719 104 NEisakyaEPDADFDKLAAEQAELQEIidaadawdldsqleiamdalrcppWDADVTKLSGGERRRVALCRLLLSKPDML 183
|
....*
gi 444285220 159 LLDEP 163
Cdd:TIGR03719 184 LLDEP 188
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
6-233 |
2.36e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 67.51 E-value: 2.36e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYGMIQAVRDVSFEV-------------NEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPA 72
Cdd:PRK10575 1 MQEYTNHSDTTFALRNVSFRVpgrtllhplsltfPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 qKIVAGGLSQVPEGRHVFPGLTVMENLEMGAF-----LKKNREENQANLKKVFSrFPRLEERKNQDAATLSGGEQQM--L 145
Cdd:PRK10575 81 -KAFARKVAYLPQQLPAAEGMTVRELVAIGRYpwhgaLGRFGAADREKVEEAIS-LVGLKPLAHRLVDSLSGGERQRawI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 146 AMGRALMStpKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELA 224
Cdd:PRK10575 159 AMLVAQDS--RCLLLDEPTSALDIAHQVDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELM 236
|
....*....
gi 444285220 225 SSEEVRKAY 233
Cdd:PRK10575 237 RGETLEQIY 245
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
1-163 |
2.55e-13 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 68.44 E-value: 2.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlgqeiqkmpAQKIVAGGL 80
Cdd:PRK11147 1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY---------EQDLIVARL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEgRH----VFPglTVMENL-EMGAFLKK--------NREENQANLKKVfSRFP---------RLEERKNQ------ 132
Cdd:PRK11147 72 QQDPP-RNvegtVYD--FVAEGIeEQAEYLKRyhdishlvETDPSEKNLNEL-AKLQeqldhhnlwQLENRINEvlaqlg 147
|
170 180 190
....*....|....*....|....*....|....*.
gi 444285220 133 -DAAT----LSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:PRK11147 148 lDPDAalssLSGGWLRKAALGRALVSNPDVLLLDEP 183
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-164 |
2.85e-13 |
|
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: 68.42 E-value: 2.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEfLGQEIQkmpaqkivaggLSQV 83
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIE-IGETVK-----------LAYV 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGR-HVFPGLTVMENLEMGAFLKK--NREENQanlKKVFSRFprleERKNQD----AATLSGGEQQMLAMGRALMSTPK 156
Cdd:TIGR03719 391 DQSRdALDPNKTVWEEISGGLDIIKlgKREIPS---RAYVGRF----NFKGSDqqkkVGQLSGGERNRVHLAKTLKSGGN 463
|
....*...
gi 444285220 157 LLLLDEPS 164
Cdd:TIGR03719 464 VLLLDEPT 471
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
3-227 |
3.37e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.46 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKiVAGGL 80
Cdd:PLN03232 1234 SIKFEDVHLRYrpGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTD-LRRVL 1312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 81 SQVPEGRHVFPGlTVMENLEmgAFLKKNREE-----NQANLKKVFSRFP-RLEERKNQDAATLSGGEQQMLAMGRALMST 154
Cdd:PLN03232 1313 SIIPQSPVLFSG-TVRFNID--PFSEHNDADlwealERAHIKDVIDRNPfGLDAEVSEGGENFSVGQRQLLSLARALLRR 1389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 155 PKLLLLDEPSMGLapifiqeifDIIQD--IQK------QGTTVLLIEQNANKALAiSDRGYVLETGKIVLSGTGKELASS 226
Cdd:PLN03232 1390 SKILVLDEATASV---------DVRTDslIQRtireefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSR 1459
|
.
gi 444285220 227 E 227
Cdd:PLN03232 1460 D 1460
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-223 |
4.72e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 67.06 E-value: 4.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVrPSSGKIE----FLGQEIQKMPA 72
Cdd:PRK09473 10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLL-AANGRIGgsatFNGREILNLPE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 Q---KIVAGGLSQV---------PEGRhvfPGLTVMENLEMGAFLKKNR--EENQANLKKVfsRFPRLEERKNQDAATLS 138
Cdd:PRK09473 89 KelnKLRAEQISMIfqdpmtslnPYMR---VGEQLMEVLMLHKGMSKAEafEESVRMLDAV--KMPEARKRMKMYPHEFS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 139 GGEQQ--MLAMgrALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLETGKIV 215
Cdd:PRK09473 164 GGMRQrvMIAM--ALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
....*...
gi 444285220 216 LSGTGKEL 223
Cdd:PRK09473 242 EYGNARDV 249
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-205 |
6.12e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 65.64 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 24 FEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAgGLSQVPEGRhvfPGLTVMENLEMGA 103
Cdd:PRK13543 32 FHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMA-YLGHLPGLK---ADLSTLENLHFLC 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 104 FLKKNR-EENQANLKKVFSrfprLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI 182
Cdd:PRK13543 108 GLHGRRaKQMPGSALAIVG----LAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAH 183
|
170 180
....*....|....*....|...
gi 444285220 183 QKQGTTVLLIEQNANKALAISDR 205
Cdd:PRK13543 184 LRGGGAALVTTHGAYAAPPVRTR 206
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
4-192 |
1.41e-12 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 63.71 E-value: 1.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQA-VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEflgqeiqkMPAQKIVAgGLSQ 82
Cdd:cd03223 1 IELENLSLATPDGRVlLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------MPEGEDLL-FLPQ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 VPegrhVFPGLTVMENLemgaflkknreenqanlkkvfsRFPRLEErknqdaatLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:cd03223 72 RP----YLPLGTLREQL----------------------IYPWDDV--------LSGGEQQRLAFARLLLHKPKFVFLDE 117
|
170 180 190
....*....|....*....|....*....|
gi 444285220 163 PSMGLAPifiQEIFDIIQDIQKQGTTVLLI 192
Cdd:cd03223 118 ATSALDE---ESEDRLYQLLKELGITVISV 144
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
4-223 |
1.55e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 65.76 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY----------GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQ 73
Cdd:PRK11308 6 LQAIDLKKHYpvkrglfkpeRLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 74 ---------KIVAgglsQVPEG----RHVFpGLTVMENLEMGAFLKK--NREENQANLKKV------FSRFPRLeerknq 132
Cdd:PRK11308 86 aqkllrqkiQIVF----QNPYGslnpRKKV-GQILEEPLLINTSLSAaeRREKALAMMAKVglrpehYDRYPHM------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 133 daatLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLaPIFIQ-EIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLE 210
Cdd:PRK11308 155 ----FSGGQRQRIAIARALMLDPDVVVADEPVSAL-DVSVQaQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMY 229
|
250
....*....|...
gi 444285220 211 TGKIVLSGTGKEL 223
Cdd:PRK11308 230 LGRCVEKGTKEQI 242
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
8-225 |
1.87e-12 |
|
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 65.26 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 8 NLSVHYGMIqaVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlgqeiqkmpaqkivAGGLSQVPEGR 87
Cdd:cd03291 44 NLCLVGAPV--LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKH--------------SGRISFSSQFS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 88 HVFPGlTVMENLEMGAFLKKNREEN---QANLKKVFSRFPrleERKN----QDAATLSGGEQQMLAMGRALMSTPKLLLL 160
Cdd:cd03291 108 WIMPG-TIKENIIFGVSYDEYRYKSvvkACQLEEDITKFP---EKDNtvlgEGGITLSGGQRARISLARAVYKDADLYLL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 161 DEPSMGLAPIFIQEIFD-IIQDIQKQGTTVLLieQNANKALAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:cd03291 184 DSPFGYLDVFTEKEIFEsCVCKLMANKTRILV--TSKMEHLKKADKILILHEGSSYFYGTFSELQS 247
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
25-164 |
1.96e-12 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 64.74 E-value: 1.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 25 EVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIVAGglsqvpegrhvFPGlTVMENLemgaF 104
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKP-QYIKAD-----------YEG-TVRDLL----S 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 105 LKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:cd03237 84 SITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPS 143
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-163 |
2.26e-12 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 65.68 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlgqeiqkmpAQKIVAGGLSQV 83
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW---------SENANIGYYAQD 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEgrHVFPG-LTVMEnlEMGAFlKKNREENQAnlkkVFSRFPRL---EERKNQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:PRK15064 391 HA--YDFENdLTLFD--WMSQW-RQEGDDEQA----VRGTLGRLlfsQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461
|
....
gi 444285220 160 LDEP 163
Cdd:PRK15064 462 MDEP 465
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-226 |
3.39e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.11 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVR----DVSFEVNEGEVVSLIGANGAGKT----TILRTL-SGLVRPSSGKIEFLGQEIQKMP 71
Cdd:PRK15134 3 QPLLAIENLSVAFRQQQTVRtvvnDVSLQIEAGETLALVGESGSGKSvtalSILRLLpSPPVVYPSGDIRFHGESLLHAS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 72 AQKI--VAGG----LSQVPegrhvFPGLTVMENLEM----------GAFLKKNREENQANLKKVFSRFP--RLEERKNQd 133
Cdd:PRK15134 83 EQTLrgVRGNkiamIFQEP-----MVSLNPLHTLEKqlyevlslhrGMRREAARGEILNCLDRVGIRQAakRLTDYPHQ- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 134 aatLSGGEQQ--MLAMgrALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ-GTTVLLIEQNANKALAISDRGYVLE 210
Cdd:PRK15134 157 ---LSGGERQrvMIAM--ALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQ 231
|
250
....*....|....*.
gi 444285220 211 TGKIVLSGTGKELASS 226
Cdd:PRK15134 232 NGRCVEQNRAATLFSA 247
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-164 |
5.55e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 64.75 E-value: 5.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEfLGQEIQkmpaqkivaggLSQV 83
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIK-IGETVK-----------LAYV 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGR-HVFPGLTVMEN-------LEMGaflkkNREENqanlkkvfSR-------FprleerKNQD----AATLSGGEQQM 144
Cdd:PRK11819 393 DQSRdALDPNKTVWEEisggldiIKVG-----NREIP--------SRayvgrfnF------KGGDqqkkVGVLSGGERNR 453
|
170 180
....*....|....*....|
gi 444285220 145 LAMGRALMSTPKLLLLDEPS 164
Cdd:PRK11819 454 LHLAKTLKQGGNVLLLDEPT 473
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
28-204 |
5.64e-12 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.44 E-value: 5.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 28 EGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIE-----------FLGQEIQKMpAQKIVAGGLS---------QVPEgr 87
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrFRGTELQNY-FKKLYNGEIKvvhkpqyvdLIPK-- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 88 hVFPGlTVMEnlemgaFLKKNREENqaNLKKVFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS--- 164
Cdd:PRK13409 175 -VFKG-KVRE------LLKKVDERG--KLDEVVERL-GLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTsyl 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 444285220 165 -----MGLApifiqeifDIIQDIQKqGTTVLLIEQNankaLAISD 204
Cdd:PRK13409 244 dirqrLNVA--------RLIRELAE-GKYVLVVEHD----LAVLD 275
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
8-177 |
1.09e-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: 64.16 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 8 NLSVHygMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlgqeiqkmpaqkivAGGLSQVPEGR 87
Cdd:TIGR01271 433 NFSLY--VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKH--------------SGRISFSPQTS 496
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 88 HVFPGlTVMENLEMGAFLKKNREE---NQANLKKVFSRFPRLEERKNQDAA-TLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:TIGR01271 497 WIMPG-TIKDNIIFGLSYDEYRYTsviKACQLEEDIALFPEKDKTVLGEGGiTLSGGQRARISLARAVYKDADLYLLDSP 575
|
170
....*....|....
gi 444285220 164 SMGLAPIFIQEIFD 177
Cdd:TIGR01271 576 FTHLDVVTEKEIFE 589
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-223 |
1.09e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.28 E-value: 1.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHY----GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLV----RPSSGKIEFLGQEIQKMPA 72
Cdd:PRK15093 1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 73 ---QKIVAGGLS---QVPE---------GRHV---FPGLTVmenlemgaflkKNREENQANLKK--VFSRFPRLEERKNQ 132
Cdd:PRK15093 81 rerRKLVGHNVSmifQEPQscldpservGRQLmqnIPGWTY-----------KGRWWQRFGWRKrrAIELLHRVGIKDHK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 133 DAA-----TLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRG 206
Cdd:PRK15093 150 DAMrsfpyELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSQWADKI 229
|
250
....*....|....*..
gi 444285220 207 YVLETGKIVLSGTGKEL 223
Cdd:PRK15093 230 NVLYCGQTVETAPSKEL 246
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
2-233 |
1.19e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 62.35 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGlvRPS----SGKIEFLGQEIQKMPAQKIVA 77
Cdd:CHL00131 6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKGESILDLEPEERAH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGL---SQVP----------------EGRHVFPGLTVMENLEmgaFLKKNREE-NQANLKKVFsrfprLEERKNQDaatL 137
Cdd:CHL00131 84 LGIflaFQYPieipgvsnadflrlayNSKRKFQGLPELDPLE---FLEIINEKlKLVGMDPSF-----LSRNVNEG---F 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 138 SGGEQ---QMLAMgrALMStPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAIS-DRGYVLETGK 213
Cdd:CHL00131 153 SGGEKkrnEILQM--ALLD-SELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHYQRLLDYIKpDYVHVMQNGK 229
|
250 260
....*....|....*....|
gi 444285220 214 IVLSGtGKELASSEEvRKAY 233
Cdd:CHL00131 230 IIKTG-DAELAKELE-KKGY 247
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
3-185 |
1.78e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQ-----------AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRpSSGKIEFLGQEIQKMP 71
Cdd:PRK15134 275 LLDVEQLQVAFPIRKgilkrtvdhnvVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLIN-SQGEIWFDGQPLHNLN 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 72 AQKIvagglsqVPEGRH---VF--------PGLTVMENLEMGAFLKK---NREENQANLKKVFSRFPRLEERKNQDAATL 137
Cdd:PRK15134 354 RRQL-------LPVRHRiqvVFqdpnsslnPRLNVLQIIEEGLRVHQptlSAAQREQQVIAVMEEVGLDPETRHRYPAEF 426
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 444285220 138 SGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQ 185
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQK 474
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
5-225 |
2.76e-11 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 62.60 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 5 KVENLSVHYgmiqAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIeflgqEIQKMPAQKIVAGGLSQvp 84
Cdd:PRK13545 30 RSKDGEYHY----ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKGSAALIAISSGLNG-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 85 egrhvfpGLTVMENLEM-GAFLKKNREENQANLKKVFSrFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:PRK13545 99 -------QLTGIENIELkGLMMGLTKEKIKEIIPEIIE-FADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 164 SMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKELAS 225
Cdd:PRK13545 171 LSVGDQTFTKKCLDKMNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-163 |
3.26e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 3.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 34 LIGANGAGKTTILRTLSGLVRPSSGkieflgqEIQKMPAQKIvaGGLSQVPegrHVFPGLTVMENLEMG-----AFLKKN 108
Cdd:PRK11819 38 VLGLNGAGKSTLLRIMAGVDKEFEG-------EARPAPGIKV--GYLPQEP---QLDPEKTVRENVEEGvaevkAALDRF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 109 RE------ENQANLKKVFSRFPRLEER------------------------KNQDAATLSGGEQQMLAMGRALMSTPKLL 158
Cdd:PRK11819 106 NEiyaayaEPDADFDALAAEQGELQEIidaadawdldsqleiamdalrcppWDAKVTKLSGGERRRVALCRLLLEKPDML 185
|
....*
gi 444285220 159 LLDEP 163
Cdd:PRK11819 186 LLDEP 190
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-192 |
3.43e-11 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 62.34 E-value: 3.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 1 MSMLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMP---AQKIVA 77
Cdd:PRK10938 1 MSSLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSfeqLQKLVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 --------GGLSQVPEGRhvfpGLTVMENLEMGafLKKNreENQANLKKVFSRFPRLEERKNQdaatLSGGEQQMLAMGR 149
Cdd:PRK10938 81 dewqrnntDMLSPGEDDT----GRTTAEIIQDE--VKDP--ARCEQLAQQFGITALLDRRFKY----LSTGETRKTLLCQ 148
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 444285220 150 ALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLI 192
Cdd:PRK10938 149 ALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
4-195 |
3.45e-11 |
|
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: 60.03 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHygmiqAVRDVSFEVNEGEVVSLIGANGAGKTTILrtlsglvrpssgkieflgQEIQKMPAQKIVAGGLSQV 83
Cdd:cd03238 1 LTVSGANVH-----NLQNLDVSIPLNVLVVVTGVSGSGKSTLV------------------NEGLYASGKARLISFLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPG-LTVMENLEMGaFLKKNREenqanlkkvfsrfprleerknqdAATLSGGEQQMLAMGRALMSTPK--LLLL 160
Cdd:cd03238 58 SRNKLIFIDqLQFLIDVGLG-YLTLGQK-----------------------LSTLSGGELQRVKLASELFSEPPgtLFIL 113
|
170 180 190
....*....|....*....|....*....|....*
gi 444285220 161 DEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQN 195
Cdd:cd03238 114 DEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEHN 148
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
4-231 |
3.53e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.30 E-value: 3.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG-MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEI--QKMPA-QKIVAGG 79
Cdd:PRK10522 323 LELRNVTFAYQdNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtaEQPEDyRKLFSAV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQV--------PEGRHVFPGL--TVMENLEMGAflKKNREENQ-ANLKkvfsrfprleerknqdaatLSGGEQQMLAMG 148
Cdd:PRK10522 403 FTDFhlfdqllgPEGKPANPALveKWLERLKMAH--KLELEDGRiSNLK-------------------LSKGQKKRLALL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 149 RALMSTPKLLLLDEPSMGLAPIFIQEIF-DIIQDIQKQGTTVllieqnankaLAIS---------DRGYVLETGKIV-LS 217
Cdd:PRK10522 462 LALAEERDILLLDEWAADQDPHFRREFYqVLLPLLQEMGKTI----------FAIShddhyfihaDRLLEMRNGQLSeLT 531
|
250
....*....|....
gi 444285220 218 GTGKELASSEEVRK 231
Cdd:PRK10522 532 GEERDAASRDAVAR 545
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-192 |
3.97e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 60.74 E-value: 3.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 20 RDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLV--RPSSGKIEFLGQEI-QKMPaqkivagGLSQVPegrHVFPGLTVM 96
Cdd:COG2401 47 RDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFgREAS-------LIDAIG---RKGDFKDAV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 97 ENLemgaflkknreeNQANLKKVFSRFPRLEErknqdaatLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIF 176
Cdd:COG2401 117 ELL------------NAVGLSDAVLWLRRFKE--------LSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVA 176
|
170
....*....|....*..
gi 444285220 177 DIIQDI-QKQGTTVLLI 192
Cdd:COG2401 177 RNLQKLaRRAGITLVVA 193
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
25-164 |
6.79e-11 |
|
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: 61.34 E-value: 6.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 25 EVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlGQEIQKMPaQKIVAGglsqvpegrhvFPGlTVMENLEmgaf 104
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDE-DLKISYKP-QYISPD-----------YDG-TVEEFLR---- 423
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 105 lKKNREENQANLKK--VFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:COG1245 424 -SANTDDFGSSYYKteIIKPL-GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 483
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-218 |
6.98e-11 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 60.48 E-value: 6.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 2 SMLKVENLSVhYGMIQAVRDVSFEVNEGEVVSLIGANGAGKT----TILRTLSGLVRPSSGKIEFLGQEiqkmpaqkIVA 77
Cdd:PRK10418 3 QQIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKP--------VAP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 78 GGLsqvpEGRHVfpgLTVMEN---------------LEMGAFLKKNREENQ----------ANLKKVFSRFPrleerknq 132
Cdd:PRK10418 74 CAL----RGRKI---ATIMQNprsafnplhtmhthaRETCLALGKPADDATltaaleavglENAARVLKLYP-------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 133 daATLSGGEQQ--MLAMgrALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI-QKQGTTVLLIEQNANKALAISDRGYVL 209
Cdd:PRK10418 139 --FEMSGGMLQrmMIAL--ALLCEAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVM 214
|
....*....
gi 444285220 210 ETGKIVLSG 218
Cdd:PRK10418 215 SHGRIVEQG 223
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
4-213 |
7.34e-11 |
|
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: 59.41 E-value: 7.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYG-----MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEflgqeiqkmpaqkiVAG 78
Cdd:cd03250 1 ISVEDASFTWDsgeqeTSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVS--------------VPG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLSQVPEGRHVFPGlTVMENLEMGAflkknrEENQANLKKV---------FSRFPRLE-----ERknqdAATLSGGEQQM 144
Cdd:cd03250 67 SIAYVSQEPWIQNG-TIRENILFGK------PFDEERYEKVikacalepdLEILPDGDlteigEK----GINLSGGQKQR 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 145 LAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFD-IIQDIQKQGTTVLLIEQNANkALAISDRGYVLETGK 213
Cdd:cd03250 136 ISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
66-234 |
7.81e-11 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 61.38 E-value: 7.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 66 EIQKMPAQKIVAGgLSQVPEgrhvfPGLTVMENLEmgAFlkKNREENQANLKkvfsrFPRLEerKNQDAATLSGGEQQML 145
Cdd:PRK00635 423 EFQQMSLQELFIF-LSQLPS-----KSLSIEEVLQ--GL--KSRLSILIDLG-----LPYLT--PERALATLSGGEQERT 485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 146 A----MGRALMSTpkLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNaNKALAISDR------GYVLETGKIV 215
Cdd:PRK00635 486 AlakhLGAELIGI--TYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRiidigpGAGIFGGEVL 562
|
170 180
....*....|....*....|
gi 444285220 216 LSGTGKE-LASSEEVRKAYL 234
Cdd:PRK00635 563 FNGSPREfLAKSDSLTAKYL 582
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-233 |
9.02e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 60.21 E-value: 9.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQeiqkMPAQKIVAGGLSQvpegrhvfpgLTVME 97
Cdd:PRK13546 39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----VSVIAISAGLSGQ----------LTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 98 NLEMGAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFD 177
Cdd:PRK13546 105 NIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 444285220 178 IIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIvlsgtgKELASSEEVRKAY 233
Cdd:PRK13546 185 KIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL------KDYGELDDVLPKY 234
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
6-223 |
1.26e-10 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 60.50 E-value: 1.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYGMIQAV-RDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQkIVAGGLSQVP 84
Cdd:PRK10790 343 IDNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHS-VLRQGVAMVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 85 EGRHVFPGlTVMENLEMGAFLKKNR-----EENQ-ANLKKVFSR--FPRLEERKNqdaaTLSGGEQQMLAMGRALMSTPK 156
Cdd:PRK10790 422 QDPVVLAD-TFLANVTLGRDISEEQvwqalETVQlAELARSLPDglYTPLGEQGN----NLSVGQKQLLALARVLVQTPQ 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 157 LLLLDEPSMGLAPIFIQEIFDIIQDIQKQgTTVLLIeqnANKALAI--SDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK10790 497 ILILDEATANIDSGTEQAIQQALAAVREH-TTLVVI---AHRLSTIveADTILVLHRGQAVEQGTHQQL 561
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-204 |
1.68e-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: 59.30 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 28 EGEVVSLIGANGAGKTTILRTLSGLVRPSSGKI-----------EFLGQEIQKMpAQKIVAGGLSQVPEGRHV------F 90
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFddppdwdeildEFRGSELQNY-FTKLLEGDVKVIVKPQYVdlipkaV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 91 PGlTVMENLEmgaflKKNREENQANLKKVFSrfprLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLApi 170
Cdd:cd03236 104 KG-KVGELLK-----KKDERGKLDELVDQLE----LRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD-- 171
|
170 180 190
....*....|....*....|....*....|....*..
gi 444285220 171 fIQEIFD---IIQDIQKQGTTVLLIEQNankaLAISD 204
Cdd:cd03236 172 -IKQRLNaarLIRELAEDDNYVLVVEHD----LAVLD 203
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
18-223 |
1.83e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.03 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 18 AVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIvAGGLSQVPEGRHVFPGlTVME 97
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASL-RNQVALVSQNVHLFND-TIAN 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 98 NLEMGAFLKKNRE--ENQANLKKVFSRFPRLEERKN----QDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGL---A 168
Cdd:PRK11176 436 NIAYARTEQYSREqiEEAARMAYAMDFINKMDNGLDtvigENGVLLSGGQRQRIAIARALLRDSPILILDEATSALdteS 515
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 169 PIFIQEIFDIIQdiqkQGTTVLLIeqnANKALAI--SDRGYVLETGKIVLSGTGKEL 223
Cdd:PRK11176 516 ERAIQAALDELQ----KNRTSLVI---AHRLSTIekADEILVVEDGEIVERGTHAEL 565
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-231 |
3.57e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.60 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSgkieflgqeiqkmPAQKIVAGGLSQVPEGRHVFPGlTVMENLE 100
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE-------------TSSVVIRGSVAYVPQVSWIFNA-TVRENIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 101 MGAFLKKNREENQAN---LKKVFSRFP-RLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIF 176
Cdd:PLN03232 701 FGSDFESERYWRAIDvtaLQHDLDLLPgRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 177 DIIQDIQKQGTTVLLIeQNANKALAISDRGYVLETGKIVLSGTGKELASSEEVRK 231
Cdd:PLN03232 781 DSCMKDELKGKTRVLV-TNQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFK 834
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
20-223 |
3.71e-10 |
|
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: 59.06 E-value: 3.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 20 RDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIVAGGLSQVPEGrhvfpglTVM--- 96
Cdd:COG5265 375 KGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVT-QASLRAAIGIVPQD-------TVLfnd 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 97 ---ENLEMGAfLKKNREE-----NQANLKKVFSRFP-----RLEER--KnqdaatLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:COG5265 447 tiaYNIAYGR-PDASEEEveaaaRAAQIHDFIESLPdgydtRVGERglK------LSGGEKQRVAIARTLLKNPPILIFD 519
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 162 EPSMGLAPIFIQEIFDIIQDIqKQGTTVLLIE------QNAnkalaisDRGYVLETGKIVLSGTGKEL 223
Cdd:COG5265 520 EATSALDSRTERAIQAALREV-ARGRTTLVIAhrlstiVDA-------DEILVLEAGRIVERGTHAEL 579
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
8-223 |
3.89e-10 |
|
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: 59.57 E-value: 3.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 8 NLSVHY--GMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAgGLSQVPE 85
Cdd:TIGR00957 1289 NYCLRYreDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF-KITIIPQ 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 86 GRHVFPGLTVMeNLEmgAFLKKNREE-----NQANLKKVFSRFP-RLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLL 159
Cdd:TIGR00957 1368 DPVLFSGSLRM-NLD--PFSQYSDEEvwwalELAHLKTFVSALPdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILV 1444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 160 LDEPSMGLApifiQEIFDIIQD---IQKQGTTVLLIEQNANKALAISdRGYVLETGKIVLSGTGKEL 223
Cdd:TIGR00957 1445 LDEATAAVD----LETDNLIQStirTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNL 1506
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-164 |
5.65e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 58.67 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 25 EVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlGQEIQKMPaQKIVAGglsqvpegrhvFPGlTVMEnlemgaF 104
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYKP-QYIKPD-----------YDG-TVED------L 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 444285220 105 LKKNREENQANLKK--VFSRFpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:PRK13409 421 LRSITDDLGSSYYKseIIKPL-QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPS 481
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
132-224 |
1.10e-09 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 58.10 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 132 QDAATLSGGEQQMLAMGRALM--ST-PKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANkalAISDRGYV 208
Cdd:TIGR00630 825 QPATTLSGGEAQRIKLAKELSkrSTgRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLD---VIKTADYI 901
|
90 100
....*....|....*....|....
gi 444285220 209 LET--------GKIVLSGTGKELA 224
Cdd:TIGR00630 902 IDLgpeggdggGTVVASGTPEEVA 925
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-190 |
1.27e-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: 55.71 E-value: 1.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEGEVVSLIGANGAGKTTILRTLSGlvRPSSGKIE----FLGQEIQKmpAQKIVAGGLSQVPegRHvFPGLTVM 96
Cdd:cd03232 25 NISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVITgeilINGRPLDK--NFQRSTGYVEQQD--VH-SPNLTVR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 97 ENLEMGAFLkknreenqanlkkvfsRFPRLEERKnqdaatlsggeqqMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIF 176
Cdd:cd03232 98 EALRFSALL----------------RGLSVEQRK-------------RLTIGVELAAKPSILFLDEPTSGLDSQAAYNIV 148
|
170
....*....|....
gi 444285220 177 DIIQDIQKQGTTVL 190
Cdd:cd03232 149 RFLKKLADSGQAIL 162
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-163 |
2.62e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 2.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 6 VENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlgqeiqkmpAQKIVAGGLSQVPE 85
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC---------GTKLEVAYFDQHRA 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 86 grHVFPGLTVMENLEMGaflkknREENQANLKK----------VFSrfPRleeRKNQDAATLSGGEQQMLAMGRALMSTP 155
Cdd:PRK11147 393 --ELDPEKTVMDNLAEG------KQEVMVNGRPrhvlgylqdfLFH--PK---RAMTPVKALSGGERNRLLLARLFLKPS 459
|
....*...
gi 444285220 156 KLLLLDEP 163
Cdd:PRK11147 460 NLLILDEP 467
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
132-219 |
7.42e-09 |
|
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: 54.54 E-value: 7.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 132 QDAATLSGGEQQMLAMGRALM--STPK-LLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANkALAISDrgYV 208
Cdd:cd03271 165 QPATTLSGGEAQRIKLAKELSkrSTGKtLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLD-VIKCAD--WI 241
|
90
....*....|....*....
gi 444285220 209 LET--------GKIVLSGT 219
Cdd:cd03271 242 IDLgpeggdggGQVVASGT 260
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-222 |
1.10e-08 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 54.89 E-value: 1.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 29 GEVVSLIGANGAGKTTILRTLSGLVRPSS--GKIEFLGQEIQKMPAQKIvagglSQVPEGRHVFPGLTVMENLEMGAFLK 106
Cdd:PLN03211 94 GEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQILKRT-----GFVTQDDILYPHLTVRETLVFCSLLR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 107 KNRE-ENQANLKKVFSRFPRLEERK-------NQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGL-APIFIQEIFD 177
Cdd:PLN03211 169 LPKSlTKQEKILVAESVISELGLTKcentiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLdATAAYRLVLT 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 444285220 178 IIQDIQKQGTTVLLIEQNANKALAISDRGYVLETGKIVLSGTGKE 222
Cdd:PLN03211 249 LGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-224 |
1.27e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQkmpaqkivAGGL-------SQVPEGRHVFP 91
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIG--------AYGLrelrrqfSMIPQDPVLFD 1397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 92 GlTVMENLEmgAFLKKNREENQANLKKVFSRFPRLEERKNQDAATLSG------GEQQMLAMGRALMST-PKLLLLDEPS 164
Cdd:PTZ00243 1398 G-TVRQNVD--PFLEASSAEVWAALELVGLRERVASESEGIDSRVLEGgsnysvGQRQLMCMARALLKKgSGFILMDEAT 1474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 165 MGLAPIFiqeifdiiqDIQKQGT--------TVLLIEQNANkALAISDRGYVLETGKIVLSGTGKELA 224
Cdd:PTZ00243 1475 ANIDPAL---------DRQIQATvmsafsayTVITIAHRLH-TVAQYDKIIVMDHGAVAEMGSPRELV 1532
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
22-67 |
1.49e-08 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 54.42 E-value: 1.49e-08
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 444285220 22 VSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEI 67
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV 396
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-218 |
1.54e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 54.73 E-value: 1.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 15 MIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLS----GLVRPSSGKIEFLG---QEIQKMPAQKIVAGGLSQVpegr 87
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGitpEEIKKHYRGDVVYNAETDV---- 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 88 HvFPGLTVMENLEMGAFLKK--------NREENQANLKKVFSRFPRLEERKNQDAAT-----LSGGEQQMLAMGRALMST 154
Cdd:TIGR00956 149 H-FPHLTVGETLDFAARCKTpqnrpdgvSREEYAKHIADVYMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 155 PKLLLLDEPSMGL----APIFIQEIfDIIQDIQKqgTTVLL-IEQNANKALAISDRGYVLETGKIVLSG 218
Cdd:TIGR00956 228 AKIQCWDNATRGLdsatALEFIRAL-KTSANILD--TTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFG 293
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
136-212 |
1.69e-08 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 54.45 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 136 TLSGGEQQMLAMGRALMST---PKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANkALAISDrgYVLETG 212
Cdd:PRK00635 809 SLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMH-VVKVAD--YVLELG 885
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
131-193 |
2.78e-08 |
|
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: 52.65 E-value: 2.78e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 131 NQDAATLSGGEQQMLAMGRALMS--TPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIE 193
Cdd:cd03270 132 SRSAPTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVE 196
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-226 |
6.23e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.82 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGkieflgqeiqkmpAQKIVAGGLSQVPEGRHVFPGlTVMENLE 100
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-------------ASVVIRGTVAYVPQVSWIFNA-TVRDNIL 700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 101 MGAFLKKNREENQ---ANLKKVFSRFP-----RLEERknqdAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFI 172
Cdd:PLN03130 701 FGSPFDPERYERAidvTALQHDLDLLPggdltEIGER----GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVG 776
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 173 QEIFD-IIQDIQKQGTTVLLIEQnaNKALAISDRGYVLETGKIVLSGTGKELASS 226
Cdd:PLN03130 777 RQVFDkCIKDELRGKTRVLVTNQ--LHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
131-236 |
7.44e-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: 52.32 E-value: 7.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 131 NQDAATLSGGEQQMLAMGRALMS--TPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANkalAISDRGYV 208
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSglTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDED---TIRAADYV 559
|
90 100 110
....*....|....*....|....*....|....*..
gi 444285220 209 LET--------GKIVLSGTGKE-LASSEEVRKAYLGG 236
Cdd:TIGR00630 560 IDIgpgagehgGEVVASGTPEEiLANPDSLTGQYLSG 596
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
4-167 |
8.21e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 8.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGM---IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKI-----EFLGQEIQKMPAQKI 75
Cdd:PTZ00265 383 IQFKNVRFHYDTrkdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIiindsHNLKDINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 76 vaGGLSQVPE------GRHVFPGLTVMENLE-MGAFLKKNREENQANLKKVFSRFPR-----------------LEERKN 131
Cdd:PTZ00265 463 --GVVSQDPLlfsnsiKNNIKYSLYSLKDLEaLSNYYNEDGNDSQENKNKRNSCRAKcagdlndmsnttdsnelIEMRKN 540
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 132 ----------------------------------QDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGL 167
Cdd:PTZ00265 541 yqtikdsevvdvskkvlihdfvsalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSL 610
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
36-162 |
1.31e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 50.26 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 36 GANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKM--PAQKIVAGGLSQVPEgrhvfpgLTVMENLEMGAFLKKNREENQ 113
Cdd:PRK13541 33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIakPYCTYIGHNLGLKLE-------MTVFENLKFWSEIYNSAETLY 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 444285220 114 ANLkkvfsRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDE 162
Cdd:PRK13541 106 AAI-----HYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
26-167 |
4.01e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 4.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 26 VNEGEVVSLIGANGAGKTTILRTLSGlvRPSSGKIEF-----LGQEIQKMPAQKIvaGGLSQvpEGRHVfPGLTVMENLE 100
Cdd:TIGR00956 786 VKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGgdrlvNGRPLDSSFQRSI--GYVQQ--QDLHL-PTSTVRESLR 858
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 101 MGAFLKK----NREENQANLKKVFSrfpRLEERKNQDAATLSGGE------QQMLAMGRALMSTPKLLL-LDEPSMGL 167
Cdd:TIGR00956 859 FSAYLRQpksvSKSEKMEYVEEVIK---LLEMESYADAVVGVPGEglnveqRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
19-181 |
1.11e-06 |
|
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: 48.98 E-value: 1.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGL--------VRPSSGKIEFLGQE------------IQKMPAQKIVAG 78
Cdd:TIGR00954 468 IESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYVPQRpymtlgtlrdqiIYPDSSEDMKRR 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 79 GLS-QVPEgrhvfpglTVMENLEMGAFLKKNRE-ENQANLKKVfsrfprleerknqdaatLSGGEQQMLAMGRALMSTPK 156
Cdd:TIGR00954 548 GLSdKDLE--------QILDNVQLTHILEREGGwSAVQDWMDV-----------------LSGGEKQRIAMARLFYHKPQ 602
|
170 180
....*....|....*....|....*
gi 444285220 157 LLLLDEPSMGLAPIFIQEIFDIIQD 181
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRLCRE 627
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
25-210 |
1.25e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 47.18 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 25 EVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPaQKIvagglsqvpegrhvfpgltvmenlemgaf 104
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYKP-QYI----------------------------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 105 lkknreenqanlkkvfsrfprleerknqdaaTLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLapifiqeifDIIQD--- 181
Cdd:cd03222 71 -------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYL---------DIEQRlna 110
|
170 180 190
....*....|....*....|....*....|....*.
gi 444285220 182 -------IQKQGTTVLLIEQNANKALAISDRGYVLE 210
Cdd:cd03222 111 arairrlSEEGKKTALVVEHDLAVLDYLSDRIHVFE 146
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
16-167 |
1.36e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 48.69 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 16 IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGlvRPSSGKIEflGQ-EIQKMPAQKIVAGGLSQVPEGRHVF-PGL 93
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE--GDiRISGFPKKQETFARISGYCEQNDIHsPQV 968
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 94 TVMENLEMGAFLKKNREENQANLKKVFSRFPRLEERKN-QDAAT-------LSGGEQQMLAMGRALMSTPKLLLLDEPSM 165
Cdd:PLN03140 969 TVRESLIYSAFLRLPKEVSKEEKMMFVDEVMELVELDNlKDAIVglpgvtgLSTEQRKRLTIAVELVANPSIIFMDEPTS 1048
|
..
gi 444285220 166 GL 167
Cdd:PLN03140 1049 GL 1050
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
22-223 |
2.31e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.02 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 22 VSFEVNEGEVVSLIGANGAGKTTILRTLSGlvrpssgkieflgqEIQKMPAQKIVAGGLSQVPEGRHVfPGLTVMENLEM 101
Cdd:TIGR00957 657 ITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKVEGHVHMKGSVAYVPQQAWI-QNDSLRENILF 721
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 102 GAFLKKNREenQANLKKVfSRFPRLEERKNQD-------AATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQE 174
Cdd:TIGR00957 722 GKALNEKYY--QQVLEAC-ALLPDLEILPSGDrteigekGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKH 798
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 444285220 175 IFDII---QDIQKQGTTVLLieQNANKALAISDRGYVLETGKIVLSGTGKEL 223
Cdd:TIGR00957 799 IFEHVigpEGVLKNKTRILV--THGISYLPQVDVIIVMSGGKISEMGSYQEL 848
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
136-234 |
2.31e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.10 E-value: 2.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 136 TLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAISDRGYVL----ET 211
Cdd:PTZ00265 1358 SLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVFnnpdRT 1437
|
90 100
....*....|....*....|....*
gi 444285220 212 GKIVLS-GTGKELASSEE-VRKAYL 234
Cdd:PTZ00265 1438 GSFVQAhGTHEELLSVQDgVYKKYV 1462
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-164 |
3.06e-06 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 47.47 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFlgqeiqkmpAQKIVAGGLSQ 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYFAQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 83 vpegrHVFPGLTVMEN-LEMGAFLKKNREENQanLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLD 161
Cdd:PRK10636 383 -----HQLEFLRADESpLQHLARLAPQELEQK--LRDYLGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLD 455
|
...
gi 444285220 162 EPS 164
Cdd:PRK10636 456 EPT 458
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-164 |
4.04e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.16 E-value: 4.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 20 RDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIeFLGQEIQ-KMPAQKIVAG-GLSQVP--EGRHVFPGLTv 95
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-FRSAKVRmAVFSQHHVDGlDLSSNPllYMMRCFPGVP- 603
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 96 menlemgaflkknreenQANLKKVFSRFPRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:PLN03073 604 -----------------EQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPS 655
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
19-191 |
2.30e-05 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 44.61 E-value: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVsLIGANGAGKTTILRTLSGLVRPSSGK----------IEFLGQEIQ-----KMPAQKIVAGGLSQV 83
Cdd:COG3593 14 IKDLSIELSDDLTV-LVGENNSGKSSILEALRLLLGPSSSRkfdeedfylgDDPDLPEIEieltfGSLLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 84 PEGRHVFPGLTVMENLE---------MGAFLKKNREENQANLKKVFSRFP--------RLEERKNQDAATLSGGEQQM-- 144
Cdd:COG3593 93 DKEELEEALEELNEELKealkalnelLSEYLKELLDGLDLELELSLDELEdllkslslRIEDGKELPLDRLGSGFQRLil 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 444285220 145 LAMGRALM-----STPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLL 191
Cdd:COG3593 173 LALLSALAelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVII 224
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
132-228 |
3.23e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.68 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 132 QDAATLSGGEQQMLAMGRALM--STPK-LLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNankaLAI------ 202
Cdd:PRK00349 826 QPATTLSGGEAQRVKLAKELSkrSTGKtLYILDEPTTGLHFEDIRKLLEVLHRLVDKGNTVVVIEHN----LDViktadw 901
|
90 100 110
....*....|....*....|....*....|....
gi 444285220 203 --------SDRGyvletGKIVLSGTGKELASSEE 228
Cdd:PRK00349 902 iidlgpegGDGG-----GEIVATGTPEEVAKVEA 930
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
19-163 |
4.10e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.38 E-value: 4.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 19 VRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIeFLGQEIQKMPAQKIVagglsqvpegrhvfpgltvmen 98
Cdd:PTZ00243 676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-WAERSIAYVPQQAWI---------------------- 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 99 leMGAFLKKN----REENQANLKKVFsRFPRLEERKNQDAA-----------TLSGGEQQMLAMGRALMSTPKLLLLDEP 163
Cdd:PTZ00243 733 --MNATVRGNilffDEEDAARLADAV-RVSQLEADLAQLGGgleteigekgvNLSGGQKARVSLARAVYANRDVYLLDDP 809
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
132-195 |
4.58e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 43.86 E-value: 4.58e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 132 QDAATLSGGEQQMLAMGRALM--STPK-LLLLDEPSMGLApifiqeiFDiiqDIQK----------QGTTVLLIEQN 195
Cdd:COG0178 822 QPATTLSGGEAQRVKLASELSkrSTGKtLYILDEPTTGLH-------FH---DIRKllevlhrlvdKGNTVVVIEHN 888
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
16-192 |
5.55e-05 |
|
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: 42.70 E-value: 5.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 16 IQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAGGLSQVPEGRHVfPGL-- 93
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQK-PWLln 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 94 -TVMENLEMGAFLKKNREE---NQANLKKVFSRFPRLEERK-NQDAATLSGGEQQMLAMGRALMSTPKLLLLDEP----S 164
Cdd:cd03290 93 aTVEENITFGSPFNKQRYKavtDACSLQPDIDLLPFGDQTEiGERGINLSGGQRQRICVARALYQNTNIVFLDDPfsalD 172
|
170 180
....*....|....*....|....*....
gi 444285220 165 MGLAPIFIQE-IFDIIQDIQKqgtTVLLI 192
Cdd:cd03290 173 IHLSDHLMQEgILKFLQDDKR---TLVLV 198
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
3-67 |
1.55e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.70 E-value: 1.55e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGL--VRPSSGKIEFLGQEI 67
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDL 67
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
137-191 |
1.79e-04 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 41.92 E-value: 1.79e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 444285220 137 LSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLL 191
Cdd:PRK10938 402 LSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLL 456
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-60 |
1.94e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.80 E-value: 1.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 444285220 3 MLKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKI 60
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV 58
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
134-236 |
2.03e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.94 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 134 AATLSGGEQQ--MLA--MGRALMSTpkLLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNANKALAiSDrgYVL 209
Cdd:COG0178 483 AGTLSGGEAQriRLAtqIGSGLVGV--LYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRA-AD--YII 557
|
90 100 110
....*....|....*....|....*....|....*.
gi 444285220 210 ET--------GKIVLSGTGKELASSEE-VRKAYLGG 236
Cdd:COG0178 558 DIgpgagehgGEVVAQGTPEEILKNPDsLTGQYLSG 593
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
80-236 |
2.63e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.74 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 80 LSQ--VPEGRHvFPGL---TVMENLEMGAFLKKNREENQANLKKVFSRFPRleerkNQDAATLSGGEQQMLAMGRALMST 154
Cdd:PRK00635 1644 LAQevVYEGKH-FGQLlqtPIEEVAETFPFLKKIQKPLQALIDNGLGYLPL-----GQNLSSLSLSEKIAIKIAKFLYLP 1717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 155 PK---LLLLDEPSMGLAPIFIQEIFDIIQDIQKQGTTVLLIEQNAnKALAISDrgYVLETG--------KIVLSGTGKEL 223
Cdd:PRK00635 1718 PKhptLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQAD--YLIEMGpgsgktggKILFSGPPKDI 1794
|
170
....*....|....
gi 444285220 224 ASSEE-VRKAYLGG 236
Cdd:PRK00635 1795 SASKDsLLKTYMCN 1808
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
4-164 |
6.66e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 40.61 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHYGMIQAVRDVSFEVNEGEVVSLIGANGAGKTTILRTLS-----GLvrPSSGKIEFLGQEI---QKMPAQKI 75
Cdd:PLN03073 178 IHMENFSISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAmhaidGI--PKNCQILHVEQEVvgdDTTALQCV 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 76 VAGGLSQVPEGRHVFPGLTVMENLEMGAFLKKNREENQANLKK--VFSR----FPRLE---------------------- 127
Cdd:PLN03073 256 LNTDIERTQLLEEEAQLVAQQRELEFETETGKGKGANKDGVDKdaVSQRleeiYKRLElidaytaearaasilaglsftp 335
|
170 180 190
....*....|....*....|....*....|....*..
gi 444285220 128 ERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPS 164
Cdd:PLN03073 336 EMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPT 372
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
4-162 |
8.92e-04 |
|
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: 39.51 E-value: 8.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 4 LKVENLSVHY-GMIQAV-RDVSFEVNEGEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGQEIQKMPAQKIVAgGLS 81
Cdd:cd03288 20 IKIHDLCVRYeNNLKPVlKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRS-RLS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 82 QVPEGRHVFPGlTVMENLEMGAFLKKNR---EENQANLKKVFSRFP-RLEERKNQDAATLSGGEQQMLAMGRALMSTPKL 157
Cdd:cd03288 99 IILQDPILFSG-SIRFNLDPECKCTDDRlweALEIAQLKNMVKSLPgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSI 177
|
....*
gi 444285220 158 LLLDE 162
Cdd:cd03288 178 LIMDE 182
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
29-192 |
1.97e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 37.74 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 29 GEVVSLIGANGAGKTTILRTLSGLVRPSSGKIEFLGqeiqkmpaqkivagglsqvpegrhvfpgltvMENLEMGAFLKkn 108
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYID-------------------------------GEDILEEVLDQ-- 48
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 109 reenqanlkkvfsrfpRLEERKNQDAATLSGGEQQMLAMGRALMSTPKLLLLDEPSMGLAPIFIQEIFDII------QDI 182
Cdd:smart00382 49 ----------------LLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrlllLLK 112
|
170
....*....|
gi 444285220 183 QKQGTTVLLI 192
Cdd:smart00382 113 SEKNLTVILT 122
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
21-193 |
4.04e-03 |
|
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: 36.95 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFevNEGEVVSLIGANGAGKTTILRTLSGLVrpssgkieflgqeIQKMPAQKIVAGGLSQVPEG-RHVFPGLTVMenl 99
Cdd:cd03227 15 DVTF--GEGSLTIITGPNGSGKSTILDAIGLAL-------------GGAQSATRRRSGVKAGCIVAaVSAELIFTRL--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 100 emgaflkknreenqanlkkvfsrfprleerknqdaaTLSGGEQQMLAM-----GRALMSTPkLLLLDEPSMGLAPIFIQE 174
Cdd:cd03227 77 ------------------------------------QLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLDPRDGQA 119
|
170
....*....|....*....
gi 444285220 175 IFDIIQDIQKQGTTVLLIE 193
Cdd:cd03227 120 LAEAILEHLVKGAQVIVIT 138
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
21-182 |
7.95e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.51 E-value: 7.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 21 DVSFEVNEGEVVsLIGANGAGKTTILRTLSGLVRPSSGKI------EFLGQEIQKMPAQKIVAG----------GLSQVP 84
Cdd:COG3950 18 EIDFDNPPRLTV-LVGENGSGKTTLLEAIALALSGLLSRLddvkfrKLLIRNGEFGDSAKLILYygtsrllldgPLKKLE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 444285220 85 EGRH-VFPGLTVMENL-----EMGAFLK---------KNREENQAN---------LKKVFSRFPRLEERKNQ-------- 132
Cdd:COG3950 97 RLKEeYFSRLDGYDSLldedsNLREFLEwlreyledlENKLSDELDekleavreaLNKLLPDFKDIRIDRDPgrlvildk 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 444285220 133 -----DAATLSGGEQQMLAM--------------GRALMSTPKLLLLDEPSMGLAPIFIQEIFDIIQDI 182
Cdd:COG3950 177 ngeelPLNQLSDGERSLLALvgdlarrlaelnpaLENPLEGEGIVLIDEIDLHLHPKWQRRILPDLRKI 245
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
31-52 |
9.23e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 36.60 E-value: 9.23e-03
|
| |
