|
Name |
Accession |
Description |
Interval |
E-value |
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
21-259 |
3.51e-175 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 481.84 E-value: 3.51e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 21 GLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIG 100
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:COG1137 82 YLPQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLD 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 181 EPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYLGRDFVL 259
Cdd:COG1137 162 EPFAGVDPIAVADIQKIIRHLKERGIGVLITDHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVRKVYLGEDFRL 240
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
23-254 |
2.45e-151 |
|
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: 421.57 E-value: 2.45e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYL 102
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYLG 254
Cdd:cd03218 161 FAGVDPIAVQDIQKIIKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVYLG 232
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
23-259 |
4.51e-136 |
|
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: 383.16 E-value: 4.51e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYL 102
Cdd:TIGR04406 2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTP-LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:TIGR04406 82 PQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYLGRDFVL 259
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRVYLGEQFRL 239
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
22-259 |
5.15e-96 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 281.78 E-value: 5.15e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGY 101
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKAVLEMTP-LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 181 EPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYLGRDFVL 259
Cdd:PRK10895 163 EPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVKRVYLGEDFRL 241
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
23-247 |
2.30e-71 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 218.78 E-value: 2.30e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlgIGYL 102
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR--IGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:COG1131 79 PQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENAL 247
Cdd:COG1131 159 TSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
22-254 |
3.09e-71 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 218.70 E-value: 3.09e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGY 101
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNikavLEM---TPLTPDQQRERLEMLIEEF-GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFI 177
Cdd:COG0410 83 VPEGRRIFPSLTVEEN----LLLgayARRDRAEVRADLERVYELFpRLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 178 MLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYLG 254
Cdd:COG0410 159 LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPEVREAYLG 235
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-245 |
4.52e-70 |
|
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: 214.99 E-value: 4.52e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYL 102
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKavLEMTPLTPDQQRERLEMLIEEF-GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:cd03224 81 PEGRRIFPELTVEENLL--LGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:cd03224 159 PSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
22-256 |
6.87e-70 |
|
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: 215.67 E-value: 6.87e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGY 101
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIK------------AVLEMTPLTPDQQRERLEM---LIEEFGLHKVRTNQGNRLSGGERRRVEI 166
Cdd:COG0411 84 TFQNPRLFPELTVLENVLvaaharlgrgllAALLRLPRARREEREARERaeeLLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 167 ARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQ-RNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRAD 243
|
250
....*....|.
gi 490460070 246 ALVREKYLGRD 256
Cdd:COG0411 244 PRVIEAYLGEE 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
23-248 |
1.55e-68 |
|
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: 1.55e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYL 102
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIK-AVLEMTPLTP---------DQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAI 172
Cdd:cd03219 81 FQIPRLFPELTVLENVMvAAQARTGSGLllararreeREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 173 DPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALV 248
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
22-245 |
1.92e-63 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 198.93 E-value: 1.92e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlgIGY 101
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ--IGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:COG4555 79 LPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:COG4555 159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREE 222
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
22-250 |
1.91e-58 |
|
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: 185.95 E-value: 1.91e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL--GI 99
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELrrRI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFRKLSVEDNIKAVLEM-TPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIM 178
Cdd:COG1127 85 GMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPEILL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL--AENALVRE 250
Cdd:COG1127 165 YDEPTAGLDPITSAVIDELIRELrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELlaSDDPWVRQ 239
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
23-233 |
2.32e-58 |
|
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: 183.37 E-value: 2.32e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlgIGYL 102
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR--IGYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKavlemtpltpdqqrerlemlieefglhkvrtnqgnrLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03230 79 PEEPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEP 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:cd03230 123 TSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
26-242 |
1.66e-56 |
|
ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213228 [Multi-domain] Cd Length: 235 Bit Score: 180.78 E-value: 1.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPV--YQRARLGIGYLA 103
Cdd:cd03261 4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEaeLYRLRRRMGMLF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 104 QEASVFRKLSVEDNIKAVL-EMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03261 84 QSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYDEP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03261 164 TAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
23-234 |
1.13e-53 |
|
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: 173.09 E-value: 1.13e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYL 102
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR---NIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLhkvrTNQGNR----LSGGERRRVEIARCLAIDPKFIM 178
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGL----EGLLNRypheLSGGQQQRVALARALAREPSLLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKLkQRNIG---ILITdHNVNETLSITDRAYLLFEGKVL 234
Cdd:cd03259 154 LDEPLSALDAKLREELREELKEL-QRELGittIYVT-HDQEEALALADRIAVMNEGRIV 210
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
23-251 |
2.10e-52 |
|
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: 170.21 E-value: 2.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYR-SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGY 101
Cdd:COG1122 1 IELENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQ--EASVFRKlSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIML 179
Cdd:COG1122 80 VFQnpDDQLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREK 251
Cdd:COG1122 159 DEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYELLEE 230
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
23-242 |
3.15e-51 |
|
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: 166.91 E-value: 3.15e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVyqRARLGIG 100
Cdd:cd03263 1 LQIRNLTKTYkkGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRK--AARQSLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:cd03263 79 YCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLD 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 181 EPFAGVDPIAVQDIQSIVAKLKqRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03263 159 EPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
22-245 |
2.51e-50 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 168.74 E-value: 2.51e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGY 101
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKR---NVGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLhkvrTNQGNR----LSGGERRRVEIARCLAIDPKFI 177
Cdd:COG3842 82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGL----EGLADRyphqLSGGQQQRVALARALAPEPRVL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 178 MLDEPFAGVDPIAVQDIQSIVAKLkQRNIGI---LITdHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:COG3842 158 LLDEPLSALDAKLREEMREELRRL-QRELGItfiYVT-HDQEEALALADRIAVMNDGRIEQVGTPEEIYER 226
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
22-252 |
6.42e-50 |
|
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: 164.45 E-value: 6.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGY 101
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARR-IAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDnikaVLEM--TPLTP------DQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAID 173
Cdd:COG1120 80 VPQEPPAPFGLTVRE----LVALgrYPHLGlfgrpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 174 PKFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKY 252
Cdd:COG1120 156 PPLLLLDEPTSHLDLAHQLEVLELLRRLaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVY 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
22-252 |
3.47e-48 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 159.87 E-value: 3.47e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDItklpvyQRARLGIGY 101
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------RRARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFR--KLSVEDnikaVLEM--------TPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLA 171
Cdd:COG1121 80 VPQRAEVDWdfPITVRD----VVLMgrygrrglFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 172 IDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLfEGKVLFQGTAEQLAENALVREK 251
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRA 234
|
.
gi 490460070 252 Y 252
Cdd:COG1121 235 Y 235
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
23-250 |
3.63e-48 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 159.23 E-value: 3.63e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYL 102
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEmtpLTPDQQRERLEMLIEEFG-LHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:TIGR03410 81 PQGREIFPRLTVEENLLTGLA---ALPRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 182 PFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEnALVRE 250
Cdd:TIGR03410 158 PTEGIQPSIIKDIGRVIRRLrAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDE-DKVRR 226
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
23-260 |
1.79e-47 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 159.50 E-value: 1.79e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITklpvyQRARLGIGYL 102
Cdd:COG4152 2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-----PEDRRRIGYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:COG4152 77 PEERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEP 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQlaenalVREKYLGRDFVLR 260
Cdd:COG4152 157 FSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDE------IRRQFGRNTLRLE 228
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
24-232 |
2.74e-47 |
|
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: 156.47 E-value: 2.74e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 24 RTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGY 101
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRK-VGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASV-FRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:cd03225 80 VFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 181 EPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGK 232
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-237 |
8.16e-47 |
|
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: 155.38 E-value: 8.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 24 RTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKlpvyqrARLGIGYLA 103
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK------ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 104 QEASVFRK--LSVEDnikaVLEMTPL--------TPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAID 173
Cdd:cd03235 75 QRRSIDRDfpISVRD----VVLMGLYghkglfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQD 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 174 PKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRaYLLFEGKVLFQG 237
Cdd:cd03235 151 PDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDR-VLLLNRTVVASG 213
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
25-242 |
2.81e-46 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 154.06 E-value: 2.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 25 TEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlgIGYLAQ 104
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR--IGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 105 EASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFA 184
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 185 GVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
22-256 |
6.79e-46 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 154.38 E-value: 6.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGY 101
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDN------------IKAVLEMTPLTPDQQRERLE---MLIEEFGLHKVRTNQGNRLSGGERRRVEI 166
Cdd:PRK11300 85 TFQHVRLFREMTVIENllvaqhqqlktgLFSGLLKTPAFRRAESEALDraaTWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 167 ARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLK-QRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRnEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
250
....*....|.
gi 490460070 246 ALVREKYLGRD 256
Cdd:PRK11300 245 PDVIKAYLGEA 255
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
23-242 |
9.08e-46 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 156.46 E-value: 9.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDI-TKLPVYQRarlGIGY 101
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRER---RVGF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEF---GLHKVRTNQgnrLSGGERRRVEIARCLAIDPKFIM 178
Cdd:COG1118 80 VFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVqleGLADRYPSQ---LSGGQRQRVALARALAVEPEVLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 179 LDEPFAGVDpiavqdiqsivAKLKQ----------RNIG---ILITdHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:COG1118 157 LDEPFGALD-----------AKVRKelrrwlrrlhDELGgttVFVT-HDQEEALELADRVVVMNQGRIEQVGTPDEV 221
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-237 |
9.31e-46 |
|
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: 151.43 E-value: 9.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 24 RTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGYLA 103
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-IAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 104 QeasvfrklsvednikavlemtpltpdqqrerlemLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:cd03214 80 Q----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPT 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 184 AGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03214 126 SHLDIAHQIELLELLRRLaRERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
22-228 |
4.80e-45 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 152.17 E-value: 4.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSR----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITklpvyqRARL 97
Cdd:COG1116 7 ALELRGVSKRFPTGgggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT------GPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFI 177
Cdd:COG1116 81 DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 178 MLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLL 228
Cdd:COG1116 161 LMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHDVDEAVFLADRVVVL 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-245 |
1.26e-44 |
|
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: 157.37 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 4 TIDTAEALSPDRHKGETGLLRTEHLVKRYRSR-----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGK 78
Cdd:COG1123 242 RLGAARGRAAPAAAAAEPLLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGS 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 79 IYLNEQDITKLPVYQRARLG--IGYLAQ--EASVFRKLSVEDNIKAVLE-MTPLTPDQQRERLEMLIEEFGLhkvRTNQG 153
Cdd:COG1123 322 ILFDGKDLTKLSRRSLRELRrrVQMVFQdpYSSLNPRMTVGDIIAEPLRlHGLLSRAERRERVAELLERVGL---PPDLA 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 154 NR----LSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPiAVQ-DIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYL 227
Cdd:COG1123 399 DRypheLSGGQRQRVAIARALALEPKLLILDEPTSALDV-SVQaQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAV 477
|
250
....*....|....*...
gi 490460070 228 LFEGKVLFQGTAEQLAEN 245
Cdd:COG1123 478 MYDGRIVEDGPTEEVFAN 495
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
23-232 |
3.10e-44 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 147.72 E-value: 3.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRA-RLGIGY 101
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIkavlemtpltpdqqrerlemlieEFGlhkvrtnqgnrLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:cd03229 81 VFQDFALFPHLTVLENI-----------------------ALG-----------LSGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGK 232
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
23-228 |
1.45e-43 |
|
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213260 [Multi-domain] Cd Length: 220 Bit Score: 147.23 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSR----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITklpvyqRARLG 98
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT------GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIM 178
Cdd:cd03293 75 RGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKL--KQRNIGILITdHNVNETLSITDRAYLL 228
Cdd:cd03293 155 LDEPFSALDALTREQLQEELLDIwrETGKTVLLVT-HDIDEAVFLADRVVVL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
23-256 |
2.33e-43 |
|
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: 147.45 E-value: 2.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYR-SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYqRARLGIGY 101
Cdd:cd03295 1 IEFENVTKRYGgGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV-ELRRKIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGL--HKVRTNQGNRLSGGERRRVEIARCLAIDPKFIML 179
Cdd:cd03295 80 VIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLKQRnIG--ILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL---AENALVREkYLG 254
Cdd:cd03295 160 DEPFGALDPITRDQLQEEFKRLQQE-LGktIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEIlrsPANDFVAE-FVG 237
|
..
gi 490460070 255 RD 256
Cdd:cd03295 238 AD 239
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
23-245 |
5.98e-43 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 146.33 E-value: 5.98e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYL 102
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER---NVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTP----DQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIM 178
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSErppeAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:cd03296 160 LDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
30-242 |
9.73e-43 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 147.54 E-value: 9.73e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 30 KRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIgyLAQEASVF 109
Cdd:TIGR01188 1 KVYGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGI--VPQYASVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 110 RKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPI 189
Cdd:TIGR01188 79 EDLTGRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490460070 190 AVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:TIGR01188 159 TRRAIWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEEL 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
24-232 |
1.49e-42 |
|
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: 142.38 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 24 RTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVyQRARLGIGYLA 103
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPL-EELRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 104 QeasvfrklsvednikavlemtpltpdqqrerlemlieefglhkvrtnqgnrLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:cd00267 80 Q---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPT 108
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490460070 184 AGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGK 232
Cdd:cd00267 109 SGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
23-237 |
1.94e-42 |
|
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: 143.96 E-value: 1.94e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQditklPVYQRARLGIGYL 102
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK-----PLDIAARNRIGYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03269 76 PEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03269 156 FSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
23-237 |
1.98e-42 |
|
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: 143.90 E-value: 1.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKL-PVYQRarlgIGY 101
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNiEALRR----IGA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNikavLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:cd03268 77 LIEAPGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03268 153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
26-237 |
7.45e-42 |
|
ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213231 [Multi-domain] Cd Length: 211 Bit Score: 142.33 E-value: 7.45e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSIELRQGeIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlgIGYLAQE 105
Cdd:cd03264 4 ENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR--IGYLPQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 106 ASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAG 185
Cdd:cd03264 81 FGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAG 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 186 VDPIAVQDIQSIVAKLKQRNIGILITdHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03264 161 LDPEERIRFRNLLSELGEDRIVILST-HIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
23-249 |
1.10e-41 |
|
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; Phosphonates are a class of organophosphorus compounds characterized by a chemically stable carbon-to-phosphorus (C-P) bond. Phosphonates are widespread among naturally occurring compounds in all kingdoms of wildlife, but only prokaryotic microorganisms are able to cleave this bond. Certain bacteria such as E. coli can use alkylphosphonates as a phosphorus source. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213223 [Multi-domain] Cd Length: 241 Bit Score: 143.09 E-value: 1.10e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRS-RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLP--VYQRARLGI 99
Cdd:cd03256 1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKgkALRQLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFRKLSVEDNI--KAVLEMTP------LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLA 171
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVlsGRLGRRSTwrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 172 IDPKFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVR 249
Cdd:cd03256 161 QQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVLDE 239
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
22-225 |
1.32e-41 |
|
ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 141.85 E-value: 1.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGigY 101
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLA--Y 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKAVLEMTPLTPDqqRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:COG4133 80 LGHADGLKPELTVRENLRFWAALYGLRAD--REAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQRNIGILITDH-----NVNETLSITDRA 225
Cdd:COG4133 158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHqplelAAARVLDLGDFK 206
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
23-245 |
2.72e-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: 141.61 E-value: 2.72e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYL 102
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR---PVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 183 FAGVDPIAVQDIQSIVAKLkQRNIGI--LITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:cd03300 158 LGALDLKLRKDMQLELKRL-QKELGItfVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEE 221
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
22-233 |
3.26e-41 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 141.33 E-value: 3.26e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRS----RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL 97
Cdd:COG1136 4 LLELRNLTKSYGTgegeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 ---GIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDP 174
Cdd:COG1136 84 rrrHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNvNETLSITDRAYLLFEGKV 233
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELnRELGTTIVMVTHD-PELAARADRVIRLRDGRI 222
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
23-233 |
3.71e-41 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 140.72 E-value: 3.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-RARlgIGY 101
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwRRQ--VAY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKlSVEDNIKAVLEMTPLTPDqqRERLEMLIEEFGL-HKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:COG4619 79 VPQEPALWGG-TVRDNLPFPFQLRERKFD--RERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLLLD 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490460070 181 EPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:COG4619 156 EPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
22-247 |
4.47e-41 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 141.73 E-value: 4.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRS-RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLP--VYQRARLG 98
Cdd:COG3638 2 MLELRNLSKRYPGgTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRgrALRRLRRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFRKLSVednIKAVL-----------EMTPLTPDQQRERLEMLIEEFGL-HK--VRTNQgnrLSGGERRRV 164
Cdd:COG3638 82 IGMIFQQFNLVPRLSV---LTNVLagrlgrtstwrSLLGLFPPEDRERALEALERVGLaDKayQRADQ---LSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLA 243
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELT 235
|
....
gi 490460070 244 ENAL 247
Cdd:COG3638 236 DAVL 239
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
23-255 |
7.01e-41 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 140.66 E-value: 7.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIElrQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYL 102
Cdd:COG3840 2 LRLDDLTYRYGDFPLRFDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAER---PVSML 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKavLEMTP---LTPDqQRERLEMLIEEFGLhkvrTNQGNR----LSGGERRRVEIARCLAIDPK 175
Cdd:COG3840 77 FQENNLFPHLTVAQNIG--LGLRPglkLTAE-QRAQVEQALERVGL----AGLLDRlpgqLSGGQRQRVALARCLVRKRP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL--AENALVREKY 252
Cdd:COG3840 150 ILLLDEPFSALDPALRQEMLDLVDELcRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALldGEPPPALAAY 229
|
...
gi 490460070 253 LGR 255
Cdd:COG3840 230 LGI 232
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
38-184 |
1.67e-40 |
|
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: 137.01 E-value: 1.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKlPVYQRARLGIGYLAQEASVFRKLSVEDN 117
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 118 IKAVLEMTPLTPDQQRERLEMLIEEFGL----HKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFA 184
Cdd:pfam00005 80 LRLGLLLKGLSKREKDARAEEALEKLGLgdlaDRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
22-245 |
3.55e-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: 3.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRS--RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNG---GKIYLNEQDITKLPVYQRAR 96
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALRGR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LgIGYLAQEA-SVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPK 175
Cdd:COG1123 84 R-IGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPD 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:COG1123 163 LLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAA 233
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
22-237 |
4.25e-40 |
|
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: 138.41 E-value: 4.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSR----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL 97
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 G--IGYLAQEA--SVFRKLSVEDNIKAVLEM-TPLTPDQQRERLEMLI-EEFGLHKVRTNQ-GNRLSGGERRRVEIARCL 170
Cdd:cd03257 81 RkeIQMVFQDPmsSLNPRMTIGEQIAEPLRIhGKLSKKEARKEAVLLLlVGVGLPEEVLNRyPHELSGGQRQRVAIARAL 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 171 AIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLK-QRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03257 161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQeELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| PQQ_ABC_ATP |
TIGR03864 |
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of ... |
23-243 |
9.28e-40 |
|
ABC transporter, ATP-binding subunit, PQQ-dependent alcohol dehydrogenase system; Members of this protein family are the ATP-binding subunit of an ABC transporter system that is associated with PQQ biosynthesis and PQQ-dependent alcohol dehydrogenases. While this family shows homology to several efflux ABC transporter subunits, the presence of a periplasmic substrate-binding protein and association with systems for catabolism of alcohols suggests a role in import rather than detoxification. [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 274822 [Multi-domain] Cd Length: 236 Bit Score: 137.81 E-value: 9.28e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYl 102
Cdd:TIGR03864 2 LEVAGLSFRYGARRALDDVSFTVRPGRFVALLGPNGAGKSTLFSLLTRLYVAQSGQISVAGHDLRRAPRAALARLGVVF- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 aQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:TIGR03864 81 -QQPTLDLDLSVRQNLRYHAALHGLSRAEARARIAELLARLGLAERADDKVRELNGGHRRRVEIARALLHRPALLLLDEP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQ-RNIGILITDHNVNEtLSITDRAYLLFEGKVLFQGTAEQLA 243
Cdd:TIGR03864 160 TVGLDPASRAAITAHVRALARdQGLSVLWATHLVDE-IEASDRLVVLHRGRVLADGAAAELR 220
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
38-255 |
3.38e-39 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 136.79 E-value: 3.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQEASVFRKLSVEDN 117
Cdd:COG4674 26 LNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGRKFQKPTVFEELTVFEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 118 I-------KAVLE--MTPLTPDqQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDP 188
Cdd:COG4674 106 LelalkgdRGVFAslFARLTAE-ERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGMLLAQDPKLLLLDEPVAGMTD 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 189 IAVQDIQSIVAKLKQRNiGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYLGR 255
Cdd:COG4674 185 AETERTAELLKSLAGKH-SVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPRVIEVYLGR 250
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
22-237 |
5.02e-39 |
|
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: 135.57 E-value: 5.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYR--SRTV--VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPvyQRARL 97
Cdd:cd03266 1 MITADALTKRFRdvKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP--AEARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFI 177
Cdd:cd03266 79 RLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 178 MLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03266 159 LLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
23-233 |
6.03e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 135.31 E-value: 6.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRS----RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL- 97
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 --GIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPK 175
Cdd:cd03255 81 rrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNvNETLSITDRAYLLFEGKV 233
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHD-PELAEYADRIIELRDGKI 218
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
23-242 |
2.47e-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: 133.85 E-value: 2.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLV-----VPNGGKIYLNEQDITKLPVYQRA-R 96
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDVLElR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LGIGYLAQEASVFRKlSVEDNIKAVLEMTPLTPDQQR-ERLEMLIEEFGLH---KVRTNqGNRLSGGERRRVEIARCLAI 172
Cdd:cd03260 81 RRVGMVFQKPNPFPG-SIYDNVAYGLRLHGIKLKEELdERVEEALRKAALWdevKDRLH-ALGLSGGQQQRLCLARALAN 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 173 DPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRnIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03260 159 EPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-252 |
9.66e-38 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 133.32 E-value: 9.66e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGY 101
Cdd:COG4559 1 MLEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARR-RAV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDnikaVLEM--TPLTPDQQRER--LEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLA------ 171
Cdd:COG4559 80 LPQHSSLAFPFTVEE----VVALgrAPHGSSAAQDRqiVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepv 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 172 -IDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVRE 250
Cdd:COG4559 156 dGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLER 235
|
..
gi 490460070 251 KY 252
Cdd:COG4559 236 VY 237
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
19-254 |
1.10e-37 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 132.70 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 19 ETGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLG 98
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFRKLSVEDNikavLEMTPLTPDQQR--ERLEMLIEEFG-LHKVRTNQGNRLSGGERRRVEIARCLAIDPK 175
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEEN----LAMGGFFAERDQfqERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYLG 254
Cdd:PRK11614 158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYLG 236
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
23-245 |
6.98e-37 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 136.82 E-value: 6.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIG 100
Cdd:COG4987 334 LELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR-IA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YLAQEASVFRKlSVEDNIK------------AVLEMTPLTP--DQQRERLEMLIEEfglhkvrtnQGNRLSGGERRRVEI 166
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRlarpdatdeelwAALERVGLGDwlAALPDGLDTWLGE---------GGRRLSGGERRRLAL 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 167 ARCLAIDPKFIMLDEPFAGVDPIAVQDI-QSIVAKLKQRNIgILITdHNVNEtLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:COG4987 483 ARALLRDAPILLLDEPTEGLDAATEQALlADLLEALAGRTV-LLIT-HRLAG-LERMDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
40-237 |
5.56e-36 |
|
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: 127.22 E-value: 5.56e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRArlgIGYLAQEASVFRKLSVEDNIK 119
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP---VSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 120 avLEMTP---LTPdQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQS 196
Cdd:cd03298 93 --LGLSPglkLTA-EDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490460070 197 IVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03298 170 LVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-244 |
7.72e-36 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 134.96 E-value: 7.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 2 TDTIDTAEALSPDRHKGEtglLRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKI 79
Cdd:COG2274 456 PEREEGRSKLSLPRLKGD---IELENVSFRYpgDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRI 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 80 YLNEQDITKLPVYQRARLgIGYLAQEASVFRKlSVEDNIkaVLEMTPLTPDQQRERLEML-IEEF------GLHKVRTNQ 152
Cdd:COG2274 533 LIDGIDLRQIDPASLRRQ-IGVVLQDVFLFSG-TIRENI--TLGDPDATDEEIIEAARLAgLHDFiealpmGYDTVVGEG 608
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 153 GNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVnETLSITDRAYLLFEGK 232
Cdd:COG2274 609 GSNLSGGQRQRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIA-HRL-STIRLADRIIVLDKGR 686
|
250
....*....|..
gi 490460070 233 VLFQGTAEQLAE 244
Cdd:COG2274 687 IVEDGTHEELLA 698
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
26-214 |
8.48e-36 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 127.09 E-value: 8.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYR-SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL--GIGYL 102
Cdd:COG2884 5 ENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrRIGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:COG2884 85 FQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEP 164
|
170 180 190
....*....|....*....|....*....|..
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILITDHN 214
Cdd:COG2884 165 TGNLDPETSWEIMELLEEINRRGTTVLIATHD 196
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
34-245 |
8.57e-36 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 128.73 E-value: 8.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLP---VYQrARLGIGYLAQEASVFR 110
Cdd:PRK11831 19 NRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSrsrLYT-VRKRMSMLFQSGALFT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 111 KLSVEDNIKAVL-EMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPI 189
Cdd:PRK11831 98 DMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPI 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 190 AVQDIQSIVAKLKQrNIGI--LITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK11831 178 TMGVLVKLISELNS-ALGVtcVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAN 234
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
23-242 |
2.12e-35 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 129.42 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYL 102
Cdd:COG3839 4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---NIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRER----LEML-IEEFGLHKVRTnqgnrLSGGERRRVEIARCLAIDPKFI 177
Cdd:COG3839 81 FQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRvreaAELLgLEDLLDRKPKQ-----LSGGQRQRVALGRALVREPKVF 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 178 MLDEPFAGVDpiavqdiqsivAKLK----------QRNIG---ILITdHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:COG3839 156 LLDEPLSNLD-----------AKLRvemraeikrlHRRLGtttIYVT-HDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
37-240 |
3.31e-35 |
|
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: 125.91 E-value: 3.31e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYLAQEASVFRKLSVED 116
Cdd:cd03299 14 KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR---DISYVPQNYALFPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 117 NI----KAVLEMTPLTPDQQRERLEML-IEEFGLHKVRTnqgnrLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAV 191
Cdd:cd03299 91 NIayglKKRKVDKKEIERKVLEIAEMLgIDHLLNRKPET-----LSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTK 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490460070 192 QDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAE 240
Cdd:cd03299 166 EKLREELKKIrKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
23-233 |
4.94e-35 |
|
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: 125.06 E-value: 4.94e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYL 102
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR---DIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:cd03301 158 LSNLDAKLRVQMRAELKRLQQRlGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
14-237 |
1.46e-34 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 124.37 E-value: 1.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 14 DRHKGETGLLRT-EHLVKR-YRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPV 91
Cdd:cd03267 11 RVYSKEPGLIGSlKSLFKRkYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 92 YQRARLGIgYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLA 171
Cdd:cd03267 91 KFLRRIGV-VFGQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 172 IDPKFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYnRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
23-232 |
1.61e-34 |
|
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: 122.11 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIG 100
Cdd:cd03228 1 IEFKNVSFSYpgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN-IA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YLAQEASVFrKLSVEDNIkavlemtpltpdqqrerlemlieefglhkvrtnqgnrLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:cd03228 80 YVPQDPFLF-SGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILD 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 181 EPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVnETLSITDRAYLLFEGK 232
Cdd:cd03228 122 EATSALDPETEALILEALRALAKGKTVIVIA-HRL-STIRDADRIIVLDDGR 171
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
48-237 |
3.90e-34 |
|
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213264 [Multi-domain] Cd Length: 214 Bit Score: 122.79 E-value: 3.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 48 GEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQ---DITK---LPVYQRarlGIGYLAQEASVFRKLSVEDNIKAV 121
Cdd:cd03297 23 EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfDSRKkinLPPQQR---KIGLVFQQYALFPHLNVRENLAFG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 122 LEMtpLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKL 201
Cdd:cd03297 100 LKR--KRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQI 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 490460070 202 KQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03297 178 KKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-246 |
4.63e-34 |
|
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: 123.37 E-value: 4.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRY----RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARl 97
Cdd:COG1124 1 MLEVRNLSVSYgqggRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIGYLAQ--EASVFRKLSVEDnikAVLEmtPLT----PDQQRERLEMLiEEFGLHK-VRTNQGNRLSGGERRRVEIARCL 170
Cdd:COG1124 80 RVQMVFQdpYASLHPRHTVDR---ILAE--PLRihglPDREERIAELL-EQVGLPPsFLDRYPHQLSGGQRQRVAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 171 AIDPKFIMLDEPFAGVDPIaVQD-IQSIVAKLK-QRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENA 246
Cdd:COG1124 154 ILEPELLLLDEPTSALDVS-VQAeILNLLKDLReERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGP 230
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-246 |
6.63e-34 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 122.38 E-value: 6.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIElrQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRArlgIGY 101
Cdd:PRK10771 1 MLKLTDITWLYHHLPMRFDLTVE--RGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP---VSM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKavLEMTP---LTpDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIM 178
Cdd:PRK10771 76 LFQENNLFSHLTVAQNIG--LGLNPglkLN-AAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG-TAEQLAENA 246
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGpTDELLSGKA 222
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
22-252 |
7.28e-34 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 122.96 E-value: 7.28e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGY 101
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR-RAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDnikaVLEM--TPLTPDQQRER--LEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLA------ 171
Cdd:PRK13548 81 LPQHSSLSFPFTVEE----VVAMgrAPHGLSRAEDDalVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 172 IDPKFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVRE 250
Cdd:PRK13548 157 GPPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRR 236
|
..
gi 490460070 251 KY 252
Cdd:PRK13548 237 VY 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-267 |
8.14e-34 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 124.15 E-value: 8.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 18 GETGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL 97
Cdd:PRK13537 3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIgyLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFI 177
Cdd:PRK13537 83 GV--VPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 178 MLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENAL---VREKYlG 254
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIgcdVIEIY-G 239
|
250
....*....|...
gi 490460070 255 RDFVLRRKSFADL 267
Cdd:PRK13537 240 PDPVALRDELAPL 252
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
22-257 |
1.10e-33 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 127.44 E-value: 1.10e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTfyMTV--GLVVPNGGKIYLNEQDITKLPVYQRARLGI 99
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTL--MKIlsGVYQPDSGEILLDGEPVRFRSPRDAQAAGI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFRKLSVEDNIkaVLEMTPLTP-----DQQRERLEMLIEEFGLH-----KVRTnqgnrLSGGERRRVEIARC 169
Cdd:COG1129 82 AIIHQELNLVPNLSVAENI--FLGREPRRGglidwRAMRRRARELLARLGLDidpdtPVGD-----LSVAQQQLVEIARA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 170 LAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVR 249
Cdd:COG1129 155 LSRDARVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELVR 234
|
....*...
gi 490460070 250 eKYLGRDF 257
Cdd:COG1129 235 -LMVGREL 241
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
23-240 |
1.82e-33 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 120.32 E-value: 1.82e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGlvVPN----GGKIYLNEQDITKLPVYQRARLG 98
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--HPKyevtEGEILFKGEDITDLPPEERARLG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFRKLSVEDNIKAVlemtpltpdqqrerlemlieefglhkvrtNQGnrLSGGERRRVEIARCLAIDPKFIM 178
Cdd:cd03217 79 IFLAFQYPPEIPGVKNADFLRYV-----------------------------NEG--FSGGEKKRNEILQLLLLEPDLAI 127
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNvNETLS--ITDRAYLLFEGKVLFQGTAE 240
Cdd:cd03217 128 LDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY-QRLLDyiKPDRVHVLYDGRIVKSGDKE 190
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-249 |
3.01e-33 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 124.56 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 1 MTDTIDTAEALSPdrhKGETGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIY 80
Cdd:PRK11607 1 MNDAIPRPQAKTR---KALTPLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIM 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 81 LNEQDITKLPVYQRArlgIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGE 160
Cdd:PRK11607 78 LDGVDLSHVPPYQRP---INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 161 RRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRnIGI--LITDHNVNETLSITDRAYLLFEGKVLFQGT 238
Cdd:PRK11607 155 RQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILER-VGVtcVMVTHDQEEAMTMAGRIAIMNRGKFVQIGE 233
|
250
....*....|.
gi 490460070 239 AEQLAENALVR 249
Cdd:PRK11607 234 PEEIYEHPTTR 244
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-233 |
4.80e-33 |
|
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: 118.30 E-value: 4.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYL 102
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQeasvfrklsvednikavlemtpltpdqqrerlemlieefglhkvrtnqgnrLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03216 81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
40-243 |
5.32e-33 |
|
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: 123.30 E-value: 5.32e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNE---QDITK---LPVYQRArlgIGYLAQEASVFRKLS 113
Cdd:TIGR02142 15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGrtlFDSRKgifLPPEKRR---IGYVFQEARLFPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIkaVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQD 193
Cdd:TIGR02142 92 VRGNL--RYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490460070 194 IQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLA 243
Cdd:TIGR02142 170 ILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
29-233 |
5.54e-33 |
|
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: 118.69 E-value: 5.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 29 VKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLA---QE 105
Cdd:cd03215 7 VRGLSVKGAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAGIAYVPedrKR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 106 ASVFRKLSVEDNIkaVLemtpltpdqqrerlemlieefglhkvrtnqGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAG 185
Cdd:cd03215 87 EGLVLDLSVAENI--AL------------------------------SSLLSGGNQQKVVLARWLARDPRVLILDEPTRG 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490460070 186 VDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:cd03215 135 VDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
42-237 |
7.83e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 119.20 E-value: 7.83e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 42 SIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRArlgIGYLAQEASVFRKLSVEDNI--- 118
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP---VSMLFQENNLFAHLTVRQNIglg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 119 -KAVLEMTPLtpdqQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSI 197
Cdd:TIGR01277 95 lHPGLKLNAE----QQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLAL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490460070 198 VAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:TIGR01277 171 VKQLcSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
35-244 |
6.74e-32 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 117.48 E-value: 6.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGL--VVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQEASVFRKL 112
Cdd:COG0396 13 KEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAGIFLAFQYPVEIPGV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 113 SVEDNIKAVLEM---TPLTPDQQRERLEMLIEEFGLHK------VrtNQGnrLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:COG0396 93 SVSNFLRTALNArrgEELSAREFLKLLKEKMKELGLDEdfldryV--NEG--FSGGEKKRNEILQMLLLEPKLAILDETD 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 184 AGVDPIAVQDIQSIVAKLKQRNIGILITDHNvNETLSIT--DRAYLLFEGKVLFQGTAEqLAE 244
Cdd:COG0396 169 SGLDIDALRIVAEGVNKLRSPDRGILIITHY-QRILDYIkpDFVHVLVDGRIVKSGGKE-LAL 229
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
26-245 |
8.67e-32 |
|
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: 118.13 E-value: 8.67e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPvyqRARL------GI 99
Cdd:cd03294 28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMS---RKELrelrrkKI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIML 179
Cdd:cd03294 105 SMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLM 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLkQRNIG---ILITdHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:cd03294 185 DEAFSALDPLIRREMQDELLRL-QAELQktiVFIT-HDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
40-242 |
8.90e-32 |
|
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: 119.82 E-value: 8.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNE---QDITK---LPVYQRArlgIGYLAQEASVFRKLS 113
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSARgifLPPHRRR---IGYVFQEARLFPHLS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIKAVLEMTPltPDQQRERLEMLIEEFGL-----HKVRTnqgnrLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDP 188
Cdd:COG4148 94 VRGNLLYGRKRAP--RAERRISFDEVVELLGIghlldRRPAT-----LSGGERQRVAIGRALLSSPRLLLMDEPLAALDL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 189 IAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:COG4148 167 ARKAEILPYLERLRDElDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEV 221
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-245 |
1.66e-31 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 118.65 E-value: 1.66e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 15 RHKGETGLLRT-EHLVKR-YRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDitklPVY 92
Cdd:COG4586 13 VYEKEPGLKGAlKGLFRReYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV----PFK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 93 QRARlgigYLAQEASVF-RK------LSVEDN---IKAVLEMtpltPDQQ-RERLEMLIEEFGLHKVRTNQGNRLSGGER 161
Cdd:COG4586 89 RRKE----FARRIGVVFgQRsqlwwdLPAIDSfrlLKAIYRI----PDAEyKKRLDELVELLDLGELLDTPVRQLSLGQR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 162 RRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAE 240
Cdd:COG4586 161 MRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLE 240
|
....*
gi 490460070 241 QLAEN 245
Cdd:COG4586 241 ELKER 245
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
22-242 |
3.07e-31 |
|
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: 115.76 E-value: 3.07e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSR----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQR--A 95
Cdd:cd03258 1 MIELKNVSKVFGDTggkvTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELrkA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 96 RLGIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPK 175
Cdd:cd03258 81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 176 FIMLDEPFAGVDPiavQDIQSIVAKLKQ----RNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03258 161 VLLCDEATSALDP---ETTQSILALLRDinreLGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
22-244 |
4.53e-31 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 120.13 E-value: 4.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTtfYMTV--GLVVPNGGKIYLNEQditklPVYQR----- 94
Cdd:COG3845 5 ALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKST--LMKIlyGLYQPDSGEILIDGK-----PVRIRsprda 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 95 ARLGIGYLAQEASVFRKLSVEDNIkaVLEMTP-----LTPDQQRERLEMLIEEFGLH-----KVRTnqgnrLSGGERRRV 164
Cdd:COG3845 78 IALGIGMVHQHFMLVPNLTVAENI--VLGLEPtkggrLDRKAARARIRELSERYGLDvdpdaKVED-----LSVGEQQRV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG-----TA 239
Cdd:COG3845 151 EILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVdtaetSE 230
|
....*
gi 490460070 240 EQLAE 244
Cdd:COG3845 231 EELAE 235
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
19-249 |
1.53e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 115.33 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 19 ETGLLRTEHLVKRYRSRT-VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDI---TKLPVYQR 94
Cdd:PRK13636 2 EDYILKVEELNYNYSDGThALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 95 ARLGIGYLAQEASVFRKLSVEDNIKAVLEMTpLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDP 174
Cdd:PRK13636 82 ESVGMVFQDPDNQLFSASVYQDVSFGAVNLK-LPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGT-AEQLAENALVR 249
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMqKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNpKEVFAEKEMLR 237
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
23-245 |
1.99e-30 |
|
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: 119.09 E-value: 1.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRY-RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGY 101
Cdd:COG4988 337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ-IAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFrKLSVEDNI------------KAVLEMTPLTP--DQQRERLEMLIEEfglhkvrtnQGNRLSGGERRRVEIA 167
Cdd:COG4988 416 VPQNPYLF-AGTIRENLrlgrpdasdeelEAALEAAGLDEfvAALPDGLDTPLGE---------GGRGLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 168 RCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVnETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILIT-HRL-ALLAQADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
35-242 |
4.43e-30 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 113.70 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL--GIGYLAQ--EASVFr 110
Cdd:TIGR04521 18 KKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLrkKVGLVFQfpEHQLF- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 111 KLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKvrtNQGNR----LSGGERRRVEIARCLAIDPKFIMLDEPFAGV 186
Cdd:TIGR04521 97 EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDE---EYLERspfeLSGGQMRRVAIAGVLAMEPEVLILDEPTAGL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 187 DPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:TIGR04521 174 DPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREV 230
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
27-242 |
6.11e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 114.82 E-value: 6.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 27 HLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYLAQEA 106
Cdd:PRK11432 11 NITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQR---DICMVFQSY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 107 SVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGV 186
Cdd:PRK11432 88 ALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 187 DPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK11432 168 DANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
22-242 |
1.63e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.09 E-value: 1.63e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVV-NDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDIT---KLPVYQRARL 97
Cdd:PRK13639 1 ILETRDLKYSYPDGTEAlKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydkKSLLEVRKTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIGYLAQEASVFRKLSVEDNIKAVLEMTpLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFI 177
Cdd:PRK13639 81 GIVFQNPDDQLFAPTVEEDVAFGPLNLG-LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 178 MLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEV 224
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
41-247 |
1.80e-29 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 111.47 E-value: 1.80e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 41 VSIELRQGEIVGLLGPNGAGKTTTFYMTVGLvVPNGGKIYLNEQDITKLPVYQRARLGiGYLAQEAS------VFRKLSv 114
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGL-LPGQGEILLNGRPLSDWSAAELARHR-AYLSQQQSppfampVFQYLA- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 ednikavLEMTPLTPDQQRER-LEMLIEEFGLHKVRTNQGNRLSGGERRRVEIAR-CLAIDP------KFIMLDEPFAGV 186
Cdd:COG4138 92 -------LHQPAGASSEAVEQlLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAvLLQVWPtinpegQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 187 DpIAVQ---DiqSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQ-LAENAL 247
Cdd:COG4138 165 D-VAQQaalD--RLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEvMTPENL 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
29-242 |
2.69e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 113.25 E-value: 2.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 29 VKRYRSRT-VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRArlgIGYLAQEAS 107
Cdd:PRK10851 8 IKKSFGRTqVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK---VGFVFQHYA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 108 VFRKLSVEDNIKAVLEMTPltpdqQRERLEM---------LIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIM 178
Cdd:PRK10851 85 LFRHMTVFDNIAFGLTVLP-----RRERPNAaaikakvtqLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKLKQ--RNIGILITdHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK10851 160 LDEPFGALDAQVRKELRRWLRQLHEelKFTSVFVT-HDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
23-219 |
8.24e-29 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 109.95 E-value: 8.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRY----RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITklpvyqrarlG 98
Cdd:COG4525 4 LTVRHVSVRYpgggQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT----------G 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGylAQEASVFRK------LSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAI 172
Cdd:COG4525 74 PG--ADRGVVFQKdallpwLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490460070 173 DPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETL 219
Cdd:COG4525 152 DPRFLLMDEPFGALDALTREQMQELLLDVWQRtGKGVFLITHSVEEAL 199
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
26-233 |
1.02e-28 |
|
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: 108.39 E-value: 1.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITK-LPVYQRARLGIGYLAQ 104
Cdd:cd03262 4 KNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdKKNINELRQKVGMVFQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 105 EASVFRKLSVEDNIK-AVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:cd03262 84 QFNLFPHLTVLENITlAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPT 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490460070 184 AGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:cd03262 164 SALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
9-233 |
1.38e-28 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 113.19 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 9 EALSPDRHK--GETgLLRTEHLvkryRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDI 86
Cdd:COG1129 242 EDLFPKRAAapGEV-VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPV 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 87 TKLPVYQRARLGIGYLA---QEASVFRKLSVEDNI-----KAVLEMTPLTPDQQRERLEMLIEEFGlhkVRTNQGNR--- 155
Cdd:COG1129 317 RIRSPRDAIRAGIAYVPedrKGEGLVLDLSIRENItlaslDRLSRGGLLDRRRERALAEEYIKRLR---IKTPSPEQpvg 393
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 156 -LSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:COG1129 394 nLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRI 472
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-249 |
1.94e-28 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 109.33 E-value: 1.94e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYR--SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-RARLG 98
Cdd:PRK13635 5 IIRVEHISFRYPdaATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDvRRQVG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IgylaqeasVFRK-------LSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLA 171
Cdd:PRK13635 85 M--------VFQNpdnqfvgATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 172 IDPKFIMLDEPFAGVDPIAVQDIQSIVAKLK-QRNIGILITDHNVNETLSiTDRAYLLFEGKVLFQGTAEQLAE--NALV 248
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKeQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKsgHMLQ 235
|
.
gi 490460070 249 R 249
Cdd:PRK13635 236 E 236
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
35-264 |
2.20e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 109.37 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ---RARLGIGYLAQEASVFrk 111
Cdd:PRK13637 20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdiRKKVGLVFQYPEYQLF-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 112 lsvEDNIKAVLEMTP----LTPDQQRERLEMLIEEFGL--HKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAG 185
Cdd:PRK13637 98 ---EETIEKDIAFGPinlgLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 186 VDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREK---------YLGR 255
Cdd:PRK13637 175 LDPKGRDEILNKIKELhKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVETLESiglavpqvtYLVR 254
|
....*....
gi 490460070 256 DfvLRRKSF 264
Cdd:PRK13637 255 K--LRKKGF 261
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-214 |
3.27e-28 |
|
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages
Pssm-ID: 213259 [Multi-domain] Cd Length: 214 Bit Score: 107.11 E-value: 3.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTV-VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLP----VYQRARLGIG 100
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRgraiPYLRRKIGVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YlaQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGL-HKVRTnQGNRLSGGERRRVEIARCLAIDPKFIML 179
Cdd:cd03292 84 F--QDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLsHKHRA-LPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHN 214
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
22-238 |
4.30e-28 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 110.42 E-value: 4.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRArlgIGY 101
Cdd:PRK09452 14 LVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRH---VNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRER-LEML----IEEFGLHKVRtnqgnRLSGGERRRVEIARCLAIDPKF 176
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRvMEALrmvqLEEFAQRKPH-----QLSGGQQQRVAIARAVVNKPKV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 177 IMLDEPFAGVDPIAVQDIQSIVAKLkQRNIGI---LITdHNVNETLSITDRAYLLFEGKVLFQGT 238
Cdd:PRK09452 166 LLLDESLSALDYKLRKQMQNELKAL-QRKLGItfvFVT-HDQEEALTMSDRIVVMRDGRIEQDGT 228
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-241 |
6.79e-28 |
|
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: 111.76 E-value: 6.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 20 TGLLRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPvyqRARL 97
Cdd:COG4618 328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWD---REEL 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 G--IGYLAQEASVFRKlSVEDNIkAvlEMTPLTPDQ-----QRERLEMLIEEF--GLHKVRTNQGNRLSGGERRRVEIAR 168
Cdd:COG4618 405 GrhIGYLPQDVELFDG-TIAENI-A--RFGDADPEKvvaaaKLAGVHEMILRLpdGYDTRIGEGGARLSGGQRQRIGLAR 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 169 CLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNeTLSITDRAYLLFEGKVLFQGTAEQ 241
Cdd:COG4618 481 ALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDE 552
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
22-245 |
7.19e-28 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 107.00 E-value: 7.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPV-YQRARLGIG 100
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKdINKLRRKVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YLAQEASVFRKLSVEDNI----KAVLEMTPltpDQQRERLEMLIEEFGLhkvrTNQGN----RLSGGERRRVEIARCLAI 172
Cdd:COG1126 81 MVFQQFNLFPHLTVLENVtlapIKVKKMSK---AEAEERAMELLERVGL----ADKADaypaQLSGGQQQRVAIARALAM 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 173 DPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFEN 226
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
22-247 |
8.24e-28 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440213 [Multi-domain] Cd Length: 320 Bit Score: 108.60 E-value: 8.24e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSR----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNG---GKIYLNEQDITKLPVYQR 94
Cdd:COG0444 1 LLEVRNLKVYFPTRrgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGitsGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 95 ARL---GIGYLAQEAS-----VFRklsVEDNIKAVLEM-TPLTPDQQRERLEMLIEEFGLHKVRtNQGNR----LSGGER 161
Cdd:COG0444 81 RKIrgrEIQMIFQDPMtslnpVMT---VGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPE-RRLDRypheLSGGMR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 162 RRVEIARCLAIDPKFIMLDEPFAGVDPIavqdIQ-SIVAKLK--QRNIG---ILITdHNVNETLSITDRAYLLFEGKVLF 235
Cdd:COG0444 157 QRVMIARALALEPKLLIADEPTTALDVT----IQaQILNLLKdlQRELGlaiLFIT-HDLGVVAEIADRVAVMYAGRIVE 231
|
250
....*....|..
gi 490460070 236 QGTAEQLAENAL 247
Cdd:COG0444 232 EGPVEELFENPR 243
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
23-252 |
8.67e-28 |
|
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: 106.96 E-value: 8.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVG----LVVpnGGKIYLNEQDITKLPVYQRARLG 98
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpsyEVT--SGTILFKGQDLLELEPDERARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IgYLAQEAS-----VFRKLSVEDNIKAVLEMTPLTP----------DQQRERLEMlIEEFGLHKVrtNQGnrLSGGERRR 163
Cdd:TIGR01978 79 L-FLAFQYPeeipgVSNLEFLRSALNARRSARGEEPldlldfekllKEKLALLDM-DEEFLNRSV--NEG--FSGGEKKR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 164 VEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSIT-DRAYLLFEGKVLFQGTAEqL 242
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKpDYVHVLLDGRIVKSGDVE-L 231
|
250
....*....|
gi 490460070 243 AENaLVREKY 252
Cdd:TIGR01978 232 AKE-LEAKGY 240
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
41-247 |
8.75e-28 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 106.94 E-value: 8.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 41 VSIELRQGEIVGLLGPNGAGKTTTFYMTVGLvVPNGGKIYLNEQDITKLPVYQRARLGiGYLAQEAS------VFRKLSv 114
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR-AYLSQQQTppfampVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 ednikavLEMTPLTP-DQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIAR-CLAIDP------KFIMLDEPFAGV 186
Cdd:PRK03695 92 -------LHQPDKTRtEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAvVLQVWPdinpagQLLLLDEPMNSL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 187 DpIAVQDI-QSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQ-LAENAL 247
Cdd:PRK03695 165 D-VAQQAAlDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEvLTPENL 226
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
26-251 |
9.00e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 107.38 E-value: 9.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYR--SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQrARLGIGYLA 103
Cdd:PRK13632 11 ENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE-IRKKIGIIF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 104 QEA-SVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PRK13632 90 QNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDES 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILIT-DHNVNETLsITDRAYLLFEGKVLFQGTAEQLAENALVREK 251
Cdd:PRK13632 170 TSMLDPKGKREIKKIMVDLRKTRKKTLISiTHDMDEAI-LADKVIVFSEGKLIAQGKPKEILNNKEILEK 238
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
29-237 |
1.13e-27 |
|
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: 106.20 E-value: 1.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 29 VKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVvPNG----GKIYLNEQDITKLPVYQRarlgIGYLAQ 104
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV-EGGgttsGQILFNGQPRKPDQFQKC----VAYVRQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 105 EASVFRKLSVEDNIK--AVLEMTPLTPDQQRERLE--MLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:cd03234 89 DDILLPGLTVRETLTytAILRLPRKSSDAIRKKRVedVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 181 EPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHN-VNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03234 169 EPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
23-216 |
1.15e-27 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 105.64 E-value: 1.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPN---GGKIYLNEQDITKLPVYQRarlGI 99
Cdd:COG4136 2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR---RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFRKLSVEDNIkaVLEMTPLTPDQQR-ERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIM 178
Cdd:COG4136 79 GILFQDDLLFPHLSVGENL--AFALPPTIGRAQRrARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALL 156
|
170 180 190
....*....|....*....|....*....|....*....
gi 490460070 179 LDEPFAGVDPIAVQDIQSIV-AKLKQRNIGILITDHNVN 216
Cdd:COG4136 157 LDEPFSKLDAALRAQFREFVfEQIRQRGIPALLVTHDEE 195
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
20-256 |
1.16e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 111.03 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 20 TGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGI 99
Cdd:PRK09700 3 TPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQLGI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFRKLSVEDNI-------KAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAI 172
Cdd:PRK09700 83 GIIYQELSVIDELTVLENLyigrhltKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLML 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 173 DPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVReKY 252
Cdd:PRK09700 163 DAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVR-LM 241
|
....
gi 490460070 253 LGRD 256
Cdd:PRK09700 242 VGRE 245
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
36-253 |
1.78e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 107.48 E-value: 1.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 36 TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKI---YLNEQDITKLPVYQ------------------- 93
Cdd:PRK13651 21 KALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEkvleklviqktrfkkikki 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 94 ---RARLGIGYLAQEASVFRKLSVEDNIKAVLEMTpLTPDQQRERLEMLIEEFGLHKVRTNQGN-RLSGGERRRVEIARC 169
Cdd:PRK13651 101 keiRRRVGVVFQFAEYQLFEQTIEKDIIFGPVSMG-VSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQKRRVALAGI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 170 LAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG-TAEQLAENALV 248
Cdd:PRK13651 180 LAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGdTYDILSDNKFL 259
|
....*
gi 490460070 249 REKYL 253
Cdd:PRK13651 260 IENNM 264
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
40-233 |
2.80e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 109.76 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTT---TFYmtvGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLA---QEASVFRKLS 113
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTElaeTLY---GLRPARGGRIMLNGKEINALSTAQRLARGLVYLPedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIKAVLEMTP---LTPDQQRERLEMLIEEFGLHKVRTNQGNR-LSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPI 189
Cdd:PRK15439 358 LAWNVCALTHNRRgfwIKPARENAVLERYRRALNIKFNHAEQAARtLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490460070 190 AVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK15439 438 ARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
22-244 |
4.80e-27 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 109.12 E-value: 4.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRS--RTV---VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIY--LNEQ--DITKLPVY 92
Cdd:TIGR03269 279 IIKVRNVSKRYISvdRGVvkaVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvrVGDEwvDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 93 QRARLG--IGYLAQEASVFRKLSVEDNI---------------KAV--LEMTPLTPDQQRERLEMLIEEfglhkvrtnqg 153
Cdd:TIGR03269 359 GRGRAKryIGILHQEYDLYPHRTVLDNLteaiglelpdelarmKAVitLKMVGFDEEKAEEILDKYPDE----------- 427
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 154 nrLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDI-QSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGK 232
Cdd:TIGR03269 428 --LSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVtHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGK 505
|
250
....*....|..
gi 490460070 233 VLFQGTAEQLAE 244
Cdd:TIGR03269 506 IVKIGDPEEIVE 517
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-238 |
5.11e-27 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 110.10 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYR--SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDI-TKLPVyqrARLGIGYL 102
Cdd:TIGR01257 932 KNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA---VRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIgILITDHNVNETLSITDRAYLLFEGKVLFQGT 238
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLLKYRSGRT-IIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
22-234 |
6.47e-27 |
|
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: 105.27 E-value: 6.47e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRS---------RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVY 92
Cdd:TIGR02769 2 LLEVRDVTHTYRTgglfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 93 QRARL--GIGYLAQEA--SVFRKLSVEDNIKAVLE-MTPLTPDQQRERLEMLIEEFGLH-KVRTNQGNRLSGGERRRVEI 166
Cdd:TIGR02769 82 QRRAFrrDVQLVFQDSpsAVNPRMTVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINI 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 167 ARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVL 234
Cdd:TIGR02769 162 ARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAfGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
30-244 |
1.42e-26 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 105.68 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 30 KRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIylneqDITKLPVYQRARL---GIGYLAQEA 106
Cdd:PRK13536 49 KSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKI-----TVLGVPVPARARLaraRIGVVPQFD 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 107 SVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGV 186
Cdd:PRK13536 124 NLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 187 DPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAE 244
Cdd:PRK13536 204 DPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALID 261
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
22-214 |
1.48e-26 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 103.20 E-value: 1.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSR----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL 97
Cdd:TIGR02211 1 LLKCENLGKRYQEGkldtRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 ---GIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDP 174
Cdd:TIGR02211 81 rnkKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKLKQ-RNIGILITDHN 214
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNReLNTSFLVVTHD 201
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
26-245 |
1.99e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 103.29 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDI-TKLPVYQRARL------G 98
Cdd:PRK11264 7 KNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdTARSLSQQKGLirqlrqH 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFRKLSVEDNI---KAVLEMTPltPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPK 175
Cdd:PRK11264 87 VGFVFQNFNLFPHRTVLENIiegPVIVKGEP--KEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK11264 165 VILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
22-247 |
2.10e-26 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 104.81 E-value: 2.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRY---------RSRTV--VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLP 90
Cdd:COG4608 7 LLEVRDLKKHFpvrgglfgrTVGVVkaVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 91 VYQRARL--GIGYLAQE--ASVFRKLSVEDNIKAVLEM-TPLTPDQQRERLEMLIEEFGLhkvRTNQGNR----LSGGER 161
Cdd:COG4608 87 GRELRPLrrRMQMVFQDpyASLNPRMTVGDIIAEPLRIhGLASKAERRERVAELLELVGL---RPEHADRypheFSGGQR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 162 RRVEIARCLAIDPKFIMLDEPFAGVDpIAVQ--------DIQsivaklKQRNIGILITDHNvnetLS----ITDRA---Y 226
Cdd:COG4608 164 QRIGIARALALNPKLIVCDEPVSALD-VSIQaqvlnlleDLQ------DELGLTYLFISHD----LSvvrhISDRVavmY 232
|
250 260
....*....|....*....|.
gi 490460070 227 LlfeGKVLFQGTAEQLAENAL 247
Cdd:COG4608 233 L---GKIVEIAPRDELYARPL 250
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-244 |
2.13e-26 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 107.83 E-value: 2.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 24 RTEHLVKRYRSR-TVVNDVSIELRQGEIVGLLGPNGAGKTT-----TFYMTVGLVVpnGGKIYLNEQDITKlpvyQRARL 97
Cdd:TIGR00955 26 RLRGCFCRERPRkHLLKNVSGVAKPGELLAVMGSSGAGKTTlmnalAFRSPKGVKG--SGSVLLNGMPIDA----KEMRA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIGYLAQEASVFRKLSVED--NIKAVLEM-TPLTPDQQRERLEMLIEEFGLHK---VRTNQGNR---LSGGERRRVEIAR 168
Cdd:TIGR00955 100 ISAYVQQDDLFIPTLTVREhlMFQAHLRMpRRVTKKEKRERVDEVLQALGLRKcanTRIGVPGRvkgLSGGERKRLAFAS 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 169 CLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETL-SITDRAYLLFEGKVLFQGTAEQLAE 244
Cdd:TIGR00955 180 ELLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELfELFDKIILMAEGRVAYLGSPDQAVP 256
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
26-242 |
2.58e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 104.77 E-value: 2.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSR----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ--RARLGI 99
Cdd:COG1135 5 ENLSKTFPTKggpvTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERElrAARRKI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLhkvrTNQGNR----LSGGERRRVEIARCLAIDPK 175
Cdd:COG1135 85 GMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGL----SDKADAypsqLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 176 FIMLDEPFAGVDPiavQDIQSIVAKLKQ--RNIGI---LITdHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:COG1135 161 VLLCDEATSALDP---ETTRSILDLLKDinRELGLtivLIT-HEMDVVRRICDRVAVLENGRIVEQGPVLDV 228
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-211 |
2.77e-26 |
|
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: 106.99 E-value: 2.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRT-VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRaRLGIGY 101
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW-RDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKlSVEDNIK-AVLEMTPLTPDQQRER--LEMLIEEF--GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKF 176
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRlARPDASDAEIREALERagLDEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190
....*....|....*....|....*....|....*
gi 490460070 177 IMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILIT 211
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVT 514
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
35-242 |
3.18e-26 |
|
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: 102.30 E-value: 3.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQrARLGIGYLAQEASVFRKlSV 114
Cdd:cd03254 16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKS-LRSMIGVVLQDTFLFSG-TI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 EDNIKavleMTPLTPDQQRE-------RLEMLIE--EFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAG 185
Cdd:cd03254 94 MENIR----LGRPNATDEEVieaakeaGAHDFIMklPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSN 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 186 VDPIAVQDIQSIVAKLKQRNIGILITDHnvnetLSIT---DRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03254 170 IDTETEKLIQEALEKLMKGRTSIIIAHR-----LSTIknaDKILVLDDGKIIEEGTHDEL 224
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-242 |
5.15e-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: 102.08 E-value: 5.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTT-----TFYM--TVGLVVPNGGKIYLNEqDITKLpvyqR 94
Cdd:COG1119 3 LLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTllsliTGDLppTYGNDVRLFGERRGGE-DVWEL----R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 95 ARLGIGYLAQEASVFRKLSVEDNIK----AVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCL 170
Cdd:COG1119 78 KRIGLVSPALQLRFPRDETVLDVVLsgffDSIGLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARAL 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 171 AIDPKFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:COG1119 158 VKDPELLILDEPTAGLDLGARELLLALLDKLaAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEV 230
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
38-231 |
7.45e-26 |
|
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: 101.39 E-value: 7.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKlPVYQRArlgigYLAQEASVFRKLSVEDN 117
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITE-PGPDRM-----VVFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 118 IK-AVLEMTP-LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQ 195
Cdd:TIGR01184 75 IAlAVDRVLPdLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180 190
....*....|....*....|....*....|....*..
gi 490460070 196 SIVAKLKQRN-IGILITDHNVNETLSITDRAYLLFEG 231
Cdd:TIGR01184 155 EELMQIWEEHrVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
6-245 |
8.09e-26 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 106.02 E-value: 8.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 6 DTAEALSPDRHKGEtglLRTEHLVKRYR-SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQ 84
Cdd:COG1132 326 DPPGAVPLPPVRGE---IEFENVSFSYPgDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGV 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 85 DITKLPVYQ-RARlgIGYLAQEASVFrKLSVEDNIKAVLemtpltPDQQRERLEM---------LIEEF--GLHKVRTNQ 152
Cdd:COG1132 403 DIRDLTLESlRRQ--IGVVPQDTFLF-SGTIRENIRYGR------PDATDEEVEEaakaaqaheFIEALpdGYDTVVGER 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 153 GNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNeTLSITDRAYLLFEGK 232
Cdd:COG1132 474 GVNLSGGQRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLMKGRTTIVIA-HRLS-TIRNADRILVLDDGR 551
|
250
....*....|...
gi 490460070 233 VLFQGTAEQLAEN 245
Cdd:COG1132 552 IVEQGTHEELLAR 564
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
26-253 |
1.80e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 101.35 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRT-VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-RARLGIGYLA 103
Cdd:PRK13647 8 EDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGLVFQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 104 QEASVFRKLSVEDNIKAVLEMTpLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:PRK13647 88 PDDQVFSSTVWDDVAFGPVNMG-LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPM 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 184 AGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYL 253
Cdd:PRK13647 167 AYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQAGL 236
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
34-238 |
3.64e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 100.93 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQE------AS 107
Cdd:PRK13633 22 EKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWDIRNKAGMVFQNpdnqivAT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 108 VfrklsVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:PRK13633 102 I-----VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 188 PIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSiTDRAYLLFEGKVLFQGT 238
Cdd:PRK13633 177 PSGRREVVNTIKELnKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
23-233 |
4.84e-25 |
|
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: 97.67 E-value: 4.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKlpvYQRARLG-- 98
Cdd:cd03246 1 LEVENVSFRYpgAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQ---WDPNELGdh 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFrKLSVEDNIkavlemtpltpdqqrerlemlieefglhkvrtnqgnrLSGGERRRVEIARCLAIDPKFIM 178
Cdd:cd03246 78 VGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILV 119
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVnETLSITDRAYLLFEGKV 233
Cdd:cd03246 120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRP-ETLASADRILVLEDGRV 173
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-247 |
7.48e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 102.80 E-value: 7.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 1 MTDTIDTAEA---------------LSPDRHKGETG--LLRTEHL-VKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKT 62
Cdd:COG3845 219 VVGTVDTAETseeelaelmvgrevlLRVEKAPAEPGevVLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 63 TTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQE----ASVfRKLSVEDNikAVLEMTPLTPDQQ------ 132
Cdd:COG3845 299 ELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGVAYIPEDrlgrGLV-PDMSVAEN--LILGRYRRPPFSRggfldr 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 133 ---RERLEMLIEEFGlhkVRTNQGN----RLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRN 205
Cdd:COG3845 376 kaiRAFAEELIEEFD---VRTPGPDtparSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAG 452
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 490460070 206 IGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENAL 247
Cdd:COG3845 453 AAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATREEI 494
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-244 |
1.23e-24 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 102.90 E-value: 1.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYL-----NEQDItklpvyqRARLGIG 100
Cdd:NF033858 270 RGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvDAGDI-------ATRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YLAQEASVFRKLSVEDNikavLEMTP----LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIArcLAI--DP 174
Cdd:NF033858 343 YMSQAFSLYGELTVRQN----LELHArlfhLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLA--VAVihKP 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSiTDRAYLLFEGKVLFQGTAEQLAE 244
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLLIELsREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVA 486
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
22-242 |
1.36e-24 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 98.93 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVpnGGKIYLNEQDITKLPVYQRARLG--- 98
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLIT--GDKSAGSHIELLGRTVQREGRLArdi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 ------IGYLAQEASVFRKLSVEDNIK-AVLEMTPL--------TPDQQRERLEML----IEEFGLHKVRTnqgnrLSGG 159
Cdd:PRK09984 82 rksranTGYIFQQFNLVNRLSVLENVLiGALGSTPFwrtcfswfTREQKQRALQALtrvgMVHFAHQRVST-----LSGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 160 ERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRN-IGILITDHNVNETLSITDRAYLLFEGKVLFQGT 238
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
|
....
gi 490460070 239 AEQL 242
Cdd:PRK09984 237 SQQF 240
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
23-240 |
2.44e-24 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 97.78 E-value: 2.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYL--NEQDITKLPVYQRARL--- 97
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIagHQFDFSQKPSEKAIRLlrq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIGYLAQEASVFRKLSVEDN-IKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKF 176
Cdd:COG4161 83 KVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQV 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 177 IMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAE 240
Cdd:COG4161 163 LLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDAS 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
24-233 |
2.48e-24 |
|
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: 96.56 E-value: 2.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 24 RTEHLVKRY-RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITklpvyQRARLG-IGY 101
Cdd:cd03226 1 RIENISFSYkKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-----AKERRKsIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEasVFRKL---SVEDNIKAVLEMTPLTPDQQRErlemLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIM 178
Cdd:cd03226 76 VMQD--VDYQLftdSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:cd03226 150 FDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-248 |
2.54e-24 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 101.28 E-value: 2.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGY 101
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIkavLEMTPLTPDQQReRLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:PRK15439 91 VPQEPLLFPNLSVKENI---LFGLPKRQASMQ-KMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDE 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALV 248
Cdd:PRK15439 167 PTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
32-242 |
2.55e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 98.63 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 32 YRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTtFYMTVGLV------------VPNGGKIYLNEQDITKLpvyqraRLGI 99
Cdd:PRK14271 31 FAGKTVLDQVSMGFPARAVTSLMGPTGSGKTT-FLRTLNRMndkvsgyrysgdVLLGGRSIFNYRDVLEF------RRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFrKLSVEDNIKAVLEMTPLTPDQQ-RERLEMLIEEFGLHKVRTNQGN----RLSGGERRRVEIARCLAIDP 174
Cdd:PRK14271 104 GMLFQRPNPF-PMSIMDNVLAGVRAHKLVPRKEfRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKLKQRnIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
22-254 |
2.65e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRT-VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIG 100
Cdd:PRK13644 1 MIRLENVSYSYPDGTpALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKLVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YLAQEASV-FRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIML 179
Cdd:PRK13644 81 IVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIF 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNEtLSITDRAYLLFEGKVLFQGTAEQLAENalVREKYLG 254
Cdd:PRK13644 161 DEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSD--VSLQTLG 232
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
22-219 |
3.34e-24 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 97.46 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKlPVYQRarlgiGY 101
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER-----GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRER-LEML----IEEFGLHKVRtnqgnRLSGGERRRVEIARCLAIDPKF 176
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIaHQMLkkvgLEGAEKRYIW-----QLSGGQRQRVGIARALAANPQL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490460070 177 IMLDEPFAGVDPIAVQDIQSIVAKLKQRNIG--ILITdHNVNETL 219
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKqvLLIT-HDIEEAV 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
38-242 |
4.48e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 97.88 E-value: 4.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGYLAQEA-SVFRKLSVED 116
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-IGMVFQNPdNQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 117 NIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQS 196
Cdd:PRK13650 102 DVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490460070 197 IVAKLKQRN--IGILITdHNVNEtLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK13650 182 TIKGIRDDYqmTVISIT-HDLDE-VALSDRVLVMKNGQVESTSTPREL 227
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-252 |
6.05e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.69 E-value: 6.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 24 RTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRAR-LGIgyL 102
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKrLAI--L 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDnikavLEM---TP-----LTPdQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDP 174
Cdd:COG4604 81 RQENHINSRLTVRE-----LVAfgrFPyskgrLTA-EDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDT 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKY 252
Cdd:COG4604 155 DYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIY 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-245 |
7.09e-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: 100.14 E-value: 7.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYR------SRTV-----VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVvPNGGKIYLNEQDITKLP 90
Cdd:COG4172 275 LLEARDLKVWFPikrglfRRTVghvkaVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLS 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 91 VYQ----RARLGIgylaqeasVFR--------KLSVEDNIK---AVLEmTPLTPDQQRERLEMLIEEFGLHKvrtNQGNR 155
Cdd:COG4172 354 RRAlrplRRRMQV--------VFQdpfgslspRMTVGQIIAeglRVHG-PGLSAAERRARVAEALEEVGLDP---AARHR 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 156 ----LSGGERRRVEIARCLAIDPKFIMLDEPFAGVDpIAVQdiQSIVAKLK--QRNIG---ILITdHNVNETLSITDRAY 226
Cdd:COG4172 422 ypheFSGGQRQRIAIARALILEPKLLVLDEPTSALD-VSVQ--AQILDLLRdlQREHGlayLFIS-HDLAVVRALAHRVM 497
|
250
....*....|....*....
gi 490460070 227 LLFEGKVLFQGTAEQLAEN 245
Cdd:COG4172 498 VMKDGKVVEQGPTEQVFDA 516
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
22-242 |
7.96e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 97.18 E-value: 7.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYR-SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-RARLGI 99
Cdd:PRK13652 3 LIETRDLCYSYSgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvRKFVGL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFRKlSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIML 179
Cdd:PRK13652 83 VFQNPDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK13652 162 DEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
23-213 |
2.02e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 98.97 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRY-RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGY 101
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRKlSVEDNIK-AVLEMTP--LTPDQQRERLEMLIEEF--GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKF 176
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRlARPDATDeeLWAALERVGLADWLRALpdGLDTVLGEGGARLSGGERQRLALARALLADAPI 492
|
170 180 190
....*....|....*....|....*....|....*..
gi 490460070 177 IMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDH 213
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHH 529
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
38-245 |
2.16e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 97.80 E-value: 2.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLP---VYQRARLGIGYLAQEASVFRKLSV 114
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISdaeLREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 EDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDI 194
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 195 QSIVAKLKQRNI-GILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK10070 204 QDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
35-255 |
2.83e-23 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 95.11 E-value: 2.83e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLV------VPNGGKIYLNEQDITKLPVYqRARLGIGYLAQEASV 108
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAI-KLRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 FRKLSVEDNIKAVLEMTPLTPDQQRERL-EMLIEEFGL----HKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIvEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 184 AGVDPIAVQDIQSIVAKLKqRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL---AENALVREKYLGR 255
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELK-NEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIftsPKNELTEKYVIGR 255
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
22-182 |
3.07e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 98.21 E-value: 3.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEqditklpvyqraRLGIGY 101
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE------------TVKIGY 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFR-KLSVEDNIKavlemtPLTPDQQRERLEMLIEEFGLH------KVRTnqgnrLSGGERRRVEIARCLAIDP 174
Cdd:COG0488 383 FDQHQEELDpDKTVLDELR------DGAPGGTEQEVRGYLGRFLFSgddafkPVGV-----LSGGEKARLALAKLLLSPP 451
|
....*...
gi 490460070 175 KFIMLDEP 182
Cdd:COG0488 452 NVLLLDEP 459
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-250 |
5.23e-23 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 94.31 E-value: 5.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlGIGYL 102
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR-RLALL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQE--------------------ASVFRKLSVEDNIKAvlemtpltpDQQRERLEmlIEEFGLHKVrtnqgNRLSGGERR 162
Cdd:PRK11231 82 PQHhltpegitvrelvaygrspwLSLWGRLSAEDNARV---------NQAMEQTR--INHLADRRL-----TDLSGGQRQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 163 RVEIARCLAIDPKFIMLDEPFAGVDpIAVQ-DIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQ 241
Cdd:PRK11231 146 RAFLAMVLAQDTPVVLLDEPTTYLD-INHQvELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEE 224
|
....*....
gi 490460070 242 LAENALVRE 250
Cdd:PRK11231 225 VMTPGLLRT 233
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
34-237 |
6.74e-23 |
|
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: 91.99 E-value: 6.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlgIGYLAQEASVFRKls 113
Cdd:cd03247 14 EQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSL--ISVLNQRPYLFDT-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 vednikavlemtpltpdqqrerlemlieefglhKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQD 193
Cdd:cd03247 90 ---------------------------------TLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQ 136
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490460070 194 IQSIVAK-LKQRNIgILITDHNVNetLSITDRAYLLFEGKVLFQG 237
Cdd:cd03247 137 LLSLIFEvLKDKTL-IWITHHLTG--IEHMDKILFLENGKIIMQG 178
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-233 |
8.43e-23 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 93.98 E-value: 8.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYR---------SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVY 92
Cdd:PRK10419 3 LLNVSGLSHHYAhgglsgkhqHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 93 QRA--RLGIGYLAQEA--SVFRKLSVEDNIKAVL-EMTPLTPDQQRERLEMLIEEFGL---HKVRTNQgnRLSGGERRRV 164
Cdd:PRK10419 83 QRKafRRDIQMVFQDSisAVNPRKTVREIIREPLrHLLSLDKAERLARASEMLRAVDLddsVLDKRPP--QLSGGQLQRV 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK10419 161 CLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQfGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
17-217 |
1.14e-22 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 92.85 E-value: 1.14e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 17 KGETGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVyQRAR 96
Cdd:PRK10247 2 QENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKP-EIYR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LGIGYLAQEASVFRKlSVEDNIKAVLEMTPLTPDQQRERLEMliEEFGLHKVRTNQG-NRLSGGERRRVEIARCLAIDPK 175
Cdd:PRK10247 81 QQVSYCAQTPTLFGD-TVYDNLIFPWQIRNQQPDPAIFLDDL--ERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPK 157
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNE 217
Cdd:PRK10247 158 VLLLDEITSALDESNKHNVNEIIHRYvREQNIAVLWVTHDKDE 200
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
26-252 |
1.36e-22 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 92.93 E-value: 1.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYR--SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDI-TKLPVYQRARlgIGYL 102
Cdd:cd03252 4 EHVRFRYKpdGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLaLADPAWLRRQ--VGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKlSVEDNIKAVLEMTPLTPDQQRERL---EMLIEEF--GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFI 177
Cdd:cd03252 82 LQENVLFNR-SIRDNIALADPGMSMERVIEAAKLagaHDFISELpeGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRIL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 178 MLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNeTLSITDRAYLLFEGKVLFQGTAEQL-AENALVREKY 252
Cdd:cd03252 161 IFDEATSALDYESEHAIMRNMHDICAGRTVIIIA-HRLS-TVKNADRIIVMEKGRIVEQGSHDELlAENGLYAYLY 234
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
31-227 |
1.41e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.53 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 31 RYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKiylneqditklpVYQRARLGIGYLAQEASVFR 110
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT------------VRRAGGARVAYVPQRSEVPD 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 111 KL--SVEDnikaVLEM---------TPLTPDQqRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIML 179
Cdd:NF040873 69 SLplTVRD----LVAMgrwarrglwRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYL 227
Cdd:NF040873 144 DEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
34-237 |
1.48e-22 |
|
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: 91.84 E-value: 1.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNG--GKIYLNEQDITKLPVYQRarlgIGYLAQEASVFRK 111
Cdd:cd03213 21 GKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPLDKRSFRKI----IGYVPQDDILHPT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 112 LSVEDNIKAVLEMtpltpdqqrerlemlieefglhkvrtnQGnrLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAV 191
Cdd:cd03213 97 LTVRETLMFAAKL---------------------------RG--LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490460070 192 QDIQSIVAKLKQRNIGILITDHNV-NETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03213 148 LQVMSLLRRLADTGRTIICSIHQPsSEIFELFDKLLLLSQGRVIYFG 194
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
34-250 |
1.57e-22 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 92.68 E-value: 1.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVyQRARLGIGYLAQEASVFRKlS 113
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTL-DSLRRAIGVVPQDTVLFND-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIK-----AvlemtplTPDQQRE-----RLEMLIEEF--GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:cd03253 91 IGYNIRygrpdA-------TDEEVIEaakaaQIHDKIMRFpdGYDTIVGERGLKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNeTLSITDRAYLLFEGKVLFQGT-AEQLAENALVRE 250
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSKGRTTIVIA-HRLS-TIVNADKIIVLKDGRIVERGThEELLAKGGLYAE 231
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
23-245 |
1.75e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 93.18 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTtfymtvgLV---------VPNG---GKIYLNEQDI--TK 88
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKST-------LLrclnrmndlIPGArveGEILLDGEDIydPD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 89 LPVYQ-RARlgIGYLAQEASVFRKlSVEDNIKAVLEMTPLTPdqqRERLEMLIEEfGLHKV--------RTNQ-GNRLSG 158
Cdd:COG1117 85 VDVVElRRR--VGMVFQKPNPFPK-SIYDNVAYGLRLHGIKS---KSELDEIVEE-SLRKAalwdevkdRLKKsALGLSG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 159 GERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQrNIGILITDHNVNETLSITDRAYLLFEGKVLFQGT 238
Cdd:COG1117 158 GQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK-DYTIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
....*..
gi 490460070 239 AEQLAEN 245
Cdd:COG1117 237 TEQIFTN 243
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-245 |
2.04e-22 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.11 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 19 ETGLLRTEhLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDIT-------KLPV 91
Cdd:PRK10619 3 ENKLNVID-LHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgQLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 92 YQ-------RARLGIGYlaQEASVFRKLSVEDNI-KAVLEMTPLTPDQQRERLEMLIEEFGL-HKVRTNQGNRLSGGERR 162
Cdd:PRK10619 82 ADknqlrllRTRLTMVF--QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIdERAQGKYPVHLSGGQQQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 163 RVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK10619 160 RVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
...
gi 490460070 243 AEN 245
Cdd:PRK10619 240 FGN 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-248 |
7.67e-22 |
|
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: 94.12 E-value: 7.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGlVVPNG---GKIYLNEQDITKLPVYQRARLG 98
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHGtwdGEIYWSGSPLKASNIRDTERAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFRKLSVEDNIKAVLEMT----PLTPDQQRERLEMLIEEFGLHKVR-TNQGNRLSGGERRRVEIARCLAID 173
Cdd:TIGR02633 80 IVIIHQELTLVPELSVAENIFLGNEITlpggRMAYNAMYLRAKNLLRELQLDADNvTRPVGDYGGGQQQLVEIAKALNKQ 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 174 PKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALV 248
Cdd:TIGR02633 160 ARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMSEDDII 234
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
30-241 |
1.23e-21 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 93.79 E-value: 1.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 30 KRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNG--GKIYLNEQDITKlPVYQRarlgIGYLAQEAS 107
Cdd:PLN03211 76 RQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK-QILKR----TGFVTQDDI 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 108 VFRKLSVEDNIK--AVLEM-TPLTPDQQRERLEMLIEEFGLHKV-RTNQGNR----LSGGERRRVEIARCLAIDPKFIML 179
Cdd:PLN03211 151 LYPHLTVRETLVfcSLLRLpKSLTKQEKILVAESVISELGLTKCeNTIIGNSfirgISGGERKRVSIAHEMLINPSLLIL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHN-VNETLSITDRAYLLFEGKVLFQGTAEQ 241
Cdd:PLN03211 231 DEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQpSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
35-213 |
1.45e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 89.47 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQ-DITKLPVYQRarlGIGYLAQEASVFRKLS 113
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIAR---GLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNikavleMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQD 193
Cdd:cd03231 90 VLEN------LRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180
....*....|....*....|
gi 490460070 194 IQSIVAKLKQRNIGILITDH 213
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTH 183
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
22-187 |
1.67e-21 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 89.80 E-value: 1.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSR----TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL 97
Cdd:COG4181 8 IIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 ---GIGYlaqeasVFRK------LSVEDNIkavleMTPL----TPDQQRERLEMLiEEFGLHKVRTNQGNRLSGGERRRV 164
Cdd:COG4181 88 rarHVGF------VFQSfqllptLTALENV-----MLPLelagRRDARARARALL-ERVGLGHRLDHYPAQLSGGEQQRV 155
|
170 180
....*....|....*....|...
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVD 187
Cdd:COG4181 156 ALARAFATEPAILFADEPTGNLD 178
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
23-240 |
1.98e-21 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 89.69 E-value: 1.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGK--IYLNEQDITKLPVYQRARL--- 97
Cdd:PRK11124 3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTlnIAGNHFDFSKTPSDKAIRElrr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIGYLAQEASVFRKLSVEDN-IKAVLEMTPLTPDQ---------QRERLEMLIEEFGLHkvrtnqgnrLSGGERRRVEIA 167
Cdd:PRK11124 83 NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQalaraekllERLRLKPYADRFPLH---------LSGGQQQRVAIA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 168 RCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAE 240
Cdd:PRK11124 154 RALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDAS 226
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
38-242 |
2.28e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 90.61 E-value: 2.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDIT-----KLPVYQRARLGIGYLAQEASVFrkl 112
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThktkdKYIRPVRKRIGMVFQFPESQLF--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 113 svEDNIKAVLEMTP----LTPDQQRERLEMLIEEFGLHK-VRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:PRK13646 100 --EDTVEREIIFGPknfkMNLDEVKNYAHRLLMDLGFSRdVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 188 PIAVQDIQSIVAKLK-QRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK13646 178 PQSKRQVMRLLKSLQtDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
25-182 |
2.63e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 25 TEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNeQDITklpvyqrarlgIGYLAQ 104
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP-KGLR-----------IGYLPQ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 105 EASVFRKLSVEDNI-------------KAVLEMTPLTPDQQRERLEMLIEEF-----------------GLHkVRTNQGN 154
Cdd:COG0488 69 EPPLDDDLTVLDTVldgdaelraleaeLEELEAKLAEPDEDLERLAELQEEFealggweaearaeeilsGLG-FPEEDLD 147
|
170 180 190
....*....|....*....|....*....|..
gi 490460070 155 R----LSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:COG0488 148 RpvseLSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
35-214 |
2.63e-21 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 88.78 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITklpvYQRARLGIGYLAQEASVFRKLSV 114
Cdd:PRK13539 15 RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID----DPDVAEACHYLGHRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 EDNI---KAVLEMTPLTPDQQrerlemlIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAV 191
Cdd:PRK13539 91 AENLefwAAFLGGEELDIAAA-------LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAV 163
|
170 180
....*....|....*....|....
gi 490460070 192 QDIQSIV-AKLKQRNIgILITDHN 214
Cdd:PRK13539 164 ALFAELIrAHLAQGGI-VIAATHI 186
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
22-216 |
3.89e-21 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 89.10 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYR----SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL 97
Cdd:PRK11629 5 LLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 ---GIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRER-LEMLiEEFGLHKVRTNQGNRLSGGERRRVEIARCLAID 173
Cdd:PRK11629 85 rnqKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRaLEML-AAVGLEHRANHRPSELSGGERQRVAIARALVNN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490460070 174 PKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRN-IGILITDHNVN 216
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQgTAFLVVTHDLQ 207
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
38-246 |
4.08e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 89.43 E-value: 4.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKlPVYQRARLGIGYLAQEA-SVFRKLSVED 116
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD-DNFEKLRKHIGIVFQNPdNQFVGSIVKY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 117 NIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQS 196
Cdd:PRK13648 104 DVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 490460070 197 IVAKLKQ-RNIGILITDHNVNETLSiTDRAYLLFEGKVLFQGTAEQLAENA 246
Cdd:PRK13648 184 LVRKVKSeHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDHA 233
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
22-237 |
6.72e-21 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 89.30 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQditKLPVYQRARLGIgy 101
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGK---PLDYSKRGLLAL-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFRK-------LSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDP 174
Cdd:PRK13638 76 RQQVATVFQDpeqqifyTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
40-242 |
8.71e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 88.92 E-value: 8.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDIT------KLPVYqRARLGIGYLAQEASVFRKlS 113
Cdd:PRK13634 25 DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkknkKLKPL-RKKVGIVFQFPEHQLFEE-T 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIkAVLEMTPLTPDQQRERL--EMlIEEFGL-HKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIA 190
Cdd:PRK13634 103 VEKDI-CFGPMNFGVSEEDAKQKarEM-IELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490460070 191 VQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK13634 181 RKEMMEMFYKLhKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
34-258 |
9.89e-21 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 90.29 E-value: 9.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGYLAQEASvfrkLS 113
Cdd:PRK09536 15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRR-VASVPQDTS----LS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIKAVLEM--TPLTP------DQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAG 185
Cdd:PRK09536 90 FEFDVRQVVEMgrTPHRSrfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTAS 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 186 VD-PIAVQDIQSiVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYLGRDFV 258
Cdd:PRK09536 170 LDiNHQVRTLEL-VRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDARTAV 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-247 |
1.00e-20 |
|
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: 91.04 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHL-----VKRYRSRtvVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGlVVPNG--GKIYLNEQDITKLPVYQR 94
Cdd:TIGR02633 257 ILEARNLtcwdvINPHRKR--VDDVSFSLRRGEILGVAGLVGAGRTELVQALFG-AYPGKfeGNVFINGKPVDIRNPAQA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 95 ARLGIGYLAQEAS---VFRKLSVEDNIK-AVLE-MTPLTPDQQRERLEMLIEEFGLHKVRTNQGN----RLSGGERRRVE 165
Cdd:TIGR02633 334 IRAGIAMVPEDRKrhgIVPILGVGKNITlSVLKsFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQKAV 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 166 IARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVlfQG-------T 238
Cdd:TIGR02633 414 LAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL--KGdfvnhalT 491
|
....*....
gi 490460070 239 AEQLAENAL 247
Cdd:TIGR02633 492 QEQVLAAAL 500
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
35-245 |
1.63e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 88.32 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVP---NGGKIYLNEQDITKLPVYQ-RARLGIGYLAQEaSVFR 110
Cdd:PRK13640 20 KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDiREKVGIVFQNPD-NQFV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 111 KLSVEDNIKAVLEmtpltpDQQRERLEML------IEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFA 184
Cdd:PRK13640 99 GATVGDDVAFGLE------NRAVPRPEMIkivrdvLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 185 GVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETlSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLkKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIFSK 233
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-249 |
1.82e-20 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 90.37 E-value: 1.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGlVVPNG---GKIYLNEQDITKLPVYQRARLG 98
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHGtyeGEIIFEGEELQASNIRDTERAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFRKLSVEDNIKAVLEMTP---LTPDQQRERLEMLIEEFGLH-KVRTNQGNrLSGGERRRVEIARCLAIDP 174
Cdd:PRK13549 84 IAIIHQELALVKELSVLENIFLGNEITPggiMDYDAMYLRAQKLLAQLKLDiNPATPVGN-LGLGQQQLVEIAKALNKQA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVR 249
Cdd:PRK13549 163 RLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAGMTEDDIIT 237
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
35-266 |
1.95e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 87.45 E-value: 1.95e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGYLAQE--ASVFRKL 112
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAKY-IGRVFQDpmMGTAPSM 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 113 SVEDNikavLEM----------TPLTPDQQRERLEMLIEEFGL---HKVRTNQGNrLSGGERRRVEIARCLAIDPKFIML 179
Cdd:COG1101 98 TIEEN----LALayrrgkrrglRRGLTKKRRELFRELLATLGLgleNRLDTKVGL-LSGGQRQALSLLMATLTKPKLLLL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEnaLVREKYLGRDFV 258
Cdd:COG1101 173 DEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEEKKK--LTVEDLLELFEE 250
|
....*...
gi 490460070 259 LRRKSFAD 266
Cdd:COG1101 251 IRGEELAD 258
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
26-238 |
2.55e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.70 E-value: 2.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRY----RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ--RARLGI 99
Cdd:PRK11153 5 KNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrKARRQI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEasvFRKLS---VEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLhkvrTNQGNR----LSGGERRRVEIARCLAI 172
Cdd:PRK11153 85 GMIFQH---FNLLSsrtVFDNVALPLELAGTPKAEIKARVTELLELVGL----SDKADRypaqLSGGQKQRVAIARALAS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 173 DPKFIMLDEPFAGVDPiavQDIQSIVAKLKQ--RNIGI---LITdHNVNETLSITDRAYLLFEGKVLFQGT 238
Cdd:PRK11153 158 NPKVLLCDEATSALDP---ATTRSILELLKDinRELGLtivLIT-HEMDVVKRICDRVAVIDAGRLVEQGT 224
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-263 |
2.79e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 87.40 E-value: 2.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTtFYMTVGLV------VPNGGKIYLNEQDItklpvYQRaR 96
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKST-FLKCLNRMneleseVRVEGRVEFFNQNI-----YER-R 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LGIGYLAQEAS-VFRK-----LSVEDNIKAVLEMTPLTPDQQRERL-EMLIEEFGL-----HKVRTNQGNrLSGGERRRV 164
Cdd:PRK14258 81 VNLNRLRRQVSmVHPKpnlfpMSVYDNVAYGVKIVGWRPKLEIDDIvESALKDADLwdeikHKIHKSALD-LSGGQQQRL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRN-IGILITDHNVNETLSITDRAyLLFEGKvlfQGTAEQLA 243
Cdd:PRK14258 160 CIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSeLTMVIVSHNLHQVSRLSDFT-AFFKGN---ENRIGQLV 235
|
250 260
....*....|....*....|....*.
gi 490460070 244 ENALVREKYLG------RDFVLRRKS 263
Cdd:PRK14258 236 EFGLTKKIFNSphdsrtREYVLSRLG 261
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
22-242 |
4.57e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.07 E-value: 4.57e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVND---VSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlG 98
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQlngVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRR-K 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEA-SVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFI 177
Cdd:PRK13642 83 IGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 178 MLDEPFAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSiTDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK13642 163 ILDESTSMLDPTGRQEIMRVIHEIKEKyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSEL 227
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
5-242 |
4.73e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 89.01 E-value: 4.73e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 5 IDTA-EALSPDRHKGE-TGLLRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIY 80
Cdd:TIGR02203 311 LDSPpEKDTGTRAIERaRGDVEFRNVTFRYpgRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQIL 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 81 LNEQDITKLPVyQRARLGIGYLAQEASVFRKlSVEDNIkAVLEMTPLTPDQQRERLEML-IEEF------GLHKVRTNQG 153
Cdd:TIGR02203 391 LDGHDLADYTL-ASLRRQVALVSQDVVLFND-TIANNI-AYGRTEQADRAEIERALAAAyAQDFvdklplGLDTPIGENG 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 154 NRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNeTLSITDRAYLLFEGKV 233
Cdd:TIGR02203 468 VLLSGGQRQRLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGRTTLVIA-HRLS-TIEKADRIVVMDDGRI 545
|
....*....
gi 490460070 234 LFQGTAEQL 242
Cdd:TIGR02203 546 VERGTHNEL 554
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
37-187 |
5.64e-20 |
|
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: 85.33 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVyQRARLGIGYLAQEASVFrKLSVED 116
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDP-ADLRRNIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 117 NI---------KAVLE------MTPLTPDQQRErLEMLIEEfglhkvrtnQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:cd03245 97 NItlgapladdERILRaaelagVTDFVNKHPNG-LDLQIGE---------RGRGLSGGQRQAVALARALLNDPPILLLDE 166
|
....*.
gi 490460070 182 PFAGVD 187
Cdd:cd03245 167 PTSAMD 172
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
11-233 |
7.11e-20 |
|
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: 85.22 E-value: 7.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 11 LSPDRHKGetgLLRTEHLVKRYRSRT---VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDIt 87
Cdd:cd03248 3 LAPDHLKG---IVKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 88 klPVYQRARL--GIGYLAQEASVFRKlSVEDNIKAVLEMTPL---TPDQQRERLEMLIEEF--GLHKVRTNQGNRLSGGE 160
Cdd:cd03248 79 --SQYEHKYLhsKVSLVGQEPVLFAR-SLQDNIAYGLQSCSFecvKEAAQKAHAHSFISELasGYDTEVGEKGSQLSGGQ 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 161 RRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNeTLSITDRAYLLFEGKV 233
Cdd:cd03248 156 KQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIA-HRLS-TVERADQILVLDGGRI 226
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-253 |
7.99e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.66 E-value: 7.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTT---TFYMTV---------GLVVPNGGKIYLNEQDitklP 90
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTllrTFNRLLelneearveGEVRLFGRNIYSPDVD----P 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 91 VYQRARLGIGYlaQEASVFRKLSVEDNIKAVLEMTPLTPDQQR--ERLEMLIEEFGLHKVRTNQGN----RLSGGERRRV 164
Cdd:PRK14267 81 IEVRREVGMVF--QYPNPFPHLTIYDNVAIGVKLNGLVKSKKEldERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNETLSITDRAYLLFEGKVLFQGTAEQLAE 244
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVT-HSPAQAARVSDYVAFLYLGKLIEVGPTRKVFE 237
|
250
....*....|.
gi 490460070 245 NAL--VREKYL 253
Cdd:PRK14267 238 NPEheLTEKYV 248
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
38-245 |
8.32e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 86.60 E-value: 8.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKI----YLNEQDITKLPVYQRARLGIGYLAQ--EASVFrk 111
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTivgdYAIPANLKKIKEVKRLRKEIGLVFQfpEYQLF-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 112 lsvEDNIKAVLEMTPLTPDQQRERLEMLIEEF-GLHKVRTNQGNR----LSGGERRRVEIARCLAIDPKFIMLDEPFAGV 186
Cdd:PRK13645 105 ---QETIEKDIAFGPVNLGENKQEAYKKVPELlKLVQLPEDYVKRspfeLSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 187 DPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK13645 182 DPKGEEDFINLFERLnKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
40-254 |
1.18e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.95 E-value: 1.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-----RARLGIGYLAQEASVFRKLSV 114
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqiRKKVGLVFQFPESQLFEETVL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 EDnikavLEMTPLTPDQQRERLEMLIEE-FGLHKVRTNQGNR----LSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPI 189
Cdd:PRK13649 105 KD-----VAFGPQNFGVSQEEAEALAREkLALVGISESLFEKnpfeLSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 190 AVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL-AENALVREKYLG 254
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIfQDVDFLEEKQLG 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
20-245 |
1.20e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 88.24 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 20 TGLLRTEHLVKR---------YRSRT---VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDIT 87
Cdd:TIGR00958 467 TGTLAPLNLEGLiefqdvsfsYPNRPdvpVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV 546
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 88 KLP-VYQRARLGIgyLAQEASVFRKlSVEDNIKAVLEMTP---LTPDQQRERLEMLIEEF--GLHKVRTNQGNRLSGGER 161
Cdd:TIGR00958 547 QYDhHYLHRQVAL--VGQEPVLFSG-SVRENIAYGLTDTPdeeIMAAAKAANAHDFIMEFpnGYDTEVGEKGSQLSGGQK 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 162 RRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIvAKLKQRNIgILITDHnvnetLSITDRA---YLLFEGKVLFQGT 238
Cdd:TIGR00958 624 QRIAIARALVRKPRVLILDEATSALDAECEQLLQES-RSRASRTV-LLIAHR-----LSTVERAdqiLVLKKGSVVEMGT 696
|
....*..
gi 490460070 239 AEQLAEN 245
Cdd:TIGR00958 697 HKQLMED 703
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
22-233 |
1.33e-19 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 84.54 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRS-RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKL-----PVYQRA 95
Cdd:PRK10908 1 MIRFEHVSKAYLGgRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLknrevPFLRRQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 96 rlgIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPK 175
Cdd:PRK10908 81 ---IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK10908 158 VLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
22-245 |
1.65e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 84.83 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTF------------YMTVGLVVPNGGKIYLNEQDITKL 89
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLrsinrmndlnpeVTITGSIVYNGHNIYSPRTDTVDL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 90 pvyqraRLGIGYLAQEASVFrKLSVEDNIKAVLEMTPLtpdQQRERLEMLIEEF------------GLHkvrtNQGNRLS 157
Cdd:PRK14239 85 ------RKEIGMVFQQPNPF-PMSIYENVVYGLRLKGI---KDKQVLDEAVEKSlkgasiwdevkdRLH----DSALGLS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 158 GGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:PRK14239 151 GGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVT-RSMQQASRISDRTGFFLDGDLIEYN 229
|
....*...
gi 490460070 238 TAEQLAEN 245
Cdd:PRK14239 230 DTKQMFMN 237
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
30-245 |
2.06e-19 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 84.37 E-value: 2.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 30 KRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRA-RLGIGYLAQEASV 108
Cdd:PRK09493 9 KHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLiRQEAGMVFQQFYL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 FRKLSVEDNIK-AVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:PRK09493 89 FPHLTALENVMfGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 188 PIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK09493 169 PELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKN 226
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
20-223 |
2.09e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 84.78 E-value: 2.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 20 TGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQditklpvyqrarLGI 99
Cdd:PRK09544 2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK------------LRI 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEA--------SVFRKLSVEDNIKAvlemTPLTPDQQRERLEMLIeEFGLHKvrtnqgnrLSGGERRRVEIARCLA 171
Cdd:PRK09544 70 GYVPQKLyldttlplTVNRFLRLRPGTKK----EDILPALKRVQAGHLI-DAPMQK--------LSGGETQRVLLARALL 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 490460070 172 IDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQR-NIGILITDHNVNETLSITD 223
Cdd:PRK09544 137 NRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDLHLVMAKTD 189
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
33-233 |
2.95e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 86.76 E-value: 2.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 33 RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQ---EASVF 109
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAVKKGMAYITEsrrDNGFF 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 110 RKLSVEDNIkAVLEMTPL-----------------TPDQQRERLEMlieefGLHKVRTNQgNRLSGGERRRVEIARCLAI 172
Cdd:PRK09700 354 PNFSIAQNM-AISRSLKDggykgamglfhevdeqrTAENQRELLAL-----KCHSVNQNI-TELSGGNQQKVLISKWLCC 426
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 173 DPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK09700 427 CPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-252 |
3.47e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGYL 102
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR-IGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLSVEDNI-KAVLEMTPLTPDQQRERLEML---IEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIM 178
Cdd:PRK10253 87 AQNATTPGDITVQELVaRGRYPHQPLFTRWRKEDEEAVtkaMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 179 LDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKY 252
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
40-241 |
4.60e-19 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 85.31 E-value: 4.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQ---DITK---LPVYQRarlGIGYLAQEASVFRKLS 113
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKR---RIGYVFQDARLFPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIKavLEMTPLTPDQqrerLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQD 193
Cdd:PRK11144 93 VRGNLR--YGMAKSMVAQ----FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRE 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490460070 194 IQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQ 241
Cdd:PRK11144 167 LLPYLERLAREiNIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEE 215
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
37-253 |
5.43e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 83.42 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLV--VPNG---GKIYLNEQDITKLPVYQ-RARLGIGYlaQEASVFR 110
Cdd:PRK14247 18 VLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIelYPEArvsGEVYLDGQDIFKMDVIElRRRVQMVF--QIPNPIP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 111 KLSVEDNIKAVLEMTPLTPDQQ--RERLEMLIEEFGLHKVRTNQGN----RLSGGERRRVEIARCLAIDPKFIMLDEPFA 184
Cdd:PRK14247 96 NLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARALAFQPEVLLADEPTA 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 185 GVDPIAVQDIQSIVAKLKQRNIGILITdHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENAL--VREKYL 253
Cdd:PRK14247 176 NLDPENTAKIESLFLELKKDMTIVLVT-HFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRheLTEKYV 245
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
23-233 |
7.10e-19 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 83.19 E-value: 7.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIY-----LNE-QDITKLpVYQRAR 96
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtapLAEaREDTRL-MFQDAR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LgigyLAQEasvfrklSVEDNIKAVLEmtpltpDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKF 176
Cdd:PRK11247 92 L----LPWK-------KVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 177 IMLDEPFAGVDPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK11247 155 LLLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
40-266 |
7.86e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 83.63 E-value: 7.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKL-------PVyqRARLGIGYLAQEASVFRKL 112
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTskqkeikPV--RKKVGVVFQFPESQLFEET 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 113 SVEDnikavLEMTPLTPDQQRERLEML----IEEFGLHKVRTNQGN-RLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:PRK13643 102 VLKD-----VAFGPQNFGIPKEKAEKIaaekLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 188 PIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGT-AEQLAENALVREKYLGrdfVLRRKSFAD 266
Cdd:PRK13643 177 PKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTpSDVFQEVDFLKAHELG---VPKATHFAD 253
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
18-223 |
8.24e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 83.29 E-value: 8.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 18 GETGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTF--YMTVGLVVPNG---GKIYLNEQDITKL--- 89
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILrcFNRLNDLIPGFrveGKVTFHGKNLYAPdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 90 PVYQRARlgIGYLAQEASVFRKlSVEDNIKAVLEMTPLTPDQQrERLEMLIEEFGL-----HKVRTNqGNRLSGGERRRV 164
Cdd:PRK14243 86 PVEVRRR--IGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMD-ELVERSLRQAALwdevkDKLKQS-GLSLSGGQQQRL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIgILITDHNVNETLSITD 223
Cdd:PRK14243 161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYT-IIIVTHNMQQAARVSD 218
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
35-213 |
8.85e-19 |
|
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: 81.64 E-value: 8.85e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKL-PVYQRarlGIGYLAQEASVFRKLS 113
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQrDEPHE---NILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIK---AVLEMTPLTPDQqrerlemLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIA 190
Cdd:TIGR01189 90 ALENLHfwaAIHGGAQRTIED-------ALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAG 162
|
170 180
....*....|....*....|...
gi 490460070 191 VQDIQSIVAKLKQRNIGILITDH 213
Cdd:TIGR01189 163 VALLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
35-226 |
9.09e-19 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.77 E-value: 9.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKL-PVYQRARLGIGYLaqeASVFRKLS 113
Cdd:PRK13538 14 RILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQrDEYHQDLLYLGHQ---PGIKTELT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIKAVLemtPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQD 193
Cdd:PRK13538 91 ALENLRFYQ---RLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167
|
170 180 190
....*....|....*....|....*....|....
gi 490460070 194 IQS-IVAKLKQRNIGILITDHnvneTLSITDRAY 226
Cdd:PRK13538 168 LEAlLAQHAEQGGMVILTTHQ----DLPVASDKV 197
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
22-252 |
9.11e-19 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 83.34 E-value: 9.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVG----LVVPNG----GKIYLNEQDITKLPVYQ 93
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGarvtGDVTLNGEPLAAIDAPR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 94 RARLGiGYLAQEASVFRKLSVEDNIkaVLEMTP------LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIA 167
Cdd:PRK13547 81 LARLR-AVLPQAAQPAFAFSAREIV--LLGRYPharragALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 168 RCLA---------IDPKFIMLDEPFAGVDpIAVQD--IQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQ 236
Cdd:PRK13547 158 RVLAqlwpphdaaQPPRYLLLDEPTAALD-LAHQHrlLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
250
....*....|....*.
gi 490460070 237 GTAEQLAENALVREKY 252
Cdd:PRK13547 237 GAPADVLTPAHIARCY 252
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
22-238 |
9.78e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 83.75 E-value: 9.78e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRT-----VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLneQDITKLPVYQRAR 96
Cdd:PRK13631 21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV--GDIYIGDKKNNHE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LGIGYLAQEASVFRKLS--------------VEDNIKAVLEMTPLTPDQQ----RERLEMLIEEFGLHKVRTNQGN-RLS 157
Cdd:PRK13631 99 LITNPYSKKIKNFKELRrrvsmvfqfpeyqlFKDTIEKDIMFGPVALGVKkseaKKLAKFYLNKMGLDDSYLERSPfGLS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 158 GGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTG 258
|
.
gi 490460070 238 T 238
Cdd:PRK13631 259 T 259
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
27-247 |
1.42e-18 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.60 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 27 HLVKRYRSRtvVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGlVVP--NGGKIYLNEQDITKLPVYQRARLGIGYLAQ 104
Cdd:PRK13549 269 DPVNPHIKR--VDDVSFSLRRGEILGIAGLVGAGRTELVQCLFG-AYPgrWEGEIFIDGKPVKIRNPQQAIAQGIAMVPE 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 105 EasvfRK-------LSVEDNIK-AVLE--MTPLTPDQQRErlEMLIEEFGLH-KVRTNQG----NRLSGGERRRVEIARC 169
Cdd:PRK13549 346 D----RKrdgivpvMGVGKNITlAALDrfTGGSRIDDAAE--LKTILESIQRlKVKTASPelaiARLSGGNQQKAVLAKC 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 170 LAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV----LFQG-TAEQLAE 244
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKLkgdlINHNlTQEQVME 499
|
...
gi 490460070 245 NAL 247
Cdd:PRK13549 500 AAL 502
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-198 |
1.66e-18 |
|
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 81.39 E-value: 1.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 21 GLLRTEHLVKRYR--SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-RARL 97
Cdd:cd03244 1 GDIEFKNVSLRYRpnLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDlRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIgyLAQEASVFRKlSVEDN-----------IKAVLEMTPLTP--DQQRERLEMLIEEFGLHkvrtnqgnrLSGGERRRV 164
Cdd:cd03244 81 SI--IPQDPVLFSG-TIRSNldpfgeysdeeLWQALERVGLKEfvESLPGGLDTVVEEGGEN---------LSVGQRQLL 148
|
170 180 190
....*....|....*....|....*....|....
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIV 198
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDPETDALIQKTI 182
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
29-237 |
2.57e-18 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 81.04 E-value: 2.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 29 VKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLpvyqraRLGIGYLAQeasv 108
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL------GLGGGFNPE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 frkLSVEDNIKAVLEMTPLTPDQQRERLEMLIE-----EFGLHKVRTnqgnrLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:cd03220 99 ---LTGRENIYLNGRLLGLSRKEIDEKIDEIIEfselgDFIDLPVKT-----YSSGMKARLAFAIATALEPDILLIDEVL 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 184 AGVDPiAVQD--IQSIVAKLKQRNIGILITdHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03220 171 AVGDA-AFQEkcQRRLRELLKQGKTVILVS-HDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
38-245 |
2.71e-18 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 82.83 E-value: 2.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQR--ARLGIGYLAQE--ASVFRKLS 113
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQDplASLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIKAVLEM--TPLTPDQQRERLEMLIEEFGLhkvRTNQGNR----LSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:PRK15079 117 IGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGL---LPNLINRypheFSGGQCQRIGIARALILEPKLIICDEPVSALD 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 188 pIAVQdiQSIVAKLK--QRNIG---ILITdHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK15079 194 -VSIQ--AQVVNLLQqlQREMGlslIFIA-HDLAVVKHISDRVLVMYLGHAVELGTYDEVYHN 252
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-242 |
2.84e-18 |
|
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: 81.12 E-value: 2.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRS--RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPvYQRARLGIG 100
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYT-LASLRRQIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 101 YLAQEASVFRKlSVEDNIKAVlemtplTPDQQRERLEM---------LIEEF--GLHKVRTNQGNRLSGGERRRVEIARC 169
Cdd:cd03251 80 LVSQDVFLFND-TVAENIAYG------RPGATREEVEEaaraanaheFIMELpeGYDTVIGERGVKLSGGQRQRIAIARA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 170 LAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNeTLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03251 153 LLKDPPILILDEATSALDTESERLVQAALERLMKNRTTFVIA-HRLS-TIENADRIVVLEDGKIVERGTHEEL 223
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
36-242 |
3.41e-18 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 83.60 E-value: 3.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 36 TVVNDVSIELRQGEIVGLLGPNGAGKTTTfymtvGL----VVPNGGKIYLNEQDITK------LPVyqRARLGIGYLAQE 105
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTT-----GLallrLINSQGEIWFDGQPLHNlnrrqlLPV--RHRIQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 106 ASVFRKLSVEDNIKAVLEM--TPLTPDQQRERLEMLIEEFGLH-KVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PRK15134 373 SSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRN-IGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHqLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
38-247 |
4.02e-18 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 83.51 E-value: 4.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQEasvfRK------ 111
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIVYISED----RKrdglvl 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 112 -LSVEDNikavLEMTPLTP--------DQQRERleMLIEEF-GLHKVRT---NQ--GNrLSGGERRRVEIARCLAIDPKF 176
Cdd:PRK10762 344 gMSVKEN----MSLTALRYfsraggslKHADEQ--QAVSDFiRLFNIKTpsmEQaiGL-LSGGNQQKVAIARGLMTRPKV 416
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 177 IMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENAL 247
Cdd:PRK10762 417 LILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKL 487
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
31-242 |
4.36e-18 |
|
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: 80.66 E-value: 4.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 31 RYRSR---TVVNDVSIELRQGEIVGLLGPNGAGKTTT------FYmtvglvVPNGGKIYLNEQDITKLPVYQRARLgIGY 101
Cdd:cd03249 9 RYPSRpdvPILKGLSLTIPPGKTVALVGSSGCGKSTVvsllerFY------DPTSGEILLDGVDIRDLNLRWLRSQ-IGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFrKLSVEDNIK-----AVLEMtpltpdQQRERLEMLIEEF--GL-HKVRTNQGNR---LSGGERRRVEIARCL 170
Cdd:cd03249 82 VSQEPVLF-DGTIAENIRygkpdATDEE------VEEAAKKANIHDFimSLpDGYDTLVGERgsqLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 171 AIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKqRNIGILITDHNVNeTLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDEL 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
38-245 |
1.29e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 80.26 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDIT-----KLPVYQRARLGIGYLAQEASVFRKL 112
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnKNLKKLRKKVSLVFQFPEAQLFENT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 113 SVEDnikavLEMTPL----TPDQQRERLEMLIEEFGLHKVRTNQGN-RLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:PRK13641 103 VLKD-----VEFGPKnfgfSEDEAKEKALKWLKKVGLSEDLISKSPfELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 188 PIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSD 235
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
44-239 |
1.30e-17 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 79.76 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 44 ELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlgigylaQEASVFRKLSVEDNIKAVLE 123
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKAD-------YEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 124 ------MTPLtpdqqreRLEMLIEefglhkvrtNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDpiavQDIQSI 197
Cdd:cd03237 94 yfkteiAKPL-------QIEQILD---------REVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLD----VEQRLM 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490460070 198 VAKLKQRNI-----GILITDHNVNETLSITDRaYLLFEGKVLFQGTA 239
Cdd:cd03237 154 ASKVIRRFAennekTAFVVEHDIIMIDYLADR-LIVFEGEPSVNGVA 199
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
23-244 |
1.49e-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: 81.77 E-value: 1.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYM---------TVGLVVPN------------------ 75
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVlrgmdqyepTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 76 -----GGKIYLNEQDITKL--PVYQRARLGIGYLAQEA-SVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHK 147
Cdd:TIGR03269 81 pcpvcGGTLEPEEVDFWNLsdKLRRRIRKRIAIMLQRTfALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 148 VRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQS-IVAKLKQRNIGILITDHNVNETLSITDRAY 226
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSDKAI 240
|
250
....*....|....*...
gi 490460070 227 LLFEGKVLFQGTAEQLAE 244
Cdd:TIGR03269 241 WLENGEIKEEGTPDEVVA 258
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
30-233 |
1.66e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.84 E-value: 1.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 30 KRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIGYLAQEASVF 109
Cdd:PRK11000 11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAER---GVGMVFQSYALY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 110 RKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDP- 188
Cdd:PRK11000 88 PHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAa 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490460070 189 IAVQdIQSIVAKLKQRnIG---ILITdHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK11000 168 LRVQ-MRIEISRLHKR-LGrtmIYVT-HDQVEAMTLADKIVVLDAGRV 212
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
19-242 |
1.71e-17 |
|
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: 81.98 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 19 ETGLLRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVG-LVVPNGGKIYLNEQDITKLP-VYQr 94
Cdd:TIGR01257 1934 KTDILRLNELTKVYsgTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGdTTVTSGDATVAGKSILTNISdVHQ- 2012
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 95 arlGIGYLAQEASVFRKLSVEDNIKAVLEMTPLtPDQQRERL-EMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAID 173
Cdd:TIGR01257 2013 ---NMGYCPQFDAIDDLLTGREHLYLYARLRGV-PAEEIEKVaNWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 174 PKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-242 |
2.04e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 81.41 E-value: 2.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 19 ETGLLRTEHLVKRY--RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPvYQRAR 96
Cdd:PRK11160 335 DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYS-EAALR 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LGIGYLAQEASVFRKlSVEDNIKAVLemtpltPDQQRERLEMLIEEFGLHKVRTNQ----------GNRLSGGERRRVEI 166
Cdd:PRK11160 414 QAISVVSQRVHLFSA-TLRDNLLLAA------PNASDEALIEVLQQVGLEKLLEDDkglnawlgegGRQLSGGEQRRLGI 486
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 167 ARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNEtLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMIT-HRLTG-LEQFDRICVMDNGQIIEQGTHQEL 560
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
22-242 |
2.83e-17 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 80.88 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRS----RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPN----GGKIYLNEQDITKLPVYQ 93
Cdd:COG4172 6 LLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDPaahpSGSILFDGQDLLGLSERE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 94 RARL---GIGYLAQEAS-----VFRklsVEDNIKAVLEM-TPLTPDQQRER-LEMLiEEFGLHKVRTnqgnR-------L 156
Cdd:COG4172 86 LRRIrgnRIAMIFQEPMtslnpLHT---IGKQIAEVLRLhRGLSGAAARARaLELL-ERVGIPDPER----RldayphqL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 157 SGGERRRVEIARCLAIDPKFIMLDEPFAGVDpIAVQ-DIQSIVAKLKQR-NIGIL-ITdHNVNETLSITDRAYLLFEGKV 233
Cdd:COG4172 158 SGGQRQRVMIAMALANEPDLLIADEPTTALD-VTVQaQILDLLKDLQRElGMALLlIT-HDLGVVRRFADRVAVMRQGEI 235
|
....*....
gi 490460070 234 LFQGTAEQL 242
Cdd:COG4172 236 VEQGPTAEL 244
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
34-181 |
3.04e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 80.78 E-value: 3.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVyQRARLGIGYLAQEASVFRKlS 113
Cdd:PRK13657 347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTR-ASLRRNIAVVFQDAGLFNR-S 424
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 114 VEDNIKavLEMTPLTPDQQRERLE-------MLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:PRK13657 425 IEDNIR--VGRPDATDEEMRAAAEraqahdfIERKPDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDE 497
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
35-242 |
3.25e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 80.94 E-value: 3.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLgIGYLAQEASVF----- 109
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF-INYLPQEPYIFsgsil 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 110 --------RKLSvEDNIKAVLEMTPLTPDqqrerlemlIEEF--GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIML 179
Cdd:TIGR01193 566 enlllgakENVS-QDEIWAACEIAEIKDD---------IENMplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLIL 635
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 180 DEPFAGVDPIAVQDIQSIVAKLKQRNIgILITdHNVNeTLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:TIGR01193 636 DESTSNLDTITEKKIVNNLLNLQDKTI-IFVA-HRLS-VAKQSDKIIVLDHGKIIEQGSHDEL 695
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
35-252 |
4.64e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 4.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARlGIGYLAQ-----EASVF 109
Cdd:PRK10575 24 RTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR-KVAYLPQqlpaaEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 110 RKL---------------SVEDnikavlemtpltpdqqRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDP 174
Cdd:PRK10575 103 RELvaigrypwhgalgrfGAAD----------------REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 175 KFIMLDEPFAGVDpIAVQ-DIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKY 252
Cdd:PRK10575 167 RCLLLDEPTSALD-IAHQvDVLALVHRLsQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIY 245
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
20-209 |
7.40e-17 |
|
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: 77.09 E-value: 7.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 20 TGLLRTEHLVKRY-------RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQ----DITK 88
Cdd:COG4778 2 TTLLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 89 LPVYQRARL---GIGYLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKvrtnqgnRL--------S 157
Cdd:COG4778 82 ASPREILALrrrTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPE-------RLwdlppatfS 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 158 GGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGIL 209
Cdd:COG4778 155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAII 206
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
22-245 |
9.22e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.51 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRT-----------VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLP 90
Cdd:PRK10261 313 ILQVRNLVTRFPLRSgllnrvtrevhAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 91 VY--QRARLGIGYLAQE--ASVFRKLSVEDNIKAVLEMTPLTP-DQQRERLEMLIEEFGL---HKVRtnQGNRLSGGERR 162
Cdd:PRK10261 393 PGklQALRRDIQFIFQDpyASLDPRQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLlpeHAWR--YPHEFSGGQRQ 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 163 RVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLkQRNIGI--LITDHNVNETLSITDRAYLLFEGKVLFQGTAE 240
Cdd:PRK10261 471 RICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL-QRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRR 549
|
....*
gi 490460070 241 QLAEN 245
Cdd:PRK10261 550 AVFEN 554
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
30-241 |
1.22e-16 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 76.66 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 30 KRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQdITKLpvyqrarLGIGylaqeASVF 109
Cdd:COG1134 34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL-------LELG-----AGFH 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 110 RKLSVEDNIKAVLEMTPLTPDQQRERLEMlIEEF-GLHK-----VRTnqgnrLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:COG1134 101 PELTGRENIYLNGRLLGLSRKEIDEKFDE-IVEFaELGDfidqpVKT-----YSSGMRARLAFAVATAVDPDILLVDEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 184 AGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQ 241
Cdd:COG1134 175 AVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEE 232
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
32-240 |
1.25e-16 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 77.23 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 32 YRS-RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIylneqDITKLPVYQRARLG-IGYLAQEASV- 108
Cdd:PRK15056 16 WRNgHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQALQKNlVAYVPQSEEVd 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 --FRKLsVEDNIK----AVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PRK15056 91 wsFPVL-VEDVVMmgryGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 183 FAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAyLLFEGKVLFQGTAE 240
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYT-VMVKGTVLASGPTE 226
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
36-242 |
1.38e-16 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.84 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 36 TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNG---GKIYLNEQDITKLPVYQRARLgigyLAQEAS-VFRK 111
Cdd:PRK09473 30 TAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGrigGSATFNGREILNLPEKELNKL----RAEQISmIFQD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 112 lsvednikavlEMTPLTPDQQRErlEMLIEEFGLHK-----------VR--------------TNQGNRLSGGERRRVEI 166
Cdd:PRK09473 106 -----------PMTSLNPYMRVG--EQLMEVLMLHKgmskaeafeesVRmldavkmpearkrmKMYPHEFSGGMRQRVMI 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 167 ARCLAIDPKFIMLDEPFAGVDpIAVQ-DIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK09473 173 AMALLCRPKLLIADEPTTALD-VTVQaQIMTLLNELKREfNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
44-240 |
1.82e-16 |
|
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: 78.67 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 44 ELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNeqditklpvyqrarLGIGYLAQEASVFRKLSVEDNIKAVLE 123
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED--------------LKISYKPQYISPDYDGTVEEFLRSANT 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 124 MTPLTPDQQRErlemLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDpiaVQDiQSIVAKL-- 201
Cdd:COG1245 428 DDFGSSYYKTE----IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD---VEQ-RLAVAKAir 499
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490460070 202 ---KQRNIGILITDHNVNETLSITDRAyLLFEGKVLFQGTAE 240
Cdd:COG1245 500 rfaENRGKTAMVVDHDIYLIDYISDRL-MVFEGEPGVHGHAS 540
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
37-232 |
3.52e-16 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 74.81 E-value: 3.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEqditklpvyqrarlGIGYLAQEASVFRkLSVED 116
Cdd:cd03250 20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG--------------SIAYVSQEPWIQN-GTIRE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 117 NI-----------KAVLEMTPLTPDqqrerLEMLieEFGLhkvRTNQGNR---LSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03250 85 NIlfgkpfdeeryEKVIKACALEPD-----LEIL--PDGD---LTEIGEKginLSGGQKQRISLARAVYSDADIYLLDDP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 490460070 183 FAGVDPIAVQDI--QSIVAKLKQRNIGILITdHNVnETLSITDRAYLLFEGK 232
Cdd:cd03250 155 LSAVDAHVGRHIfeNCILGLLLNNKTRILVT-HQL-QLLPHADQIVVLDNGR 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
44-239 |
8.79e-16 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 76.77 E-value: 8.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 44 ELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLnEQDITKLPVYQRArlgigylAQEASVFRKLSvedNIKAVLE 123
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP-ELKISYKPQYIKP-------DYDGTVEDLLR---SITDDLG 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 124 MTPLTPDqqrerlemLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDpiaVQDiQSIVAKL-- 201
Cdd:PRK13409 430 SSYYKSE--------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD---VEQ-RLAVAKAir 497
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490460070 202 ---KQRNIGILITDHNVNETLSITDRAyLLFEGKVLFQGTA 239
Cdd:PRK13409 498 riaEEREATALVVDHDIYMIDYISDRL-MVFEGEPGKHGHA 537
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
37-214 |
4.92e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 74.38 E-value: 4.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL---GIGYLAQEASVFRKLS 113
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrreHFGFIFQRYHLLSHLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQD 193
Cdd:PRK10535 103 AAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEE 182
|
170 180
....*....|....*....|.
gi 490460070 194 IQSIVAKLKQRNIGILITDHN 214
Cdd:PRK10535 183 VMAILHQLRDRGHTVIIVTHD 203
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
22-243 |
8.30e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.13 E-value: 8.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRT---------VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVY 92
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 93 QRARLgIGYLAQEASVfrKLSVEDNIKAVLEM-----TPLTPDQQRERLEMLIEEFGLHKVRTN-QGNRLSGGERRRVEI 166
Cdd:PRK15112 84 YRSQR-IRMIFQDPST--SLNPRQRISQILDFplrlnTDLEPEQREKQIIETLRQVGLLPDHASyYPHMLAPGQKQRLGL 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 167 ARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRN-IGILITDHNVNETLSITDRAYLLFEGKVLFQG-TAEQLA 243
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQgISYIYVTQHLGMMKHISDQVLVMHQGEVVERGsTADVLA 239
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
19-242 |
8.65e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.60 E-value: 8.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 19 ETGLLRTEHLVKRYRS-RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPvYQRARL 97
Cdd:PRK10790 337 QSGRIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLS-HSVLRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIGYLAQEASVF-----------RKLSvEDNIKAVLEMTPLTPdqqrerlemLIEEF--GLHKVRTNQGNRLSGGERRRV 164
Cdd:PRK10790 416 GVAMVQQDPVVLadtflanvtlgRDIS-EEQVWQALETVQLAE---------LARSLpdGLYTPLGEQGNNLSVGQKQLL 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITdHNVNeTLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIA-HRLS-TIVEADTILVLHRGQAVEQGTHQQL 561
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-233 |
1.13e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 73.23 E-value: 1.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQE---ASVFRKLSV 114
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEAINHGFALVTEErrsTGIYAYLDI 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 E-----DNIKA------VLEMTPLTPDQQRERLEMLIEEFGlHKvrTNQGNrLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:PRK10982 344 GfnsliSNIRNyknkvgLLDNSRMKSDTQWVIDSMRVKTPG-HR--TQIGS-LSGGNQQKVIIGRWLLTQPEILMLDEPT 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 490460070 184 AGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK10982 420 RGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
22-213 |
1.24e-14 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 71.60 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLvvP----NGGKIYLNEQDITKLPVYQRARL 97
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGH--PaykiLEGDILFKGESILDLEPEERAHL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 GIgYLAQEASV---------FRKLSVEDNIKA--VLEMTPLTPDQQ-RERLEML-IEEFGLHKvRTNQGnrLSGGERRRV 164
Cdd:CHL00131 85 GI-FLAFQYPIeipgvsnadFLRLAYNSKRKFqgLPELDPLEFLEIiNEKLKLVgMDPSFLSR-NVNEG--FSGGEKKRN 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 490460070 165 EIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDH 213
Cdd:CHL00131 161 EILQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-242 |
1.34e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 73.20 E-value: 1.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRS----RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGL-----VVPNGGKIYLNEQDITKLPVY 92
Cdd:PRK15134 5 LLAIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLlpsppVVYPSGDIRFHGESLLHASEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 93 Q-RARLG--IGYLAQEASVfrKLSVEDNI-KAVLEMTPLTPDQQRE--RLEML--IEEFGLHKVRTNQGN---RLSGGER 161
Cdd:PRK15134 85 TlRGVRGnkIAMIFQEPMV--SLNPLHTLeKQLYEVLSLHRGMRREaaRGEILncLDRVGIRQAAKRLTDyphQLSGGER 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 162 RRVEIARCLAIDPKFIMLDEPFAGVDpIAVQ-DIQSIVAKLKQR-NIGILITDHNVNETLSITDRAYLLFEGKVLFQGTA 239
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALD-VSVQaQILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRA 241
|
...
gi 490460070 240 EQL 242
Cdd:PRK15134 242 ATL 244
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
32-213 |
1.72e-14 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 69.98 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 32 YRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITK-LPVYQRARLGIGYlaqEASVFR 110
Cdd:PRK13540 11 YHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLCFVGH---RSGINP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 111 KLSVEDNIKAVLEMTPLTPDqqrerLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIA 190
Cdd:PRK13540 88 YLTLRENCLYDIHFSPGAVG-----ITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELS 162
|
170 180
....*....|....*....|...
gi 490460070 191 VQDIQSIVAKLKQRNIGILITDH 213
Cdd:PRK13540 163 LLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
26-213 |
3.09e-14 |
|
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: 67.86 E-value: 3.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNeqditklpvyqrARLGIGYLAQe 105
Cdd:cd03221 4 ENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG------------STVKIGYFEQ- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 106 asvfrklsvednikavlemtpltpdqqrerlemlieefglhkvrtnqgnrLSGGERRRVEIARCLAIDPKFIMLDEPFAG 185
Cdd:cd03221 71 --------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100
|
170 180
....*....|....*....|....*...
gi 490460070 186 VDPIAvqdIQSIVAKLKQRNIGILITDH 213
Cdd:cd03221 101 LDLES---IEALEEALKEYPGTVILVSH 125
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
19-233 |
4.32e-14 |
|
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: 68.98 E-value: 4.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 19 ETGLLRTEHLVKRYRSR--TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVyQRAR 96
Cdd:cd03369 3 EHGEIEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPL-EDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LGIGYLAQEASVFRKlSVEDNIKAVLEMtplTPDQQRERLEMlieefglhkvrTNQGNRLSGGERRRVEIARCLAIDPKF 176
Cdd:cd03369 82 SSLTIIPQDPTLFSG-TIRSNLDPFDEY---SDEEIYGALRV-----------SEGGLNLSQGQRQLLCLARALLKRPRV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 177 IMLDEPFAGVDPIAVQDIQSIVAKLKQrNIGILITDHNVnETLSITDRAYLLFEGKV 233
Cdd:cd03369 147 LVLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRL-RTIIDYDKILVMDAGEV 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
41-243 |
4.55e-14 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 71.41 E-value: 4.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 41 VSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVvPNGGKIYLNEQDITKLPVYQrARLGIGYLAQEASVFrKLSVEDNIka 120
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPES-WRKHLSWVGQNPQLP-HGTLRDNV-- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 121 vlemTPLTPDQQRERLEMLIE-----EF------GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPI 189
Cdd:PRK11174 444 ----LLGNPDASDEQLQQALEnawvsEFlpllpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 490460070 190 AVQDIQSIVAKLKQRNIGILITdHNVNETLSItDRAYLLFEGKVLFQGTAEQLA 243
Cdd:PRK11174 520 SEQLVMQALNAASRRQTTLMVT-HQLEDLAQW-DQIWVMQDGQIVQQGDYAELS 571
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
23-182 |
6.88e-14 |
|
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: 71.12 E-value: 6.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQdiTKLPVYQRARLGigyL 102
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET--VKLAYVDQSRDA---L 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQEASVFRKLS----------VEDNIKAVLEMTPLT-PDQQRerlemlieefglhKVrtnqgNRLSGGERRRVEIARCLA 171
Cdd:TIGR03719 398 DPNKTVWEEISggldiiklgkREIPSRAYVGRFNFKgSDQQK-------------KV-----GQLSGGERNRVHLAKTLK 459
|
170
....*....|.
gi 490460070 172 IDPKFIMLDEP 182
Cdd:TIGR03719 460 SGGNVLLLDEP 470
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
46-182 |
7.01e-14 |
|
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: 69.32 E-value: 7.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 46 RQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKiYLNEQDITKLPVYQRarlgiGYLAQEasVFRKLsVEDNIKAV---- 121
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPDWDEILDEFR-----GSELQN--YFTKL-LEGDVKVIvkpq 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 122 -LEMTP----------LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03236 95 yVDLIPkavkgkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
37-242 |
1.41e-13 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 70.32 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIylneqditklpvyqRARLGIGYLAQEASVFRKlSVED 116
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI--------------KHSGRISFSPQTSWIMPG-TIKD 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 117 NIkavleMTPLTPDQQRER-------LEMLIEEFGlHKVRT---NQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGV 186
Cdd:TIGR01271 506 NI-----IFGLSYDEYRYTsvikacqLEEDIALFP-EKDKTvlgEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 187 DPIAVQDI-QSIVAKLKQRNIGILITDHnvNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:TIGR01271 580 DVVTEKEIfESCLCKLMSNKTRILVTSK--LEHLKKADKILLLHEGVCYFYGTFSEL 634
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
45-182 |
1.46e-13 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 70.22 E-value: 1.46e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 45 LRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKiYLNEQDITKlpVYQRARlgiGYLAQEasVFRKLSvEDNIKAVL-- 122
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPSWDE--VLKRFR---GTELQN--YFKKLY-NGEIKVVHkp 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 123 ---EMTP----------LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PRK13409 167 qyvDLIPkvfkgkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
45-182 |
1.50e-13 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 69.81 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 45 LRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGkIYLNEQDITKlpVYQRARlgiGYLAQEasVFRKLSvEDNIKAVL-- 122
Cdd:COG1245 96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLG-DYDEEPSWDE--VLKRFR---GTELQD--YFKKLA-NGEIKVAHkp 166
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 123 ---EMTP----------LTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:COG1245 167 qyvDLIPkvfkgtvrelLEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
37-242 |
1.92e-13 |
|
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: 68.73 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIylneqditklpvyqRARLGIGYLAQEASVFRKlSVED 116
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI--------------KHSGRISFSSQFSWIMPG-TIKE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 117 NIkavleMTPLTPDQQRER-------LEMLIEEFGL--HKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:cd03291 117 NI-----IFGVSYDEYRYKsvvkacqLEEDITKFPEkdNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 188 PIAVQDI-QSIVAKLKQRNIGILITdhNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03291 192 VFTEKEIfESCVCKLMANKTRILVT--SKMEHLKKADKILILHEGSSYFYGTFSEL 245
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
30-237 |
2.52e-13 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 66.90 E-value: 2.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 30 KRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNG---GKIYLNeqDITKLPVYQRARLGIGYLAQEA 106
Cdd:cd03233 15 KGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYN--GIPYKEFAEKYPGEIIYVSEED 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 107 SVFRKLSVEDNIKAVLEMtpltpdqqrerlemlieefglhkvrtnQGNR----LSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:cd03233 93 VHFPTLTVRETLDFALRC---------------------------KGNEfvrgISGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 183 FAGVDPIA----VQDIQSIVAKLKQRNIGILItdHNVNETLSITDRAYLLFEGKVLFQG 237
Cdd:cd03233 146 TRGLDSSTaleiLKCIRTMADVLKTTTFVSLY--QASDEIYDLFDKVLVLYEGRQIYYG 202
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-247 |
2.70e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 68.45 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 21 GLLRTEHLVKryrsrtVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL--G 98
Cdd:PRK11308 20 GLFKPERLVK------ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLrqK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQE--ASVFRKLSVEDNIKAVLEM-TPLTPDQQRERLEMLIEEFGLhkvRTNQGNR----LSGGERRRVEIARCLA 171
Cdd:PRK11308 94 IQIVFQNpyGSLNPRKKVGQILEEPLLInTSLSAAERREKALAMMAKVGL---RPEHYDRyphmFSGGQRQRIAIARALM 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 172 IDPKFIMLDEPFAGVDpIAVQ--------DIQsivaklKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLA 243
Cdd:PRK11308 171 LDPDVVVADEPVSALD-VSVQaqvlnlmmDLQ------QELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIF 243
|
....
gi 490460070 244 ENAL 247
Cdd:PRK11308 244 NNPR 247
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-267 |
3.70e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.22 E-value: 3.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 18 GETGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTfYMTVGLVVPNGGKiylNEQDITKLPVYQRA-R 96
Cdd:NF000106 9 GARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANRRAlR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LGIG-YLAQEASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPK 175
Cdd:NF000106 85 RTIG*HRPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLaenalvREKYLGR 255
Cdd:NF000106 165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL------KTKVGGR 238
|
250
....*....|..
gi 490460070 256 DFVLRRKSFADL 267
Cdd:NF000106 239 TLQIRPAHAAEL 250
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
38-232 |
4.87e-13 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 68.22 E-value: 4.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQEASVFRKLSVEDN 117
Cdd:PRK10982 14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQELNLVLQRSVMDN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 118 IkaVLEMTPLT-----PDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQ 192
Cdd:PRK10982 94 M--WLGRYPTKgmfvdQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKEVN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 490460070 193 DIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGK 232
Cdd:PRK10982 172 HLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
32-246 |
5.67e-13 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 68.28 E-value: 5.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 32 YRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTtFYMTV-----GLVVpnGGKIYLNEQDITKLPVYQRARLGIGYLAQEa 106
Cdd:NF040905 270 HPERKVVDDVSLNVRRGEIVGIAGLMGAGRTE-LAMSVfgrsyGRNI--SGTVFKDGKEVDVSTVSDAIDAGLAYVTED- 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 107 svfRK---LSVEDNIKAVLEMTPLTP-------DQQRE-------RLEMLIEEfglHKVRTNQGNrLSGGERRRVEIARC 169
Cdd:NF040905 346 ---RKgygLNLIDDIKRNITLANLGKvsrrgviDENEEikvaeeyRKKMNIKT---PSVFQKVGN-LSGGNQQKVVLSKW 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 170 LAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVlfqgTAEQLAENA 246
Cdd:NF040905 419 LFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELPELLGMCDRIYVMNEGRI----TGELPREEA 491
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
22-233 |
6.55e-13 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 68.27 E-value: 6.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEqditklpvyqrarlGI-- 99
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAK--------------GIkl 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 GYLAQEASVFrkLSVEDNikAVLEMTPLTPDQQRERLEMLIEEFGLH--KVrTNQGNRLSGGERRRVEIARCLAIDPKFI 177
Cdd:PRK10636 378 GYFAQHQLEF--LRADES--PLQHLARLAPQELEQKLRDYLGGFGFQgdKV-TEETRRFSGGEKARLVLALIVWQRPNLL 452
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 178 MLDEPFAGVDpiaVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK10636 453 LLDEPTNHLD---LDMRQALTEALIDFEGALVVVSHDRHLLRSTTDDLYLVHDGKV 505
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
48-255 |
7.50e-13 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 67.72 E-value: 7.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 48 GEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKI-YLNEQDITKLP-VYQRArlGIGYLAQEASVFRKLSVEDNIKAVLEMT 125
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPkSSQEA--GIGIIHQELNLIPQLTIAENIFLGREFV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 126 plTP------DQQRERLEMLIEEFGL-HKVRTNQGNrLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIV 198
Cdd:PRK10762 108 --NRfgridwKKMYAEADKLLARLNLrFSSDKLVGE-LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVI 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 199 AKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVrEKYLGR 255
Cdd:PRK10762 185 RELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVADLTEDSLI-EMMVGR 240
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
3-188 |
8.84e-13 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 67.52 E-value: 8.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 3 DTIDTAEALSPDRHKGET---GLLRTEHL-VKRYRSRTVVNDVSIELRQGEivGLL--GPNGAGKTTTFYMTVGLVvPNG 76
Cdd:COG4178 340 EALEAADALPEAASRIETsedGALALEDLtLRTPDGRPLLEDLSLSLKPGE--RLLitGPSGSGKSTLLRAIAGLW-PYG 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 77 -GKIYLNE-QDITKLPvyQRARLGIGYLAQeasvfrklsvednikAVLemTPLTPDQ-QRERLEMLIEEFGLHK------ 147
Cdd:COG4178 417 sGRIARPAgARVLFLP--QRPYLPLGTLRE---------------ALL--YPATAEAfSDAELREALEAVGLGHlaerld 477
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 490460070 148 VRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDP 188
Cdd:COG4178 478 EEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDE 518
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
26-182 |
1.95e-12 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 66.68 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNE---------------------- 83
Cdd:PRK11819 328 ENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGEtvklayvdqsrdaldpnktvwe 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 84 -----QDITKLPVYQ---RArlgigYLAQeasvFrklsvedNIKAvlemtpltPDQQRerlemlieefglhKVRTnqgnr 155
Cdd:PRK11819 408 eisggLDIIKVGNREipsRA-----YVGR----F-------NFKG--------GDQQK-------------KVGV----- 445
|
170 180
....*....|....*....|....*..
gi 490460070 156 LSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PRK11819 446 LSGGERNRLHLAKTLKQGGNVLLLDEP 472
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
29-233 |
2.16e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 2.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 29 VKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIgYLAQEAsv 108
Cdd:PRK11288 260 LDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGI-MLCPED-- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 fRK-------LSVEDN--IKAVLEMTP----LTPDQQRERLEMLIEEFglhKVRTNQGNR----LSGGERRRVEIARCLA 171
Cdd:PRK11288 337 -RKaegiipvHSVADNinISARRHHLRagclINNRWEAENADRFIRSL---NIKTPSREQlimnLSGGNQQKAILGRWLS 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 172 IDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKV 233
Cdd:PRK11288 413 EDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
36-187 |
6.52e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 63.26 E-value: 6.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 36 TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARL---GIGYLAQEASVFRKL 112
Cdd:PRK10584 24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakHVGFVFQSFMLIPTL 103
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 113 SVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:PRK10584 104 NALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
40-256 |
6.97e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.93 E-value: 6.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDItklpVYQRAR----LGIGYLAQEASVFRKLSVE 115
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM----RFASTTaalaAGVAIIYQELHLVPEMTVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 116 DNIkaVLEMTP---------LTPDQQRERLEMLIEEFGLH-KVRtnqgnRLSGGERRRVEIARCLAIDPKFIMLDEPFAG 185
Cdd:PRK11288 98 ENL--YLGQLPhkggivnrrLLNYEAREQLEHLGVDIDPDtPLK-----YLSIGQRQMVEIAKALARNARVIAFDEPTSS 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 186 VDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKvlFQGTAEQLAE---NALVREkYLGRD 256
Cdd:PRK11288 171 LSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGR--YVATFDDMAQvdrDQLVQA-MVGRE 241
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
38-187 |
1.38e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 62.35 E-value: 1.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLN---EQDITKLPVYQRARLGIGYLAQEASVFRKlSV 114
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSnknESEPSFEATRSRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 EDNI-----------KAVLEMTPLTPDqqrerLEMLieEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPF 183
Cdd:cd03290 96 EENItfgspfnkqryKAVTDACSLQPD-----IDLL--PFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
....
gi 490460070 184 AGVD 187
Cdd:cd03290 169 SALD 172
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
20-245 |
3.01e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 3.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 20 TGLLRTEHLVKRYRSR--TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-RAR 96
Cdd:PLN03130 1235 SGSIKFEDVVLRYRPElpPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDlRKV 1314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 97 LGIgylAQEASVFRKLSVEDNIKAVLEMT--PLTPDQQRERLEMLIEE--FGLHKVRTNQGNRLSGGERRRVEIARCLAI 172
Cdd:PLN03130 1315 LGI---IPQAPVLFSGTVRFNLDPFNEHNdaDLWESLERAHLKDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLR 1391
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 173 DPKFIMLDEPFAGVDPIAVQDIQSIVAKlKQRNIGILITDHNVNeTLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PLN03130 1392 RSKILVLDEATAAVDVRTDALIQKTIRE-EFKSCTMLIIAHRLN-TIIDCDRILVLDAGRVVEFDTPENLLSN 1462
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
38-242 |
1.83e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.83e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNeqditKLPVYQRARLGIGYLAQEASVFRKLSVEDN 117
Cdd:PRK10261 32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCD-----KMLLRRRSRQVIELSEQSAAQMRHVRGADM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 118 IKAVLE-MTPLTP--------------DQQRERLEMLIE-EFGLHKVRTNQG--------NRLSGGERRRVEIARCLAID 173
Cdd:PRK10261 107 AMIFQEpMTSLNPvftvgeqiaesirlHQGASREEAMVEaKRMLDQVRIPEAqtilsrypHQLSGGMRQRVMIAMALSCR 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 174 PKFIMLDEPFAGVD-PIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK10261 187 PAVLIADEPTTALDvTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQI 256
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
38-242 |
2.04e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.14 E-value: 2.04e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNG----GKIYLNEQDITKLPVYQRARLgIGylAQEASVFRKls 113
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDYPGrvmaEKLEFNGQDLQRISEKERRNL-VG--AEVAMIFQD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 vednikavlEMTPLTP--------------------DQQRERLEMLIEEFGLHKVRT---NQGNRLSGGERRRVEIARCL 170
Cdd:PRK11022 98 ---------PMTSLNPcytvgfqimeaikvhqggnkKTRRQRAIDLLNQVGIPDPASrldVYPHQLSGGMSQRVMIAMAI 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 171 AIDPKFIMLDEPFAGVD-PIAVQDIQSIVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK11022 169 ACRPKLLIADEPTTALDvTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDI 241
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
21-196 |
2.40e-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: 60.60 E-value: 2.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 21 GLLRTEHLVKRYRS-RTVVNDVSIELRQGEIVGLLGPNGAGKTTT------FYMtvglvvPNGGKIYLNEQDITKLPvyQ 93
Cdd:COG5265 356 GEVRFENVSFGYDPeRPILKGVSFEVPAGKTVAIVGPSGAGKSTLarllfrFYD------VTSGRILIDGQDIRDVT--Q 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 94 ---RARLG----------------IGYLAQEASvfrklsvEDNIKAVLEMTPL------TPDQqrerLEMLIEEFGLhkv 148
Cdd:COG5265 428 aslRAAIGivpqdtvlfndtiaynIAYGRPDAS-------EEEVEAAARAAQIhdfiesLPDG----YDTRVGERGL--- 493
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490460070 149 rtnqgnRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQS 196
Cdd:COG5265 494 ------KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQA 535
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
35-182 |
2.64e-10 |
|
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: 60.33 E-value: 2.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEqDITklpvyqrarlgIGYLAQEASVFRKLSV 114
Cdd:TIGR03719 18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQP-GIK-----------VGYLPQEPQLDPTKTV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 EDN-------IKAVL---------------EMTPLTPDQqrERLEMLIEEFGLHKVRTN---------------QGNRLS 157
Cdd:TIGR03719 86 RENveegvaeIKDALdrfneisakyaepdaDFDKLAAEQ--AELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKLS 163
|
170 180
....*....|....*....|....*
gi 490460070 158 GGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:TIGR03719 164 GGERRRVALCRLLLSKPDMLLLDEP 188
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
48-224 |
3.69e-10 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 58.32 E-value: 3.69e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 48 GEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLpvyQRARLgIGYLAQEASVFRKLSVEDNIKAVLEMTPL 127
Cdd:PRK13543 37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRF-MAYLGHLPGLKADLSTLENLHFLCGLHGR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 128 TPDQQRERLEMLIeefGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIG 207
Cdd:PRK13543 113 RAKQMPGSALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRGGGA 189
|
170
....*....|....*..
gi 490460070 208 ILITDHNVNETLSITDR 224
Cdd:PRK13543 190 ALVTTHGAYAAPPVRTR 206
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-245 |
3.78e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 21 GLLRTEHLVKRYRSR--TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLg 98
Cdd:PLN03232 1233 GSIKFEDVHLRYRPGlpPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV- 1311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFRKlSVEDNIKAVLEMTP--LTPDQQRERLEMLIEE--FGLHKVRTNQGNRLSGGERRRVEIARCLAIDP 174
Cdd:PLN03232 1312 LSIIPQSPVLFSG-TVRFNIDPFSEHNDadLWEALERAHIKDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRS 1390
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 175 KFIMLDEPFAGVDPIAVQDIQSIVAKlKQRNIGILITDHNVNeTLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PLN03232 1391 KILVLDEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLN-TIIDCDKILVLSSGQVLEYDSPQELLSR 1459
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
34-244 |
5.89e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 59.34 E-value: 5.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-RARLGIgyLAQEASVFRKl 112
Cdd:PRK10789 327 DHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRLAV--VSQTPFLFSD- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 113 SVEDNIKAVlemtplTPDQQRERLEMLIEEFGLHK--------VRTNQGNR---LSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:PRK10789 404 TVANNIALG------RPDATQQEIEHVARLASVHDdilrlpqgYDTEVGERgvmLSGGQKQRISIARALLLNAEILILDD 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 182 PFAGVDPiavQDIQSIVAKLKQ--RNIGILITDHNVNeTLSITDRAYLLFEGKVLFQGTAEQLAE 244
Cdd:PRK10789 478 ALSAVDG---RTEHQILHNLRQwgEGRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQ 538
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
35-213 |
7.10e-10 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 57.66 E-value: 7.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLvvpnggkiylneqdITKLPVYQRARLGIGYLAQEASVFRKLSV 114
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGA--------------LKGTPVAGCVDVPDNQFGREASLIDAIGR 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 EDNIKAVLEMtpltpdqqrerlemlieefgLHKVRTNQG-------NRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:COG2401 109 KGDFKDAVEL--------------------LNAVGLSDAvlwlrrfKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLD 168
|
170 180
....*....|....*....|....*..
gi 490460070 188 PIAVQDIQSIVAKL-KQRNIGILITDH 213
Cdd:COG2401 169 RQTAKRVARNLQKLaRRAGITLVVATH 195
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
38-245 |
8.35e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 58.75 E-value: 8.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIylneqDITKlpvyqRARLgigyLAQEASVFRKLSVEDN 117
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DIKG-----SAAL----IAISSGLNGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 118 IKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSI 197
Cdd:PRK13545 106 IELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDK 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490460070 198 VAKLKQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PRK13545 186 MNEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
35-242 |
8.51e-10 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 57.79 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPN----GGKIYLNEQDItkLPVYQRARLGIGYLAQEASVFR 110
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPV--APCALRGRKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 111 KL-SVEDNIKAVLEMTPLTPDQQreRLEMLIEEFGL---HKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGV 186
Cdd:PRK10418 94 PLhTMHTHARETCLALGKPADDA--TLTAALEAVGLenaARVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 187 DPIAVQDIQSIVAKL-KQRNIGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK10418 172 DVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-192 |
2.45e-09 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 56.47 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 22 LLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGY 101
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVFrklsVEDNIKAVLEMTPLTPDQQRERLeMLIEE--FG---------LHKVRTNQgNRL-------SGGERRR 163
Cdd:PRK11701 86 LLRTEWGF----VHQHPRDGLRMQVSAGGNIGERL-MAVGArhYGdiratagdwLERVEIDA-ARIddlpttfSGGMQQR 159
|
170 180
....*....|....*....|....*....
gi 490460070 164 VEIARCLAIDPKFIMLDEPFAGVDpIAVQ 192
Cdd:PRK11701 160 LQIARNLVTHPRLVFMDEPTGGLD-VSVQ 187
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
33-244 |
2.77e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.43 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 33 RSRTVVNDVSIELRQGEIVGLLGPNGAGKTT----TFYMTVGLVVPNGGKIYLNeqDITKLPVYQRARLGIGYLAQEASV 108
Cdd:TIGR00956 72 KTFDILKPMDGLIKPGELTVVLGRPGSGCSTllktIASNTDGFHIGVEGVITYD--GITPEEIKKHYRGDVVYNAETDVH 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 FRKLSVEDNIKAVLEM-TP------LTPDQQRERL-EMLIEEFGL-HKVRTNQGNRL----SGGERRRVEIARCLAIDPK 175
Cdd:TIGR00956 150 FPHLTVGETLDFAARCkTPqnrpdgVSREEYAKHIaDVYMATYGLsHTRNTKVGNDFvrgvSGGERKRVSIAEASLGGAK 229
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 176 FIMLDEPFAGVD-PIAVQDIQSIVAKLKQRNIGILITDHNVNE-TLSITDRAYLLFEGKVLFQGTAEQLAE 244
Cdd:TIGR00956 230 IQCWDNATRGLDsATALEFIRALKTSANILDTTPLVAIYQCSQdAYELFDKVIVLYEGYQIYFGPADKAKQ 300
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
28-187 |
4.04e-09 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 56.39 E-value: 4.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 28 LVKRYRSRT-VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRarlGIgylaqeA 106
Cdd:PRK11650 9 VRKSYDGKTqVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR---DI------A 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 107 SVFRK------LSVEDNIKAVLEMTPLTPDQQRERLE----ML-IEEFGLHKVRtnqgnRLSGGERRRVEIARCLAIDPK 175
Cdd:PRK11650 80 MVFQNyalyphMSVRENMAYGLKIRGMPKAEIEERVAeaarILeLEPLLDRKPR-----ELSGGQRQRVAMGRAIVREPA 154
|
170
....*....|..
gi 490460070 176 FIMLDEPFAGVD 187
Cdd:PRK11650 155 VFLFDEPLSNLD 166
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-250 |
5.28e-09 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 56.84 E-value: 5.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 21 GLLRTEHLVKRYRS--RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNgGKIYLNEQDITKLPVyQRARLG 98
Cdd:TIGR01271 1216 GQMDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTL-QTWRKA 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 99 IGYLAQEASVFrklsvEDNIKAVLEMTPLTPDQQRER------LEMLIEEF--GLHKVRTNQGNRLSGGERRRVEIARCL 170
Cdd:TIGR01271 1294 FGVIPQKVFIF-----SGTFRKNLDPYEQWSDEEIWKvaeevgLKSVIEQFpdKLDFVLVDGGYVLSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 171 AIDPKFIMLDEPFAGVDPIAVQDIQSivaKLKQ--RNIGILITDHNVNETLSItdRAYLLFEGKVLFQGTAEQ--LAENA 246
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRK---TLKQsfSNCTVILSEHRVEALLEC--QQFLVIEGSSVKQYDSIQklLNETS 1443
|
....
gi 490460070 247 LVRE 250
Cdd:TIGR01271 1444 LFKQ 1447
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
35-181 |
6.66e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 54.49 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLpvyqrARLGIGYLAQEASVFRKLSV 114
Cdd:PRK13541 13 QKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-----AKPYCTYIGHNLGLKLEMTV 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 115 EDNIKAVLEMTpltpdQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:PRK13541 88 FENLKFWSEIY-----NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
37-181 |
8.43e-09 |
|
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: 55.91 E-value: 8.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYL-NEQDITKLPvyQRARLGIGYLaqeasvfrklsvE 115
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKpAKGKLFYVP--QRPYMTLGTL------------R 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 116 DNIkavleMTPLTPDQQRER------LEMLIEEFGLHKVRTNQG---------NRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:TIGR00954 533 DQI-----IYPDSSEDMKRRglsdkdLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILD 607
|
.
gi 490460070 181 E 181
Cdd:TIGR00954 608 E 608
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
134-248 |
1.24e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 55.02 E-value: 1.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 134 ERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDH 213
Cdd:PRK10938 114 ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLN 193
|
90 100 110
....*....|....*....|....*....|....*
gi 490460070 214 NVNETLSITDRAYLLFEGKVLFQGTAEQLAENALV 248
Cdd:PRK10938 194 RFDEIPDFVQFAGVLADCTLAETGEREEILQQALV 228
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
39-232 |
1.51e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 39 NDVSIELRQGEIVGLLGPNGAGKTTtfYMTV--GlVVPNG---GKIYLNEQ-----DITklpvyQRARLGIGYLAQEASV 108
Cdd:NF040905 18 DDVNLSVREGEIHALCGENGAGKST--LMKVlsG-VYPHGsyeGEILFDGEvcrfkDIR-----DSEALGIVIIHQELAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 FRKLSVEDNI--------KAVLEMtpltpDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:NF040905 90 IPYLSIAENIflgnerakRGVIDW-----NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 181 EPFAgvdpiAVQDIQS-----IVAKLKQRNIGILITDHNVNETLSITDRAYLLFEGK 232
Cdd:NF040905 165 EPTA-----ALNEEDSaalldLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
33-188 |
1.57e-08 |
|
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: 52.54 E-value: 1.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 33 RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVvPNG-GKIYLNEQ-DITKLPvyQRARLGIGYLAqEASVFr 110
Cdd:cd03223 12 DGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLW-PWGsGRIGMPEGeDLLFLP--QRPYLPLGTLR-EQLIY- 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 111 klsvednikavlemtPLtpdqqrerlemlieefglhkvrtnqGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDP 188
Cdd:cd03223 87 ---------------PW-------------------------DDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE 124
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
34-231 |
2.43e-08 |
|
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: 52.63 E-value: 2.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYM-----TVGLVvpnGGKIYLNEQDITKlpVYQRarlGIGYLAQEASV 108
Cdd:cd03232 19 KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVlagrkTAGVI---TGEILINGRPLDK--NFQR---STGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 FRKLSVednikavlemtpltpdqqRERLEMlieefglhkvrtNQGNR-LSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:cd03232 91 SPNLTV------------------REALRF------------SALLRgLSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 490460070 188 PIAVQDIQSIVAKLKQRNIGILITDHNVNETL-SITDRAYLLFEG 231
Cdd:cd03232 141 SQAAYNIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
34-253 |
4.75e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 4.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 34 SRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGlvvpnggkiYLNEQDITKLPVyqraRLGIGYLAQEASVFRKlS 113
Cdd:PLN03232 629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLG---------ELSHAETSSVVI----RGSVAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIKavlemtpLTPDQQRERLEMLIEEFGLH--------KVRTNQGNR---LSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PLN03232 695 VRENIL-------FGSDFESERYWRAIDVTALQhdldllpgRDLTEIGERgvnISGGQKQRVSMARAVYSNSDIYIFDDP 767
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 183 FAGVDP-IAVQDIQSIVAKLKQRNIGILITdhNVNETLSITDRAYLLFEGKVLFQGTAEQLAENALVREKYL 253
Cdd:PLN03232 768 LSALDAhVAHQVFDSCMKDELKGKTRVLVT--NQLHFLPLMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM 837
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
37-242 |
4.85e-08 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 52.88 E-value: 4.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPN----GGKIYLNEQDITKLPVYQRARL---GIGYLAQE---- 105
Cdd:PRK15093 22 AVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNwrvtADRMRFDDIDLLRLSPRERRKLvghNVSMIFQEpqsc 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 106 ----ASVFRKLsvednIKAVLEMTPLTPDQQR--ERLEMLIEEfgLHKVRTNQGN--------RLSGGERRRVEIARCLA 171
Cdd:PRK15093 102 ldpsERVGRQL-----MQNIPGWTYKGRWWQRfgWRKRRAIEL--LHRVGIKDHKdamrsfpyELTEGECQKVMIAIALA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 172 IDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRN-IGILITDHNVNETLSITDRAYLLFEGKVLFQGTAEQL 242
Cdd:PRK15093 175 NQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNnTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKEL 246
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
35-213 |
6.43e-08 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.19 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTT----------TFYMTVGLVVPNGGKI---------YLNEQDITKLPVYQRA 95
Cdd:TIGR00956 776 RVILNNVDGWVKPGTLTALMGASGAGKTTllnvlaervtTGVITGGDRLVNGRPLdssfqrsigYVQQQDLHLPTSTVRE 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 96 RLGI-GYLAQEASVFR--KLSVEDNIKAVLEMTPLTpdqqrerlEMLIeefGLhkvrtnQGNRLSGGERRRVEIARCLAI 172
Cdd:TIGR00956 856 SLRFsAYLRQPKSVSKseKMEYVEEVIKLLEMESYA--------DAVV---GV------PGEGLNVEQRKRLTIGVELVA 918
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 490460070 173 DPKFIM-LDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITDH 213
Cdd:TIGR00956 919 KPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
35-244 |
6.46e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.10 E-value: 6.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGL--VVPNGGKIYLNEQDITKLPVYQRARLGI----GYLAQEASV 108
Cdd:PRK09580 14 KAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEGIfmafQYPVEIPGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 109 FRKLSVEDNIKAVLEMTPLTP-------DQQRERLEMLIEEFGLHKVRTNQGnrLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:PRK09580 94 SNQFFLQTALNAVRSYRGQEPldrfdfqDLMEEKIALLKMPEDLLTRSVNVG--FSGGEKKRNDILQMAVLEPELCILDE 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 182 PFAGVDPIAVQDIQSIVAKLKQRNIGILITDHNVNETLSIT-DRAYLLFEGKVLFQGT---AEQLAE 244
Cdd:PRK09580 172 SDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKpDYVHVLYQGRIVKSGDftlVKQLEE 238
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
38-187 |
9.26e-08 |
|
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: 53.03 E-value: 9.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLnEQDITKLPvyQRARLGIGYLaQEASVFRKLSVEDN 117
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM-KGSVAYVP--QQAWIQNDSL-RENILFGKALNEKY 729
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 118 IKAVLEMTPLTPDqqrerLEMLIE----EFGlhkvrtNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:TIGR00957 730 YQQVLEACALLPD-----LEILPSgdrtEIG------EKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
39-245 |
9.92e-08 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 52.33 E-value: 9.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 39 NDVSIELRQGEIVGLLGPNGAGKTTT------FYMTvglvvpNGGKIYLNEQDIT--KLP--------VYQRARL----- 97
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIanlltrFYDI------DEGEILLDGHDLRdyTLAslrnqvalVSQNVHLfndti 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 98 --GIGYLAQEasvfrKLSVEDNIKAVlEMTpltpdQQRERLEMLieEFGLHKVRTNQGNRLSGGERRRVEIARCLAIDPK 175
Cdd:PRK11176 434 anNIAYARTE-----QYSREQIEEAA-RMA-----YAMDFINKM--DNGLDTVIGENGVLLSGGQRQRIAIARALLRDSP 500
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490460070 176 FIMLDEPFAGVDPIAVQDIQSIVAKLkQRNIGILITDHNVNeTLSITDRAYLLFEGKVLFQGT-AEQLAEN 245
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLS-TIEKADEILVVEDGEIVERGThAELLAQN 569
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
24-190 |
9.98e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 9.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 24 RTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKlpVYQRARLG--IGY 101
Cdd:NF033858 3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD--ARHRRAVCprIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQ--EASVFRKLSVEDNIKAVLEMTPLTPDQQRERLEMLIEEFGLHKVRTNQGNRLSGGERRRVEIarCLAI--DPKFI 177
Cdd:NF033858 81 MPQglGKNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGL--CCALihDPDLL 158
|
170
....*....|...
gi 490460070 178 MLDEPFAGVDPIA 190
Cdd:NF033858 159 ILDEPTTGVDPLS 171
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
133-253 |
1.03e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 52.91 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 133 RERLEMLIEeFGLHKVRTNQG-NRLSGGERRRVEIARCLAIDPKFIM--LDEPFAGVDPIAVQDIQSIVAKLKQRNIGIL 209
Cdd:PRK00635 454 KSRLSILID-LGLPYLTPERAlATLSGGEQERTALAKHLGAELIGITyiLDEPSIGLHPQDTHKLINVIKKLRDQGNTVL 532
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490460070 210 ITDHNvNETLSITDR------AYLLFEGKVLFQGT-AEQLAENALVREKYL 253
Cdd:PRK00635 533 LVEHD-EQMISLADRiidigpGAGIFGGEVLFNGSpREFLAKSDSLTAKYL 582
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
26-241 |
1.41e-07 |
|
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: 50.26 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 26 EHLVKRYRSRTVVNDVSiELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNeqditklpvyqraRLGIGYLAQE 105
Cdd:cd03222 4 PDCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWD-------------GITPVYKPQY 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 106 ASvfrklsvednikavlemtpltpdqqrerlemlieefglhkvrtnqgnrLSGGERRRVEIARCLAIDPKFIMLDEPFAG 185
Cdd:cd03222 70 ID------------------------------------------------LSGGELQRVAIAAALLRNATFYLFDEPSAY 101
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 186 VDPIAVQDIQSIVAKLKQRNI-GILITDHNVNETLSITDRAYlLFEGKVLFQGTAEQ 241
Cdd:cd03222 102 LDIEQRLNAARAIRRLSEEGKkTALVVEHDLAVLDYLSDRIH-VFEGEPGVYGIASQ 157
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
72-211 |
1.51e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 52.34 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 72 VVPNGGKIYLNEQDITKLPVYQRARLgIGYLAQEASVFrKLSVEDNIKAVLEMTPLTpDQQRERLEMLIEEF--GL-HKV 148
Cdd:PTZ00265 1272 VFKNSGKILLDGVDICDYNLKDLRNL-FSIVSQEPMLF-NMSIYENIKFGKEDATRE-DVKRACKFAAIDEFieSLpNKY 1348
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490460070 149 RTN---QGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILIT 211
Cdd:PTZ00265 1349 DTNvgpYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIIT 1414
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
38-188 |
2.40e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQrarlgigYLAQEASVFRKLSVEDN 117
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPED-------YRKLFSAVFTDFHLFDQ 411
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490460070 118 I--KAVLEMTPLTPDQQRERLEMlieefgLHKVRTNQGN----RLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDP 188
Cdd:PRK10522 412 LlgPEGKPANPALVEKWLERLKM------AHKLELEDGRisnlKLSKGQKKRLALLLALAEERDILLLDEWAADQDP 482
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
36-219 |
2.94e-07 |
|
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: 50.24 E-value: 2.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 36 TVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGgKIYLNEQDITKLPVyQRARLGIGYLAQEASVFrklsvE 115
Cdd:cd03289 18 AVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEG-DIQIDGVSWNSVPL-QKWRKAFGVIPQKVFIF-----S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 116 DNIKAVLEMTPLTPDQQRER------LEMLIEEF--GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVD 187
Cdd:cd03289 91 GTFRKNLDPYGKWSDEEIWKvaeevgLKSVIEQFpgQLDFVLVDGGCVLSHGHKQLMCLARSVLSKAKILLLDEPSAHLD 170
|
170 180 190
....*....|....*....|....*....|....
gi 490460070 188 PIAVQDIQSIvakLKQ--RNIGILITDHNVNETL 219
Cdd:cd03289 171 PITYQVIRKT---LKQafADCTVILSEHRIEAML 201
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
18-242 |
3.56e-07 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 49.91 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 18 GETGLLRTEHLVKRYRS--RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQ-R 94
Cdd:cd03288 15 GLGGEIKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTlR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 95 ARLGIgyLAQEASVFRKlSVEDNIKAVLEMTPLTPDQQRE--RLEMLIEEF--GLHKVRTNQGNRLSGGERRRVEIARCL 170
Cdd:cd03288 95 SRLSI--ILQDPILFSG-SIRFNLDPECKCTDDRLWEALEiaQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAF 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490460070 171 AIDPKFIMLDEPFAGVDpIAVQDIQSIVAKLKQRNIGILITDHNVNETLSiTDRAYLLFEGKVLFQGTAEQL 242
Cdd:cd03288 172 VRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENL 241
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
31-247 |
5.27e-07 |
|
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: 50.71 E-value: 5.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 31 RYRSRT--VVNDVSIELRQGEIVGLLGPNGAGKTTtfyMTVGLVVPN---GGKIYLNEQDITKLPVYQ-RARLGI----- 99
Cdd:TIGR00957 1293 RYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSS---LTLGLFRINesaEGEIIIDGLNIAKIGLHDlRFKITIipqdp 1369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 100 ----GYLAQEASVFRKLSVEDnIKAVLEMTPL------TPDqqrerlemlieefGLHKVRTNQGNRLSGGERRRVEIARC 169
Cdd:TIGR00957 1370 vlfsGSLRMNLDPFSQYSDEE-VWWALELAHLktfvsaLPD-------------KLDHECAEGGENLSVGQRQLVCLARA 1435
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490460070 170 LAIDPKFIMLDEPFAGVDPIAVQDIQSIVaKLKQRNIGILITDHNVNETLSITdRAYLLFEGKVL-FQGTAEQLAENAL 247
Cdd:TIGR00957 1436 LLRKTKILVLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAeFGAPSNLLQQRGI 1512
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
41-181 |
8.74e-07 |
|
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: 49.41 E-value: 8.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 41 VSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLpvyQRARlgigYLAQEASVF-------RKLS 113
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAD---NREA----YRQLFSAVFsdfhlfdRLLG 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 114 VEDNIkavlemtpltpdqQRERLEMLIEEFGL-HKVRTNQGN----RLSGGERRRVEIARCLAIDPKFIMLDE 181
Cdd:COG4615 424 LDGEA-------------DPARARELLERLELdHKVSVEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-245 |
9.20e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.74 E-value: 9.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVP-NGGKIYLneqditklpvyqraRLGIGYLAQEASVFRKlS 113
Cdd:PLN03130 630 RPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVI--------------RGTVAYVPQVSWIFNA-T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIkavLEMTPLTPdqqrERLEMLIEEFGLHKV--------RTNQGNR---LSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PLN03130 695 VRDNI---LFGSPFDP----ERYERAIDVTALQHDldllpggdLTEIGERgvnISGGQKQRVSMARAVYSNSDVYIFDDP 767
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490460070 183 FAGVDP-IAVQDIQSIVAKLKQRNIGILITdhNVNETLSITDRAYLLFEGKVLFQGTAEQLAEN 245
Cdd:PLN03130 768 LSALDAhVGRQVFDKCIKDELRGKTRVLVT--NQLHFLSQVDRIILVHEGMIKEEGTYEELSNN 829
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
2-212 |
1.19e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 49.24 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 2 TDTIDTAEALSPDrhkgeTGLLRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGlVVPNGgkiYL 81
Cdd:PRK10938 245 PDEPSARHALPAN-----EPRIVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG-DHPQG---YS 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 82 NEqditkLPVYQRARlG-----------IGY----LAQEASVfrKLSVEDNI-----------KAVlemtpltPDQQRER 135
Cdd:PRK10938 316 ND-----LTLFGRRR-GsgetiwdikkhIGYvsssLHLDYRV--STSVRNVIlsgffdsigiyQAV-------SDRQQKL 380
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 136 LEMLIEEFGLHKVRTNQGNR-LSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQdiqsivakLKQRNIGILITD 212
Cdd:PRK10938 381 AQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQ--------LVRRFVDVLISE 450
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
35-182 |
2.10e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.58 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEqDITklpvyqrarlgIGYLAQEASVFRKLSV 114
Cdd:PRK11819 20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPAP-GIK-----------VGYLPQEPQLDPEKTV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 115 EDNIK-AVLEMTPL------------TPDQQRE-------RLEMLIEEFGLHKV-----------RTNQG----NRLSGG 159
Cdd:PRK11819 88 RENVEeGVAEVKAAldrfneiyaayaEPDADFDalaaeqgELQEIIDAADAWDLdsqleiamdalRCPPWdakvTKLSGG 167
|
170 180
....*....|....*....|...
gi 490460070 160 ERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PRK11819 168 ERRRVALCRLLLEKPDMLLLDEP 190
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
2-198 |
2.30e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 48.62 E-value: 2.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 2 TDTIDTAEALSPDRHKGETGLLRTEHLVKRYRS--RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKI 79
Cdd:PTZ00243 1288 TVVIEPASPTSAAPHPVQAGSLVFEGVQMRYREglPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEI 1367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 80 YLNEQDITKLPVYQRARLgIGYLAQEASVFRKlSVEDNIKAVLEMTP------LTPDQQRERLEMliEEFGLHKVRTNQG 153
Cdd:PTZ00243 1368 RVNGREIGAYGLRELRRQ-FSMIPQDPVLFDG-TVRQNVDPFLEASSaevwaaLELVGLRERVAS--ESEGIDSRVLEGG 1443
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 490460070 154 NRLSGGERRRVEIARC-LAIDPKFIMLDEPFAGVDPIAVQDIQSIV 198
Cdd:PTZ00243 1444 SNYSVGQRQLMCMARAlLKKGSGFILMDEATANIDPALDRQIQATV 1489
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-200 |
2.52e-06 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.32 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTF-YMTVGLV--VPNGGKIYLNEQ-----DITKLPVY-----QRARLgigy 101
Cdd:PLN03073 190 RDLIVDASVTLAFGRHYGLVGRNGTGKTTFLrYMAMHAIdgIPKNCQILHVEQevvgdDTTALQCVlntdiERTQL---- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 102 LAQEASVF---RKLSVEDNI--KAVLEMTPLTPDQQRERLEM------LIEEF-----------GLH---KVRTNQGNRL 156
Cdd:PLN03073 266 LEEEAQLVaqqRELEFETETgkGKGANKDGVDKDAVSQRLEEiykrleLIDAYtaearaasilaGLSftpEMQVKATKTF 345
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 490460070 157 SGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAK 200
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLK 389
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
35-182 |
3.27e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 48.02 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNeqdiTKLPVyqrarlgiGYLAQ-EASVFRKLS 113
Cdd:PRK11147 332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCG----TKLEV--------AYFDQhRAELDPEKT 399
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 114 VEDNIkAVLEMTPLTPDQQRERLEMLiEEFGLHKVRTNQGNR-LSGGERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PRK11147 400 VMDNL-AEGKQEVMVNGRPRHVLGYL-QDFLFHPKRAMTPVKaLSGGERNRLLLARLFLKPSNLLILDEP 467
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
23-182 |
5.27e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 5.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 23 LRTEHLVKRYRSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQditklpvyqrARlgIGYL 102
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSEN----------AN--IGYY 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 103 AQE-ASVFrklsveDNIKAVLE-----MTPLTPDQQ-RERLEMLIeeFGLHKVRTNQGNrLSGGERRRVEIARCLAIDPK 175
Cdd:PRK15064 388 AQDhAYDF------ENDLTLFDwmsqwRQEGDDEQAvRGTLGRLL--FSQDDIKKSVKV-LSGGEKGRMLFGKLMMQKPN 458
|
....*..
gi 490460070 176 FIMLDEP 182
Cdd:PRK15064 459 VLVMDEP 465
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
38-217 |
6.65e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 38 VNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQditklpvyqrarlgIGYLAQEASVFRKLSVEDN 117
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE--------------VSVIAISAGLSGQLTGIEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 118 IKAVLEMTPLTPDQQRERLEMLIE-----EFGLHKVRtnqgnRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQ 192
Cdd:PRK13546 106 IEFKMLCMGFKRKEIKAMTPKIIEfselgEFIYQPVK-----KYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180
|
170 180
....*....|....*....|....*
gi 490460070 193 DIQSIVAKLKQRNIGILITDHNVNE 217
Cdd:PRK13546 181 KCLDKIYEFKEQNKTIFFVSHNLGQ 205
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
35-213 |
9.40e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.29 E-value: 9.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 35 RTVVNDVSIELRQGeIVGLLGPNGAGKTTT----FYMTVGLVVPNGGKIYLNEQDITKlpvyqRARLGIGYLAQEASVFR 110
Cdd:cd03240 10 RSFHERSEIEFFSP-LTLIVGQNGAGKTTIiealKYALTGELPPNSKGGAHDPKLIRE-----GEVRAQVKLAFENANGK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 111 KLSVEDNIkAVLEMTPLTPdqQRERLEMLIEEFGlhkvrtnqgnRLSGGERR------RVEIARCLAIDPKFIMLDEPFA 184
Cdd:cd03240 84 KYTITRSL-AILENVIFCH--QGESNWPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTT 150
|
170 180 190
....*....|....*....|....*....|.
gi 490460070 185 GVDP--IAVQDIQSIVAKLKQRNIGILITDH 213
Cdd:cd03240 151 NLDEenIEESLAEIIEERKSQKNFQLIVITH 181
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
104-228 |
1.26e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.36 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 104 QEASVFRK---LSVEDNikavlEMTPLTPDQQrERLEmLIEEFGLHKVRTNQ-GNRLSGGERRRVEIARCLAIDPKFI-- 177
Cdd:PRK00635 1339 QEDVTFLKkflLTIHDD-----EEPSIIQDLL-NRLT-FIDKVGLSYITLGQeQDTLSDGEHYRLHLAKKISSNLTDIiy 1411
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 490460070 178 MLDEPFAGVDPiavQDIQSIVAKLKQrnigiLITDHNvneTLSITDRAYLL 228
Cdd:PRK00635 1412 LLEDPLSGLHP---QDAPTLLQLIKE-----LVTNNN---TVIATDRSGSL 1451
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
37-210 |
1.32e-05 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.18 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 37 VVNDVSIELRQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLNEQDITKLPVYQRARLGIGYLAQEASVFRKlSVED 116
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLKWWRSKIGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 117 NIKAVL--------------EMTPLTPDQQRER----------LEMLIEEF---GLHKVRTN------------------ 151
Cdd:PTZ00265 479 NIKYSLyslkdlealsnyynEDGNDSQENKNKRnscrakcagdLNDMSNTTdsnELIEMRKNyqtikdsevvdvskkvli 558
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 490460070 152 -----------------QGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVAKLK--QRNIGILI 210
Cdd:PTZ00265 559 hdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKgnENRITIII 636
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
51-238 |
1.95e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 45.62 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 51 VGLLGPNGAGKTTTFYMTVGLVVPNGGKiylneqditklpVYQRARLGIGYLAQEASVFRKLSVedniKAVLEMTPLTPD 130
Cdd:PLN03073 538 IAMVGPNGIGKSTILKLISGELQPSSGT------------VFRSAKVRMAVFSQHHVDGLDLSS----NPLLYMMRCFPG 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 131 QQRERLEMLIEEFGLhkvrtnQGN-------RLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQD-IQSIVakLK 202
Cdd:PLN03073 602 VPEQKLRAHLGSFGV------TGNlalqpmyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEAlIQGLV--LF 673
|
170 180 190
....*....|....*....|....*....|....*..
gi 490460070 203 QRniGILITDHNVNETLSITDRAYLLFEGKVL-FQGT 238
Cdd:PLN03073 674 QG--GVLMVSHDEHLISGSVDELWVVSEGKVTpFHGT 708
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
33-247 |
4.28e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 44.77 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 33 RSRTVVNDVSIELRQGEIVGLLGPNGAGKTTTFymtvglvvpnggKIYLNEQDITKLPVYqrARLGIGYLAQEASVFRKl 112
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLL------------QSLLSQFEISEGRVW--AERSIAYVPQQAWIMNA- 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 113 SVEDNIkavlemtpLTPDQQRE----------RLEMLIEEF--GLHKVRTNQGNRLSGGERRRVEIARCLAIDPKFIMLD 180
Cdd:PTZ00243 736 TVRGNI--------LFFDEEDAarladavrvsQLEADLAQLggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLD 807
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490460070 181 EPFAGVDP----IAVQDIqsIVAKL--KQRnigILITdHNVNeTLSITDRAYLLFEGKVLFQGTAEQLAENAL 247
Cdd:PTZ00243 808 DPLSALDAhvgeRVVEEC--FLGALagKTR---VLAT-HQVH-VVPRADYVVALGDGRVEFSGSSADFMRTSL 873
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
136-237 |
1.28e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.54 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 136 LEMLIEeFGLHKVRTNQG-NRLSGGERRRVEIARCLAIDPK--FIMLDEPFAGVDPIAVQDIQSIVAKLKQRNIGILITD 212
Cdd:cd03238 68 LQFLID-VGLGYLTLGQKlSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIE 146
|
90 100 110
....*....|....*....|....*....|...
gi 490460070 213 HNVnETLSITDraYLLF--------EGKVLFQG 237
Cdd:cd03238 147 HNL-DVLSSAD--WIIDfgpgsgksGGKVVFSG 176
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
40-182 |
1.77e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 42.63 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 40 DVSIElrQGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLnEQD--ITKLP----------VYQRARLGIGYLAQEAS 107
Cdd:PRK11147 23 ELHIE--DNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIY-EQDliVARLQqdpprnvegtVYDFVAEGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 108 VFRKLSV-----------------------------EDNIKAVLEMTPLTPDQQRerlemlieefglhkvrtnqgNRLSG 158
Cdd:PRK11147 100 RYHDISHlvetdpseknlnelaklqeqldhhnlwqlENRINEVLAQLGLDPDAAL--------------------SSLSG 159
|
170 180
....*....|....*....|....
gi 490460070 159 GERRRVEIARCLAIDPKFIMLDEP 182
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEP 183
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
155-219 |
1.08e-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: 38.88 E-value: 1.08e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490460070 155 RLSGGERRRVEIARCLAI-----DPkFIMLDEPFAGVDPiavQDIQSIVAK----LKQRNIGILIT-DHNVNETL 219
Cdd:cd03227 77 QLSGGEKELSALALILALaslkpRP-LYILDEIDRGLDP---RDGQALAEAilehLVKGAQVIVIThLPELAELA 147
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
47-227 |
4.82e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 36.58 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 47 QGEIVGLLGPNGAGKTTTFYMTVGLVVPNGGKIYLneqditklpvyqrarlgigylaqeasvfrklsvednikavlemtp 126
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--------------------------------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490460070 127 LTPDQQRERLEMLIEEFGLHKvrtnQGNRLSGGERRRVEIARCLAIDPKFIMLDEPFAGVDPIAVQDIQSIVA------K 200
Cdd:smart00382 36 IDGEDILEEVLDQLLLIIVGG----KKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEElrllllL 111
|
170 180
....*....|....*....|....*..
gi 490460070 201 LKQRNIGILITDHNVNETLSITDRAYL 227
Cdd:smart00382 112 KSEKNLTVILTTNDEKDLGPALLRRRF 138
|
|
| |
