|
Name |
Accession |
Description |
Interval |
E-value |
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
6-249 |
2.53e-121 |
|
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: 346.64 E-value: 2.53e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVR 85
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIAR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAEGSSY-----SFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:COG0411 84 TFQNPRLFPELTVLENVLVAAHARLGRGLlaallRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 161 ATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:COG0411 164 ARALATEPKLLLLDEPAAGLNPEETEELAELIRRlrDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRAD 243
|
250
....*....|.
gi 504233768 239 PRVREVYMGSD 249
Cdd:COG0411 244 PRVIEAYLGEE 254
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
7-241 |
3.36e-113 |
|
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: 325.16 E-value: 3.36e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRS 86
Cdd:cd03219 1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03219 81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRV 241
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRElRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-247 |
9.32e-80 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 240.79 E-value: 9.32e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVR 85
Cdd:COG4674 10 ILYVEDLTVSFDGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLGIGR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALqtaeGSSYSFWKSgnSLHKLN----ERCMELLESVGLAEFANTTTVELAYGRKRALELA 161
Cdd:COG4674 90 KFQKPTVFEELTVFENLELAL----KGDRGVFAS--LFARLTaeerDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 162 TTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRV 241
Cdd:COG4674 164 MLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKVTVLHQGSVLAEGSLDEVQADPRV 243
|
....*.
gi 504233768 242 REVYMG 247
Cdd:COG4674 244 IEVYLG 249
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-249 |
1.06e-63 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 200.22 E-value: 1.06e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 2 SEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK 81
Cdd:PRK11300 1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 GIVRSFQISAVFPHMTALENIRVALQTAEGSSY--------SFWKS-GNSLhklnERCMELLESVGLAEFANTTTVELAY 152
Cdd:PRK11300 81 GVVRTFQHVRLFREMTVIENLLVAQHQQLKTGLfsgllktpAFRRAeSEAL----DRAATWLERVGLLEHANRQAGNLAY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 153 GRKRALELATTLAMEPQLLLLDEPTQGMG---SEDVDRVVELVRKaAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTE 229
Cdd:PRK11300 157 GQQRRLEIARCMVTQPEILMLDEPAAGLNpkeTKELDELIAELRN-EHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLAN 235
|
250 260
....*....|....*....|
gi 504233768 230 GDYQTVSADPRVREVYMGSD 249
Cdd:PRK11300 236 GTPEEIRNNPDVIKAYLGEA 255
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-231 |
1.78e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 193.74 E-value: 1.78e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVrs 86
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVAlqtaeGSSYsfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:COG1131 79 PQEPALYPDLTVRENLRFF-----ARLY-----GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:COG1131 149 DPELLILDEPTSGLDPEARRELWELLRElAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGT 214
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
6-237 |
1.51e-56 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 181.21 E-value: 1.51e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplKSAAIARKGIVR 85
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR--KEPREARRQIGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRvalqtaegssYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:COG4555 79 LPDERGLYDRLTVRENIR----------YFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 166 MEPQLLLLDEPTQGMgseDVD---RVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:COG4555 149 HDPKVLLLDEPTNGL---DVMarrLLREILRAlKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELRE 221
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
6-249 |
4.06e-53 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 172.52 E-value: 4.06e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIvr 85
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLGI-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SF--QISAVFPHMTALENIRVALQTAEgssysfwksgNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATT 163
Cdd:COG1137 81 GYlpQEASIFRKLTVEDNILAVLELRK----------LSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 164 LAMEPQLLLLDEPTQGMgseD---VDRVVELVRK-AAQGRTVLMVEHN----LSVvsklCDRITVLAQGAVLTEGDYQTV 235
Cdd:COG1137 151 LATNPKFILLDEPFAGV---DpiaVADIQKIIRHlKERGIGVLITDHNvretLGI----CDRAYIISEGKVLAEGTPEEI 223
|
250
....*....|....
gi 504233768 236 SADPRVREVYMGSD 249
Cdd:COG1137 224 LNNPLVRKVYLGED 237
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-224 |
2.42e-48 |
|
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: 157.94 E-value: 2.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVrs 86
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRvalqtaegssYSfwksgnslhklnercmellesvglaefantttvelaYGRKRALELATTLAM 166
Cdd:cd03230 79 PEEPSLYENLTVRENLK----------LS------------------------------------GGMKQRLALAQALLH 112
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:cd03230 113 DPELLILDEPTSGLDPESRREFWELLRElKKEGKTILLSSHILEEAERLCDRVAILNNG 171
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
6-249 |
2.69e-48 |
|
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: 160.13 E-value: 2.69e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVR 85
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAEGSSYSfwksgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMAVLEIRKDLDRA---------EREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 166 MEPQLLLLDEPTQG---MGSEDVDRVVELVRkaAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVR 242
Cdd:TIGR04406 152 TNPKFILLDEPFAGvdpIAVGDIKKIIKHLK--ERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVR 229
|
....*..
gi 504233768 243 EVYMGSD 249
Cdd:TIGR04406 230 RVYLGEQ 236
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-243 |
2.70e-48 |
|
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: 159.97 E-value: 2.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSA---AIARK-G 82
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyRLRRRmG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVrsFQISAVFPHMTALENIRVALQTaegssysfwKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELAT 162
Cdd:cd03261 81 ML--FQSGALFDSLTVFENVAFPLRE---------HTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALAR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVR--KAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTV--SAD 238
Cdd:cd03261 150 ALALDPELLLYDEPTAGLDPIASGVIDDLIRslKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELraSDD 229
|
....*
gi 504233768 239 PRVRE 243
Cdd:cd03261 230 PLVRQ 234
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-247 |
4.09e-48 |
|
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: 159.25 E-value: 4.09e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRS 86
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQTAeGSSYSFWKsgnslHKLNercmELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03218 81 PQEASIFRKLTVEENILAVLEIR-GLSKKERE-----EKLE----ELLEEFHITHLRKSKASSLSGGERRRVEIARALAT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVREVY 245
Cdd:cd03218 151 NPKFLLLDEPFAGVDPIAVQDIQKIIKIlKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRKVY 230
|
..
gi 504233768 246 MG 247
Cdd:cd03218 231 LG 232
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
7-243 |
4.29e-47 |
|
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: 156.72 E-value: 4.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEF-KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIV 84
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKvGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 rsFQisavFP-----HMT-------ALENIRVALQTAEgssysfwksgnslhklnERCMELLESVGLAEFANTTTVELAY 152
Cdd:COG1122 81 --FQ----NPddqlfAPTveedvafGPENLGLPREEIR-----------------ERVEEALELVGLEHLADRPPHELSG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 153 GRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:COG1122 138 GQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRlNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGT 217
|
250
....*....|..
gi 504233768 232 YQTVSADPRVRE 243
Cdd:COG1122 218 PREVFSDYELLE 229
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
6-247 |
1.97e-46 |
|
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: 155.14 E-value: 1.97e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVR 85
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAegssysfwKSGNSLHKLNERCMELLESvgLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:COG0410 83 VPEGRRIFPSLTVEENLLLGAYAR--------RDRAEVRADLERVYELFPR--LKERRRQRAGTLSGGEQQMLAIGRALM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 166 MEPQLLLLDEPTQG----MgsedVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:COG0410 153 SRPKLLLLDEPSLGlaplI----VEEIFEIIRRlNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
|
....*..
gi 504233768 241 VREVYMG 247
Cdd:COG0410 229 VREAYLG 235
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
2-243 |
8.63e-46 |
|
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: 153.60 E-value: 8.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 2 SEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSA---AI 78
Cdd:COG1127 1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 79 ARK-GIVrsFQISAVFPHMTALENIRVALQtaEGSSYSfwksgnsLHKLNERCMELLESVGLAEFANTTTVELAYG-RKR 156
Cdd:COG1127 81 RRRiGML--FQGGALFDSLTVFENVAFPLR--EHTDLS-------EAEIRELVLEKLELVGLPGAADKMPSELSGGmRKR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 157 AlELATTLAMEPQLLLLDEPTQGMgseD---VDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:COG1127 150 V-ALARALALDPEILLYDEPTAGL---DpitSAVIDELIRElrDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGT 225
|
250
....*....|....
gi 504233768 232 YQTV--SADPRVRE 243
Cdd:COG1127 226 PEELlaSDDPWVRQ 239
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-245 |
2.77e-45 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 152.55 E-value: 2.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITpLKSAAIA- 79
Cdd:COG1121 1 MMMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR-RARRRIGy 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 ---RKGIVRSFQIsavfphmTALENIRVALQTAEGssysFWKSGNSLHKlnERCMELLESVGLAEFANTTTVELAYG-RK 155
Cdd:COG1121 80 vpqRAEVDWDFPI-------TVRDVVLMGRYGRRG----LFRRPSRADR--EAVDEALERVGLEDLADRPIGELSGGqQQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 156 RALeLATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGaVLTEGDYQT 234
Cdd:COG1121 147 RVL-LARALAQDPDLLLLDEPFAGVDAATEEALYELLRElRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEE 224
|
250
....*....|.
gi 504233768 235 VSADPRVREVY 245
Cdd:COG1121 225 VLTPENLSRAY 235
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
7-233 |
3.45e-45 |
|
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.
Pssm-ID: 213230 [Multi-domain] Cd Length: 220 Bit Score: 151.50 E-value: 3.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKG--FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIV 84
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 rsFQISAVFPHMTALENIRValqtaegssYSFWKsGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTL 164
Cdd:cd03263 81 --PQFDALFDELTVREHLRF---------YARLK-GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIAL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQ 233
Cdd:cd03263 149 IGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQ 217
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
7-238 |
4.71e-45 |
|
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: 151.05 E-value: 4.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRS 86
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAGIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQTAEGSSYSfwksgnslhklnercmELLESV-----GLAEFANTTTVELAYGRKRALELA 161
Cdd:cd03224 81 PEGRRIFPELTVEENLLLGAYARRRAKRK----------------ARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 162 TTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRElRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-230 |
6.79e-45 |
|
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213232 [Multi-domain] Cd Length: 220 Bit Score: 150.60 E-value: 6.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDItpLKSAAIARKGIVRS 86
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV--VREPREVRRRIGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRValqtaEGSSYsfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03265 79 FQDLSVDDELTGWENLYI-----HARLY-----GVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVH 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03265 149 RPEVLFLDEPTIGLDPQTRAHVWEYIEKlkEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-240 |
1.47e-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: 156.99 E-value: 1.47e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF-----KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIAR 80
Cdd:COG1123 260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 K----GIVrsFQ--ISAVFPHMTALENIRVALQTAEGSSYSfwksgnslhKLNERCMELLESVGL-AEFANTTTVELAYG 153
Cdd:COG1123 340 LrrrvQMV--FQdpYSSLNPRMTVGDIIAEPLRLHGLLSRA---------ERRERVAELLERVGLpPDLADRYPHELSGG 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 154 -RKRALeLATTLAMEPQLLLLDEPTQGMgseDV---DRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVL 227
Cdd:COG1123 409 qRQRVA-IARALALEPKLLILDEPTSAL---DVsvqAQILNLLRDLQRelGLTYLFISHDLAVVRYIADRVAVMYDGRIV 484
|
250
....*....|...
gi 504233768 228 TEGDYQTVSADPR 240
Cdd:COG1123 485 EDGPTEEVFANPQ 497
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-238 |
7.58e-44 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 154.79 E-value: 7.58e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 3 EQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKG 82
Cdd:COG1129 1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVRSFQISAVFPHMTALENIRVALQTAEGSSYSfWKsgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRALELAT 162
Cdd:COG1129 81 IAIIHQELNLVPNLSVAENIFLGREPRRGGLID-WR------AMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIAR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:COG1129 154 ALSRDARVLILDEPTASLTEREVERLFRIIRRlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTED 230
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-226 |
2.32e-43 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 146.52 E-value: 2.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTV---FNLLTKfliPTRGQILYRGEDIT-PLKSAAIARKG 82
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTIIIDGLKLTdDKKNINELRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVRSFQISAVFPHMTALENIRVALQTAEGSSYSfwksgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRALELAT 162
Cdd:cd03262 78 VGMVFQQFNLFPHLTVLENITLAPIKVKGMSKA---------EAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:cd03262 149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEeGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
21-224 |
1.80e-42 |
|
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: 144.15 E-value: 1.80e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVrsFQisavFP-HM-- 96
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKvGLV--FQ----NPdDQff 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 97 --TALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLD 174
Cdd:cd03225 90 gpTVEEEVAFGLENL----------GLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504233768 175 EPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:cd03225 160 EPTAGLDPAGRRELLELLKKlKAEGKTIIIVTHDLDLLLELADRVIVLEDG 210
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
7-227 |
2.14e-42 |
|
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: 143.81 E-value: 2.14e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLksaAIARKGIVRS 86
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV---PPERRNIGMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQtaegssysfwKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03259 78 FQDYALFPHLTVAENIAFGLK----------LRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 167 EPQLLLLDEPtqgMGSEDV---DRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVL 227
Cdd:cd03259 148 EPSLLLLDEP---LSALDAklrEELREELKElqRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-230 |
3.52e-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: 143.13 E-value: 3.52e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAiARKGIVRS 86
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL-RRIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQisAVFPHMTALENIRValqtaegssysfwkSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03268 80 AP--GFYPNLTARENLRL--------------LARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLG 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03268 144 NPDLLILDEPTNGLDPDGIKELRELILSlRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-221 |
4.51e-42 |
|
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: 143.38 E-value: 4.51e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKG----FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKsaaiARKG 82
Cdd:cd03293 1 LEVRNVSKTYGGgggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG----PDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVrsFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYG-RKRAlELA 161
Cdd:cd03293 77 YV--FQQDALLPWLTVLDNVALGLELQ----------GVPKAEARERAEELLELVGLSGFENAYPHQLSGGmRQRV-ALA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 162 TTLAMEPQLLLLDEP-------T-QGMGSEdvdrVVELVRKaaQGRTVLMVEHNLSVVSKLCDRITVL 221
Cdd:cd03293 144 RALAVDPDVLLLDEPfsaldalTrEQLQEE----LLDIWRE--TGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
7-224 |
5.66e-42 |
|
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: 141.94 E-value: 5.66e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK---GI 83
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRrriGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 84 VrsFQISAVFPHMTALENIRVALqtaegssysfwkSGnslhklnercmellesvglaefantttvelayGRKRALELATT 163
Cdd:cd03229 81 V--FQDFALFPHLTVLENIALGL------------SG--------------------------------GQQQRVALARA 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 164 LAMEPQLLLLDEPTQGMGSEDVDRVVELVR--KAAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:cd03229 115 LAMDPDVLLLDEPTSALDPITRREVRALLKslQAQLGITVVLVTHDLDEAARLADRVVVLRDG 177
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-245 |
1.08e-41 |
|
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: 143.26 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIV 84
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRiAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 rsFQISAVFPHMTALENirVAL-QTAEGSSYSFWKsgnslHKLNERCMELLESVGLAEFANTTTVELAYG-RKRALeLAT 162
Cdd:COG1120 81 --PQEPPAPFGLTVREL--VALgRYPHLGLFGRPS-----AEDREAVEEALERTGLEHLADRPVDELSGGeRQRVL-IAR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 163 TLAMEPQLLLLDEPTQGMgseDVD---RVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:COG1120 151 ALAQEPPLLLLDEPTSHL---DLAhqlEVLELLRRlaRERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
|
....*...
gi 504233768 238 DPRVREVY 245
Cdd:COG1120 228 PELLEEVY 235
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-245 |
1.17e-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: 1.17e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFK-GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAI--ARKGI 83
Cdd:cd03256 1 IEVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALrqLRRQI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 84 VRSFQISAVFPHMTALENIRVALQtaegSSYSFWKSGNSLHKLNE--RCMELLESVGLAEFANTTTVELAYGRKRALELA 161
Cdd:cd03256 81 GMIFQQFNLIERLSVLENVLSGRL----GRRSTWRSLFGLFPKEEkqRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 162 TTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSaDP 239
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINReeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELT-DE 235
|
....*.
gi 504233768 240 RVREVY 245
Cdd:cd03256 236 VLDEIY 241
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-253 |
5.45e-41 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 142.94 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIA-----R 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGylpeeR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 kGIvrsfqisavFPHMTALENIR--VALQtaegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRAL 158
Cdd:COG4152 81 -GL---------YPKMKVGEQLVylARLK------------GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 159 ELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVR-KAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIReLAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRR 218
|
250
....*....|....*.
gi 504233768 238 DPRVREVYMGSDGSGE 253
Cdd:COG4152 219 QFGRNTLRLEADGDAG 234
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
8-226 |
1.51e-40 |
|
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: 139.21 E-value: 1.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSaaiaRKGIV-RS 86
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERK----RIGYVpQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPhMTALENIRVALQtaegSSYSFWKSGNSLHKlnERCMELLESVGLAEFANTTTVELAYG-RKRALeLATTLA 165
Cdd:cd03235 77 RSIDRDFP-ISVRDVVLMGLY----GHKGLFRRLSKADK--AKVDEALERVGLSELADRQIGELSGGqQQRVL-LARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:cd03235 149 QDPDLLLLDEPFAGVDPKTQEDIYELLRElRREGMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
6-224 |
2.77e-40 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 139.84 E-value: 2.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF----KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKsaaiARK 81
Cdd:COG1116 7 ALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG----PDR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 GIVrsFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANtttvelAY------G-R 154
Cdd:COG1116 83 GVV--FQEPALLPWLTVLDNVALGLELR----------GVPKAERRERARELLELVGLAGFED------AYphqlsgGmR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 155 KRAlELATTLAMEPQLLLLDEPtqgMGSEDV-------DRVVELVRKaaQGRTVLMVEHNLS--VVskLCDRITVLAQG 224
Cdd:COG1116 145 QRV-AIARALANDPEVLLMDEP---FGALDAltrerlqDELLRLWQE--TGKTVLFVTHDVDeaVF--LADRVVVLSAR 215
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-240 |
3.75e-40 |
|
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: 138.87 E-value: 3.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKG----FVAVNDVNLQIRQGDIHALIGPNGAGKTTV---FNLLTKfliPTRGQILYRGEDITPLKSAAI 78
Cdd:cd03258 1 MIELKNVSKVFGDtggkVTALKDVSLSVPKGEIFGIIGRSGAGKSTLircINGLER---PTSGSVLVDGTDLTLLSGKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 79 --ARKGIVRSFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKR 156
Cdd:cd03258 78 rkARRRIGMIFQHFNLLSSRTVFENVALPLEIA----------GVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 157 ALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQT 234
Cdd:cd03258 148 RVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRelGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEE 227
|
....*.
gi 504233768 235 VSADPR 240
Cdd:cd03258 228 VFANPQ 233
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-240 |
4.71e-40 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 138.59 E-value: 4.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTV---FNLLTKfliPTRGQILYRGEDITPLKS--AAIAR 80
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLlrcINLLEE---PDSGTITVDGEDLTDSKKdiNKLRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 K-GIVrsFQISAVFPHMTALENIRVALQTAEGSSYSfwksgnslhKLNERCMELLESVGLAEFANtttvelAY------G 153
Cdd:COG1126 78 KvGMV--FQQFNLFPHLTVLENVTLAPIKVKKMSKA---------EAEERAMELLERVGLADKAD------AYpaqlsgG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 154 RK------RALelattlAMEPQLLLLDEPTqgmgS----EDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLA 222
Cdd:COG1126 141 QQqrvaiaRAL------AMEPKVMLFDEPT----SaldpELVGEVLDVMRDlAKEGMTMVVVTHEMGFAREVADRVVFMD 210
|
250
....*....|....*...
gi 504233768 223 QGAVLTEGDYQTVSADPR 240
Cdd:COG1126 211 GGRIVEEGPPEEFFENPQ 228
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-230 |
5.42e-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: 5.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKG----FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSA--AIA 79
Cdd:cd03257 1 LLEVKNLSVSFPTgggsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrKIR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 RKGIVRSFQ--ISAVFPHMTALENIRVALQtaegssysFWKSGNSLHKLNERCMELLESVGLAE-FANTTTVELAYG-RK 155
Cdd:cd03257 81 RKEIQMVFQdpMSSLNPRMTIGEQIAEPLR--------IHGKLSKKEARKEAVLLLLVGVGLPEeVLNRYPHELSGGqRQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 156 RALeLATTLAMEPQLLLLDEPTQGMgseDV---DRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03257 153 RVA-IARALALNPKLLIADEPTSAL---DVsvqAQILDLLKKLQEelGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
7-226 |
1.17e-39 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 137.37 E-value: 1.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLksaAIARKGIVRS 86
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL---PPHKRPVNTV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03300 78 FQNYALFPHLTVFENIAFGLRLK----------KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVN 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 167 EPQLLLLDEPtqgMGSEDV----DRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:cd03300 148 EPKVLLLDEP---LGALDLklrkDMQLELKRLQKElGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-226 |
1.33e-39 |
|
ATP-binding cassette domain of the transporters involved in export of lipoprotein and macrolide, and Cell division ATP-binding protein FtsE; This family is comprised of MJ0796 ATP-binding cassette, macrolide-specific ABC-type efflux carrier (MacAB), and proteins involved in cell division (FtsE), and release of lipoproteins from the cytoplasmic membrane (LolCDE). They are clustered together phylogenetically. MacAB is an exporter that confers resistance to macrolides, while the LolCDE system is not a transporter at all. The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages. The LolCDE complex catalyzes the release of lipoproteins from the cytoplasmic membrane prior to their targeting to the outer membrane.
Pssm-ID: 213222 [Multi-domain] Cd Length: 218 Bit Score: 136.85 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKG----FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK- 81
Cdd:cd03255 1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 ----GIVrsFQISAVFPHMTALENIRVALQtaegssysfwKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRA 157
Cdd:cd03255 81 rrhiGFV--FQSFNLLPDLTALENVELPLL----------LAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQR 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSkLCDRITVLAQGAV 226
Cdd:cd03255 149 VAIARALANDPKIILADEPTGNLDSETGKEVMELLRElnKEAGTTIVVVTHDPELAE-YADRIIELRDGKI 218
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
10-226 |
2.29e-39 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 136.34 E-value: 2.29e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 10 RNLVKEFK-GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIA---RK-GIV 84
Cdd:COG2884 5 ENVSKRYPgGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPylrRRiGVV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 rsFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTL 164
Cdd:COG2884 85 --FQDFRLLPDRTVYENVALPLRVT----------GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRKA-AQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:COG2884 153 VNRPELLLADEPTGNLDPETSWEIMELLEEInRRGTTVLIATHDLELVDRMPKRVLELEDGRL 215
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-245 |
1.18e-38 |
|
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: 135.16 E-value: 1.18e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKsaaIARKGIVRS 86
Cdd:cd03296 3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP---VQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQTAEGSSYSfwksgnSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03296 80 FQHYALFRHMTVFDNVAFGLRVKPRSERP------PEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 167 EPQLLLLDEPtqgMGSEDVDRVVELVRKAAQ-----GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRV 241
Cdd:cd03296 154 EPKVLLLDEP---FGALDAKVRKELRRWLRRlhdelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPAS 230
|
....
gi 504233768 242 REVY 245
Cdd:cd03296 231 PFVY 234
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-177 |
9.16e-38 |
|
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: 130.08 E-value: 9.16e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPlKSAAIARKGIVRSFQISAVFPHMTALEN 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD-DERKSLRKEIGYVFQDPQLFPRLTVREN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 102 IRVALQTaegssysfwkSGNSLHKLNERCMELLESVGLAEFANT----TTVELAYGRKRALELATTLAMEPQLLLLDEPT 177
Cdd:pfam00005 80 LRLGLLL----------KGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-230 |
1.47e-37 |
|
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: 131.55 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGdIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRs 86
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 fQISAVFPHMTALENIRvalqtaegssYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03264 79 -QEFGVYPNFTVREFLD----------YIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVG 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03264 148 DPSILIVDEPTAGLDPEERIRFRNLLSELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
7-244 |
1.93e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.84 E-value: 1.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLksAAIARK-GIVr 85
Cdd:COG3842 6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGL--PPEKRNvGMV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 sFQISAVFPHMTALENIRVALQtaegssysfwKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:COG3842 83 -FQDYALFPHLTVAENVAFGLR----------MRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 166 MEPQLLLLDEPtqgMGSEDV---DRVVELVRK--AAQGRTVLMVEHN----LSvvskLCDRITVLAQGAVLTEGDYQTVS 236
Cdd:COG3842 152 PEPRVLLLDEP---LSALDAklrEEMREELRRlqRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTPEEIY 224
|
....*...
gi 504233768 237 ADPRVREV 244
Cdd:COG3842 225 ERPATRFV 232
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-238 |
2.93e-37 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 137.08 E-value: 2.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 2 SEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPlKSAAIARK 81
Cdd:COG3845 1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI-RSPRDAIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 -GIVRSFQISAVFPHMTALENIRVALqtaEGSSYSFWksgnSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:COG3845 80 lGIGMVHQHFMLVPNLTVAENIVLGL---EPTKGGRL----DRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 161 ATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:COG3845 153 LKALYRGARILILDEPTAVLTPQEADELFEILRRlAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEE 231
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
6-242 |
3.64e-37 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 134.96 E-value: 3.64e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDitpLKSAAIARKGIVR 85
Cdd:PRK11607 19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVD---LSHVPPYQRPINM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAEGSSysfwksgnslHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:PRK11607 96 MFQSYALFPHMTVEQNIAFGLKQDKLPK----------AEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 166 MEPQLLLLDEPtqgMGSEDV---DR----VVELVRKAaqGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:PRK11607 166 KRPKLLLLDEP---MGALDKklrDRmqleVVDILERV--GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEH 240
|
....
gi 504233768 239 PRVR 242
Cdd:PRK11607 241 PTTR 244
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
7-240 |
6.56e-37 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 133.28 E-value: 6.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKG----FVAVNDVNLQIRQGDIHALIGPNGAGKTT---VFNLLTKfliPTRGQILYRGEDITPLKSAAI- 78
Cdd:COG1135 2 IELENLSKTFPTkggpVTALDDVSLTIEKGEIFGIIGYSGAGKSTlirCINLLER---PTSGSVLVDGVDLTALSERELr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 79 -ARKGIVRSFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRK-- 155
Cdd:COG1135 79 aARRKIGMIFQHFNLLSSRTVAENVALPLEIA----------GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKqr 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 156 ----RAlelattLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTE 229
Cdd:COG1135 149 vgiaRA------LANNPKVLLCDEATSALDPETTRSILDLLKDINRelGLTIVLITHEMDVVRRICDRVAVLENGRIVEQ 222
|
250
....*....|.
gi 504233768 230 GDYQTVSADPR 240
Cdd:COG1135 223 GPVLDVFANPQ 233
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
7-226 |
1.35e-36 |
|
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: 129.73 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKG-FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIV 84
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKiGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 rsFQISAVFPHMTALENIrVALQTAEGssysfWKSgnslHKLNERCMELLESVGL--AEFANTTTVELAYGRKRALELAT 162
Cdd:cd03295 81 --IQQIGLFPHMTVEENI-ALVPKLLK-----WPK----EKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 163 TLAMEPQLLLLDEPtqgMGSEDV---DRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:cd03295 149 ALAADPPLLLMDEP---FGALDPitrDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
7-226 |
1.35e-36 |
|
First domain of the ATP-binding cassette component of monosaccharide transport system; This family represents the domain I of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. Pentoses include xylose, arabinose, and ribose. Important hexoses include glucose, galactose, and fructose. In members of the Carb_monos family, the single hydrophobic gene product forms a homodimer while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213183 [Multi-domain] Cd Length: 163 Bit Score: 127.54 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRS 86
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAvfphmtalenirvalqtaegssysfwksgnslhklnercmellesvglaefantttvelayGRKRALELATTLAM 166
Cdd:cd03216 81 YQLSV-------------------------------------------------------------GERQMVEIARALAR 99
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:cd03216 100 NARLLILDEPTAALTPAEVERLFKVIRRlRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
6-249 |
3.27e-36 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 128.86 E-value: 3.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVR 85
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRGIGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAEGSSYsfwksgnslHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:PRK10895 83 LPQEASIFRRLSVYDNLMAVLQIRDDLSA---------EQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 166 MEPQLLLLDEPTQG---MGSEDVDRVVELVRKAAQGrtVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVR 242
Cdd:PRK10895 154 ANPKFILLDEPFAGvdpISVIDIKRIIEHLRDSGLG--VLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVK 231
|
....*..
gi 504233768 243 EVYMGSD 249
Cdd:PRK10895 232 RVYLGED 238
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
6-240 |
1.08e-35 |
|
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: 133.10 E-value: 1.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKG--FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKfLIP----TRGQILYRGEDITPLKSAaia 79
Cdd:COG1123 4 LLEVRDLSVRYPGgdVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMG-LLPhggrISGEVLLDGRDLLELSEA--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 rkgiVRSFQISAVFPH-MTALENIRVALQTAEGssysFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRAL 158
Cdd:COG1123 80 ----LRGRRIGMVFQDpMTQLNPVTVGDQIAEA----LENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 159 ELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVS 236
Cdd:COG1123 152 AIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRerGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEIL 231
|
....
gi 504233768 237 ADPR 240
Cdd:COG1123 232 AAPQ 235
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
7-231 |
2.36e-35 |
|
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: 126.14 E-value: 2.36e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTT---VFNLLTKFL--IPTRGQILYRGEDITPLKSAAIA-- 79
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTllrLLNRLNDLIpgAPDEGEVLLDGKDIYDLDVDVLElr 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 -RKGIVrsFQISAVFPhMTALENIRVALqtaegssysfWKSGNSLHK-LNERCMELLESVGLAEFAN--TTTVELAYGRK 155
Cdd:cd03260 81 rRVGMV--FQKPNPFP-GSIYDNVAYGL----------RLHGIKLKEeLDERVEEALRKAALWDEVKdrLHALGLSGGQQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 156 RALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:cd03260 148 QRLCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
1-245 |
5.08e-35 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 128.34 E-value: 5.08e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSeqyvLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDitpLKSAAIAR 80
Cdd:COG1118 1 MS----IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRD---LFTNLPPR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 K---GIVrsFQISAVFPHMTALENIRVALQtaegssysfwKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYG-RKR 156
Cdd:COG1118 74 ErrvGFV--FQHYALFPHMTVAENIAFGLR----------VRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGqRQR 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 157 -AleLATTLAMEPQLLLLDEPtqgMGSEDVDRVVELVRK-----AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:COG1118 142 vA--LARALAVEPEVLLLDEP---FGALDAKVRKELRRWlrrlhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVG 216
|
250
....*....|....*
gi 504233768 231 DYQTVSADPRVREVY 245
Cdd:COG1118 217 TPDEVYDRPATPFVA 231
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
8-224 |
5.66e-35 |
|
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: 123.12 E-value: 5.66e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKGIVRSF 87
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL-RRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 88 QISAvfphmtalenirvalqtaegssysfwksgnslhklnercmellesvglaefantttvelayGRKRALELATTLAME 167
Cdd:cd00267 80 QLSG-------------------------------------------------------------GQRQRVALARALLLN 98
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 168 PQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:cd00267 99 PDLLLLDEPTSGLDPASRERLLELLRElAEEGRTVIIVTHDPELAELAADRVIVLKDG 156
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
8-230 |
1.03e-34 |
|
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: 122.93 E-value: 1.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKgivrsf 87
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 88 qisavfphmtalenIRVALQtaegssysfwksgnslhklnercmeLLESVGLAEFANTTTVELAYG-RKRALeLATTLAM 166
Cdd:cd03214 75 --------------IAYVPQ-------------------------ALELLGLAHLADRPFNELSGGeRQRVL-LARALAQ 114
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 167 EPQLLLLDEPTQGMgseDV---DRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03214 115 EPPILLLDEPTSHL---DIahqIELLELLRRLARerGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
7-244 |
1.36e-34 |
|
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: 124.37 E-value: 1.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVaVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSaaiARKGIVRS 86
Cdd:cd03299 1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP---EKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIrvalqtaegsSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03299 77 PQNYALFPHMTVYKNI----------AYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVREV 244
Cdd:cd03299 147 NPKILLLDEPFSALDVRTKEKLREELKKIRKefGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFV 226
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
6-206 |
1.84e-34 |
|
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: 123.36 E-value: 1.84e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVr 85
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 sFQISAVFPHMTALENIRvalqtaegssysFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:COG4133 81 -GHADGLKPELTVRENLR------------FWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLL 147
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEH 206
Cdd:COG4133 148 SPAPLWLLDEPFTALDAAGVALLAELIAAhLARGGAVLLTTH 189
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
7-230 |
1.25e-33 |
|
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: 121.23 E-value: 1.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIA----RKG 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAARNRIGylpeERG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVRSFQISAVFPHMTALEnirvalqtaegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELAT 162
Cdd:cd03269 81 LYPKMKVIDQLVYLAQLK-------------------GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIA 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03269 142 AVIHDPELLILDEPFSGLDPVNVELLKDVIRElARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
12-249 |
2.46e-33 |
|
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213261 [Multi-domain] Cd Length: 269 Bit Score: 121.98 E-value: 2.46e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 12 LVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAA---IARKGIVRSFQ 88
Cdd:cd03294 30 ILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKElreLRRKKISMVFQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 89 ISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEP 168
Cdd:cd03294 110 SFALLPHRTVLENVAFGLEVQ----------GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 169 QLLLLDEPTQGMG----SEDVDRVVELVRKaaQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTV---SADPRV 241
Cdd:cd03294 180 DILLMDEAFSALDplirREMQDELLRLQAE--LQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEIltnPANDYV 257
|
....*...
gi 504233768 242 REVYMGSD 249
Cdd:cd03294 258 REFFRGVD 265
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
22-245 |
2.66e-33 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 121.76 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVRsfQISAV-FPhMTAL 99
Cdd:COG4559 17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRrAVLP--QHSSLaFP-FTVE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIRVALqtaegSSYSFWKSGNslHKLNERCMELlesVGLAEFANTTTVELAYGRKRALELATTLA-------MEPQLLL 172
Cdd:COG4559 94 EVVALGR-----APHGSSAAQD--RQIVREALAL---VGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPRWLF 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 173 LDEPTQGMgsedvD-----RVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVREVY 245
Cdd:COG4559 164 LDEPTSAL-----DlahqhAVLRLARQlARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-240 |
7.23e-33 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 120.24 E-value: 7.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQIlyRGEDITPLKSAAI-ARKGIVR 85
Cdd:PRK11264 4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGDITIDTARSLsQQKGLIR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 S--------FQISAVFPHMTALENIrvalqtAEGSSYSfwkSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRA 157
Cdd:PRK11264 82 QlrqhvgfvFQNFNLFPHRTVLENI------IEGPVIV---KGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVS 236
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQeKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALF 232
|
....
gi 504233768 237 ADPR 240
Cdd:PRK11264 233 ADPQ 236
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-240 |
7.71e-33 |
|
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: 122.08 E-value: 7.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF---KGFV-AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIP---TRGQILYRGEDITPLKSAAI 78
Cdd:COG0444 1 LLEVRNLKVYFptrRGVVkAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 79 ARkgiVRSFQISAVF--PhMTALeN--IRVALQTAEGSSYSFWKSGNSLHklnERCMELLESVGL---AEFANtttvelA 151
Cdd:COG0444 81 RK---IRGREIQMIFqdP-MTSL-NpvMTVGDQIAEPLRIHGGLSKAEAR---ERAIELLERVGLpdpERRLD------R 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 152 Y------G-RKRALeLATTLAMEPQLLLLDEPTQGMgseDV---DRVVELVR--KAAQGRTVLMVEHNLSVVSKLCDRIT 219
Cdd:COG0444 147 YphelsgGmRQRVM-IARALALEPKLLIADEPTTAL---DVtiqAQILNLLKdlQRELGLAILFITHDLGVVAEIADRVA 222
|
250 260
....*....|....*....|.
gi 504233768 220 VLAQGAVLTEGDYQTVSADPR 240
Cdd:COG0444 223 VMYAGRIVEEGPVEELFENPR 243
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
7-226 |
1.62e-32 |
|
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: 118.66 E-value: 1.62e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEF-KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIA--RKGI 83
Cdd:cd03292 1 IEFINVTKTYpNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 84 VRSFQISAVFPHMTALENIRVALQTaegssysfwkSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATT 163
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEV----------TGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARA 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 164 LAMEPQLLLLDEPTQGMGSEDVDRVVELVRKA-AQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:cd03292 151 IVNSPTILIADEPTGNLDPDTTWEIMNLLKKInKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-242 |
2.06e-32 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 124.13 E-value: 2.06e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVlETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIAR 80
Cdd:PRK09700 1 MATPYI-SMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 KGIVRSFQISAVFPHMTALENI---RVALQTAEGSSYSFWKsgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRA 157
Cdd:PRK09700 80 LGIGIIYQELSVIDELTVLENLyigRHLTKKVCGVNIIDWR------EMRVRAAMMLLRVGLKVDLDEKVANLSISHKQM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVS 236
Cdd:PRK09700 154 LEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQlRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVS 233
|
....*.
gi 504233768 237 ADPRVR 242
Cdd:PRK09700 234 NDDIVR 239
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
7-224 |
2.71e-32 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 117.61 E-value: 2.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLkSAAIARKGIVRS 86
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAM-PPPEWRRQVAYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPhMTALENIRvalqtaegssysFWKSGNSLHKLNERCMELLESVGLAE-FANTTTVELAYGRKRALELATTLA 165
Cdd:COG4619 80 PQEPALWG-GTVRDNLP------------FPFQLRERKFDRERALELLERLGLPPdILDKPVERLSGGERQRLALIRALL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:COG4619 147 LQPDVLLLDEPTSALDPENTRRVEELLREylAEEGRAVLWVSHDPEQIERVADRVLTLEAG 207
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
6-225 |
3.34e-32 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 123.36 E-value: 3.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKfLIPT---RGQILYRGEditPLKSAAIA--- 79
Cdd:NF040905 1 ILEMRGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSG-VYPHgsyEGEILFDGE---VCRFKDIRdse 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 RKGIVRSFQISAVFPHMTALENIRVALQTAEGSSYSfWksgnslHKLNERCMELLESVGLAEFANTTTVELAYGRKRALE 159
Cdd:NF040905 77 ALGIVIIHQELALIPYLSIAENIFLGNERAKRGVID-W------NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVE 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 160 LATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGA 225
Cdd:NF040905 150 IAKALSKDVKLLILDEPTAALNEEDSAALLDLLLElKAQGITSIIISHKLNEIRRVADSITVLRDGR 216
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
7-245 |
4.37e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.58 E-value: 4.37e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARkgivrs 86
Cdd:PRK11231 3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 fQISAVFPHMTALENIRVALQTAEGSS--YSFW-KSGNSLHKLNERCMellESVGLAEFANTTTVELAYG-RKRALeLAT 162
Cdd:PRK11231 77 -RLALLPQHHLTPEGITVRELVAYGRSpwLSLWgRLSAEDNARVNQAM---EQTRINHLADRRLTDLSGGqRQRAF-LAM 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 163 TLAMEPQLLLLDEPTQGMgseDVDRVVELVR----KAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:PRK11231 152 VLAQDTPVVLLDEPTTYL---DINHQVELMRlmreLNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
|
....*..
gi 504233768 239 PRVREVY 245
Cdd:PRK11231 229 GLLRTVF 235
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-243 |
5.58e-32 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 117.89 E-value: 5.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDItpLKSAAIARK---- 81
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV--NDPKVDERLirqe 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 -GIVrsFQISAVFPHMTALEN-----IRValqtaegssysfwkSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRK 155
Cdd:PRK09493 79 aGMV--FQQFYLFPHLTALENvmfgpLRV--------------RGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 156 RALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQT 234
Cdd:PRK09493 143 QRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDlAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
250
....*....|..
gi 504233768 235 VSADP---RVRE 243
Cdd:PRK09493 223 LIKNPpsqRLQE 234
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
3-241 |
7.49e-32 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 118.80 E-value: 7.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 3 EQYVLETRNLVKEFK-GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplksaaIARK 81
Cdd:PRK13636 2 EDYILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID------YSRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 GIVRSFQ-ISAVFphmTALENIRVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:PRK13636 76 GLMKLREsVGMVF---QDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 161 ATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:PRK13636 153 AGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKelGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
|
...
gi 504233768 239 PRV 241
Cdd:PRK13636 233 KEM 235
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
21-237 |
1.18e-31 |
|
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: 123.02 E-value: 1.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARkgivrsfQISAV------Fp 94
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRR-------QIGVVlqdvflF- 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 95 HMTALENIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANT------TTVE-----LAYGRKRALELATT 163
Cdd:COG2274 562 SGTIRENITLGDPDAT----------------DEEIIEAARLAGLHDFIEAlpmgydTVVGeggsnLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 164 LAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVsKLCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:COG2274 626 LLRNPRILILDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLA 698
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
7-230 |
1.72e-31 |
|
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: 115.93 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEF----KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKG 82
Cdd:cd03266 2 ITADALTKRFrdvkKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVrsFQISAVFPHMTALENIRV--ALQTAEGssysfwksgnslHKLNERCMELLESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:cd03266 82 FV--SDSTGLYDRLTARENLEYfaGLYGLKG------------DELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAI 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 161 ATTLAMEPQLLLLDEPTQG---MGSEDVDRVVELVRkaAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03266 148 ARALVHDPPVLLLDEPTTGldvMATRALREFIRQLR--ALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
21-245 |
2.99e-31 |
|
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: 121.41 E-value: 2.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKGIVRSFQISAVFpHMTALE 100
Cdd:COG4987 350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL-RRRIAVVPQRPHLF-DTTLRE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 101 NIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANTTTVELAY-----------GRKRALELATTLAMEPQ 169
Cdd:COG4987 428 NLRLARPDAT----------------DEELWAALERVGLGDWLAALPDGLDTwlgeggrrlsgGERRRLALARALLRDAP 491
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 170 LLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQT-VSADPRVREVY 245
Cdd:COG4987 492 ILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEElLAQNGRYRQLY 567
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
18-237 |
5.85e-31 |
|
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: 120.63 E-value: 5.85e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 18 GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARkgivrsfQISAV----- 92
Cdd:COG4988 349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR-------QIAWVpqnpy 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 93 FPHMTALENIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANT------TTVE-----LAYGRKRALELA 161
Cdd:COG4988 422 LFAGTIRENLRLGRPDAS----------------DEELEAALEAAGLDEFVAAlpdgldTPLGeggrgLSGGQAQRLALA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 162 TTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVsKLCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:COG4988 486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELLA 560
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-224 |
1.77e-30 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 118.49 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEqYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKfLIPT---RGQILYRGEditPLKSAA 77
Cdd:PRK13549 1 MME-YLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGE---ELQASN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 78 IA---RKGIVRSFQISAVFPHMTALENIRVAlqtAEgssysfWKSGNSLH--KLNERCMELLESVGLAEFANTTTVELAY 152
Cdd:PRK13549 76 IRdteRAGIAIIHQELALVKELSVLENIFLG---NE------ITPGGIMDydAMYLRAQKLLAQLKLDINPATPVGNLGL 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 153 GRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDlKAHGIACIYISHKLNEVKAISDTICVIRDG 219
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
17-233 |
2.45e-30 |
|
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: 113.09 E-value: 2.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 17 KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKGIVRSFQISAVFPHm 96
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL-RSMIGVVLQDTFLFSG- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 97 TALENIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANT------TTVE-----LAYGRKRALELATTLA 165
Cdd:cd03254 92 TIMENIRLGRPNAT----------------DEEVIEAAKEAGAHDFIMKlpngydTVLGenggnLSQGERQLLAIARAML 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVsKLCDRITVLAQGAVLTEGDYQ 233
Cdd:cd03254 156 RDPKILILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHD 222
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-247 |
3.55e-30 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 115.59 E-value: 3.55e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplkSAAIAR 80
Cdd:PRK11432 1 MTQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT---HRSIQQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 KGIVRSFQISAVFPHMTALENIrvalqtaegsSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:PRK11432 78 RDICMVFQSYALFPHMSLGENV----------GYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 161 ATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:PRK11432 148 ARALILKPKVLLFDEPLSNLDANLRRSMREKIRELQQqfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
250
....*....|.
gi 504233768 239 PRVREV--YMG 247
Cdd:PRK11432 228 PASRFMasFMG 238
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
6-241 |
6.56e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 113.25 E-value: 6.56e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF-KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAI-ARK-- 81
Cdd:PRK13639 1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLLeVRKtv 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 GIVrsFQISavfphmtalENIRVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELA 161
Cdd:PRK13639 81 GIV--FQNP---------DDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 162 TTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKA-AQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:PRK13639 150 GILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLnKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229
|
.
gi 504233768 241 V 241
Cdd:PRK13639 230 T 230
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
21-224 |
8.98e-30 |
|
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: 109.78 E-value: 8.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVrsFQISAVFpHMTAL 99
Cdd:cd03228 17 VLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNiAYV--PQDPFLF-SGTIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIrvaLqtaegssysfwkSGnslhklnercmellesvglaefantttvelayGRKRALELATTLAMEPQLLLLDEPTQG 179
Cdd:cd03228 94 ENI---L------------SG--------------------------------GQRQRIAIARALLRDPPILILDEATSA 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 504233768 180 MGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVsKLCDRITVLAQG 224
Cdd:cd03228 127 LDPETEALILEALRALAKGKTVIVIAHRLSTI-RDADRIIVLDDG 170
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
7-257 |
1.61e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 114.03 E-value: 1.61e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLkSAAIARKGIVrs 86
Cdd:PRK10851 3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL-HARDRKVGFV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIrvalqtAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:PRK10851 80 FQHYALFRHMTVFDNI------AFGLTVLPRRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 167 EPQLLLLDEPtqgMGSEDVDRVVELVRKAAQGR-----TVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRV 241
Cdd:PRK10851 154 EPQILLLDEP---FGALDAQVRKELRRWLRQLHeelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPAT 230
|
250 260
....*....|....*....|.
gi 504233768 242 REV--YMGSDG--SGE-RGSQ 257
Cdd:PRK10851 231 RFVleFMGEVNrlQGTiRGGQ 251
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
8-240 |
1.65e-29 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 113.74 E-value: 1.65e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEF----KGFVAVNDVNLQIRQGDIHALIGPNGAGKTT---VFNLLTKfliPTRGQILYRGEDITPLKSAAI-- 78
Cdd:PRK11153 3 ELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTlirCINLLER---PTSGRVLVDGQDLTALSEKELrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 79 ARKgivrsfQISAVFPHM------TALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAY 152
Cdd:PRK11153 80 ARR------QIGMIFQHFnllssrTVFDNVALPLELA----------GTPKAEIKARVTELLELVGLSDKADRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 153 GRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRelGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
250
....*....|
gi 504233768 231 DYQTVSADPR 240
Cdd:PRK11153 224 TVSEVFSHPK 233
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
6-245 |
4.30e-29 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 110.63 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVR 85
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPhMTALENIRVALQTaegssysfWksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:PRK13548 82 PQHSSLSFP-FTVEEVVAMGRAP--------H--GLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 166 ------MEPQLLLLDEPTqgmGSEDV---DRVVELVRKAA--QGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQT 234
Cdd:PRK13548 151 qlwepdGPPRWLLLDEPT---SALDLahqHHVLRLARQLAheRGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
250
....*....|.
gi 504233768 235 VSADPRVREVY 245
Cdd:PRK13548 228 VLTPETLRRVY 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-246 |
6.59e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 111.33 E-value: 6.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKG-----FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK 81
Cdd:PRK13651 3 IKVKNIVKIFNKklpteLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 GIVRSFQISAVFPHMTALENIR----VALQTAEgssYSFWKS-------------GNSLHKLNERCMELLESVGLAE-FA 143
Cdd:PRK13651 83 VLEKLVIQKTRFKKIKKIKEIRrrvgVVFQFAE---YQLFEQtiekdiifgpvsmGVSKEEAKKRAAKYIELVGLDEsYL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 144 NTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKA-AQGRTVLMVEHNLSVVSKLCDRITVLA 222
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLnKQGKTIILVTHDLDNVLEWTKRTIFFK 239
|
250 260
....*....|....*....|....*
gi 504233768 223 QGAVLTEGD-YQTVSADPRVREVYM 246
Cdd:PRK13651 240 DGKIIKDGDtYDILSDNKFLIENNM 264
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
1-251 |
3.19e-28 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 111.28 E-value: 3.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVkefkgfVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSA---A 77
Cdd:PRK10070 29 LSKEQILEKTGLS------LGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 78 IARKGIVRSFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRA 157
Cdd:PRK10070 103 VRRKKIAMVFQSFALMPHMTVLDNTAFGMELA----------GINAEERREKALDALRQVGLENYAHSYPDELSGGMRQR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMG----SEDVDRVVELvrKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQ 233
Cdd:PRK10070 173 VGLARALAINPDILLMDEAFSALDplirTEMQDELVKL--QAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPD 250
|
250 260
....*....|....*....|.
gi 504233768 234 TVSADPR---VREVYMGSDGS 251
Cdd:PRK10070 251 EILNNPAndyVRTFFRGVDIS 271
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
7-226 |
3.75e-28 |
|
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: 106.96 E-value: 3.75e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSaaiARKGIVRS 86
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP---KDRDIAMV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQTAEGSSysfwksgnslHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:cd03301 78 FQNYALYPHMTVYDNIAFGLKLRKVPK----------DEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 167 EPQLLLLDEPTQgmgseDVD---RV---VELVR-KAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:cd03301 148 EPKVFLMDEPLS-----NLDaklRVqmrAELKRlQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
7-245 |
4.87e-28 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 110.70 E-value: 4.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARkgivrs 86
Cdd:PRK09536 4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASR------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 fQISAVfPHMTALE-NIRVAL-----QTAEGSSYSFWKSGNSlhKLNERCMellESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:PRK09536 78 -RVASV-PQDTSLSfEFDVRQvvemgRTPHRSRFDTWTETDR--AAVERAM---ERTGVAQFADRPVTSLSGGERQRVLL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 161 ATTLAMEPQLLLLDEPTqgmGSEDVDRVV---ELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVS 236
Cdd:PRK09536 151 ARALAQATPVLLLDEPT---ASLDINHQVrtlELVRRLVDdGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVL 227
|
....*....
gi 504233768 237 ADPRVREVY 245
Cdd:PRK09536 228 TADTLRAAF 236
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
26-239 |
6.37e-28 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 106.76 E-value: 6.37e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 26 NLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLksaAIARKGIVRSFQISAVFPHMTALENIRVA 105
Cdd:COG3840 19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTAL---PPAERPVSMLFQENNLFPHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 106 LQTaegssysfwksgnSLhKLNE----RCMELLESVGLAEFANTTTVELAYG-RKRAlELATTLAMEPQLLLLDEP---- 176
Cdd:COG3840 96 LRP-------------GL-KLTAeqraQVEQALERVGLAGLLDRLPGQLSGGqRQRV-ALARCLVRKRPILLLDEPfsal 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 177 TQGMGSEDVDRVVELVRKaaQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADP 239
Cdd:COG3840 161 DPALRQEMLDLVDELCRE--RGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
6-267 |
7.09e-28 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 108.74 E-value: 7.09e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVR 85
Cdd:PRK13537 7 PIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFqiSAVFPHMTALENIRVAlqtaegSSYsfwkSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:PRK13537 87 QF--DNLDPDFTVRENLLVF------GRY----FGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADP---RV 241
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSlLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEigcDV 234
|
250 260
....*....|....*....|....*.
gi 504233768 242 REVYmGSDGSGERGSQAAASENVEAA 267
Cdd:PRK13537 235 IEIY-GPDPVALRDELAPLAERTEIS 259
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
21-230 |
8.74e-28 |
|
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: 106.13 E-value: 8.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKGIVRSFQISAVFpHMTALE 100
Cdd:cd03245 19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL-RRNIGYVPQDVTLF-YGTLRD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 101 NIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANTTT-----------VELAYGRKRALELATTLAMEPQ 169
Cdd:cd03245 97 NITLGAPLAD----------------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 170 LLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSkLCDRITVLAQGAVLTEG 230
Cdd:cd03245 161 ILLLDEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
7-230 |
2.10e-27 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 107.99 E-value: 2.10e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRS 86
Cdd:PRK13536 42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FqiSAVFPHMTALENIRValqtaegssYSFWkSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:PRK13536 122 F--DNLDLEFTVRENLLV---------FGRY-FGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALIN 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK13536 190 DPQLLILDEPTTGLDPHARHLIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEG 254
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
10-230 |
2.49e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 105.49 E-value: 2.49e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 10 RNLVK-EFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDitPLKSaaiaRKGIVRsfQ 88
Cdd:cd03267 24 KSLFKrKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLV--PWKR----RKKFLR--R 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 89 ISAVFPHMTALE-NIRVAlqtaegSSYSFWKSGNSLHKLN-----ERCMELLEsvgLAEFANTTTVELAYGRKRALELAT 162
Cdd:cd03267 96 IGVVFGQKTQLWwDLPVI------DSFYLLAAIYDLPPARfkkrlDELSELLD---LEELLDTPVRQLSLGQRMRAEIAA 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03267 167 ALLHEPEILFLDEPTIGLDVVAQENIRNFLKEynRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-250 |
2.75e-27 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 106.39 E-value: 2.75e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAI--ARKGIVRSFQISAVFPHMTALEN 101
Cdd:PRK11831 25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLytVRKRMSMLFQSGALFTDMNVFDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 102 IRVALQTAEGSSYSFWKSgnslhklneRCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMG 181
Cdd:PRK11831 105 VAYPLREHTQLPAPLLHS---------TVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQD 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 182 SEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSA--DPRVREVYMG-SDG 250
Cdd:PRK11831 176 PITMGVLVKLISElnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQAnpDPRVRQFLDGiADG 249
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
20-230 |
4.24e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 105.90 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDIT--PLKSAAIARK-GIVrsFQisavFPHM 96
Cdd:PRK13637 21 KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKvGLV--FQ----YPEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 97 TALENIrVALQTAEGSSysfwKSGNSLHKLNERCMELLESVGLA--EFANTTTVELAYGRKRALELATTLAMEPQLLLLD 174
Cdd:PRK13637 95 QLFEET-IEKDIAFGPI----NLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 175 EPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK13637 170 EPTAGLDPKGRDEILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
5.23e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 105.66 E-value: 5.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 5 YVLETRNLVKEFKGFV-AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPlKSAAIARKGI 83
Cdd:PRK13652 2 HLIETRDLCYSYSGSKeALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITK-ENIREVRKFV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 84 VRSFQ------ISAVFPHMTALENIRVALQTAegssysfwksgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRA 157
Cdd:PRK13652 81 GLVFQnpddqiFSPTVEQDIAFGPINLGLDEE---------------TVAHRVSSALHMLGLEELRDRVPHHLSGGEKKR 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTV 235
Cdd:PRK13652 146 VAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPEtyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEI 225
|
....
gi 504233768 236 SADP 239
Cdd:PRK13652 226 FLQP 229
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
7-231 |
1.18e-26 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.94 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTT---VFNLLTkflIPTRGQILYRGE--DITPLKSAAIARK 81
Cdd:COG4161 3 IQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSllrVLNLLE---TPDSGQLNIAGHqfDFSQKPSEKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 -----GIVrsFQISAVFPHMTALEN-----IRVALQTAEgssysfwksgnslhKLNERCMELLESVGLAEFANTTTVELA 151
Cdd:COG4161 80 lrqkvGMV--FQQYNLWPHLTVMENlieapCKVLGLSKE--------------QAREKAMKLLARLRLTDKADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 152 YGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQtGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
.
gi 504233768 231 D 231
Cdd:COG4161 224 D 224
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-247 |
1.40e-26 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 103.42 E-value: 1.40e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 3 EQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKG 82
Cdd:PRK11614 2 EKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIMREA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVRSFQISAVFPHMTALENIRVAlqtaegssySFWKSGNSLHKLNERCMELLESvgLAEFANTTTVELAYGRKRALELAT 162
Cdd:PRK11614 82 VAIVPEGRRVFSRMTVEENLAMG---------GFFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRV 241
Cdd:PRK11614 151 ALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQlREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAV 230
|
....*.
gi 504233768 242 REVYMG 247
Cdd:PRK11614 231 RSAYLG 236
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
6-229 |
2.15e-26 |
|
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: 102.90 E-value: 2.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKG----FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK 81
Cdd:COG4181 8 IIELRGLTKTVGTgageLTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 -----GIV-RSFQIsavFPHMTALENIRVALQTAeGSSYSFwksgnslhklnERCMELLESVGLAEFANTTTVELAYGRK 155
Cdd:COG4181 88 rarhvGFVfQSFQL---LPTLTALENVMLPLELA-GRRDAR-----------ARARALLERVGLGHRLDHYPAQLSGGEQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 156 RALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVR--KAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTE 229
Cdd:COG4181 153 QRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFelNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-231 |
2.66e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 104.78 E-value: 2.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF-------------KGFV--------AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQIL 64
Cdd:COG4586 1 IIEVENLSKTYrvyekepglkgalKGLFrreyreveAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 65 YRGEDitPLKSaaiaRKGIVRsfQISAVF-------PHMTALEnirvalqtaegssySFwksgnSLHK---------LNE 128
Cdd:COG4586 81 VLGYV--PFKR----RKEFAR--RIGVVFgqrsqlwWDLPAID--------------SF-----RLLKaiyripdaeYKK 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 129 RCMELLESVGLAEFANTTTVELAYG-RKRAlELATTLAMEPQLLLLDEPTQGMgseDV---DRVVELVRK--AAQGRTVL 202
Cdd:COG4586 134 RLDELVELLDLGELLDTPVRQLSLGqRMRC-ELAAALLHRPKILFLDEPTIGL---DVvskEAIREFLKEynRERGTTIL 209
|
250 260
....*....|....*....|....*....
gi 504233768 203 MVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:COG4586 210 LTSHDMDDIEALCDRVIVIDHGRIIYDGS 238
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-230 |
3.19e-26 |
|
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: 101.80 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplkSAAIARKGIVRSFQISAVFPHMTALENIR 103
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVT---AAPPADRPVSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 104 VALqtaegssysfwksgNSLHKLNERCMELLES----VGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQG 179
Cdd:cd03298 93 LGL--------------SPGLKLTAEDRQAIEValarVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504233768 180 MGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03298 159 LDPALRAEMLDLVLDlhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-224 |
3.62e-26 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 105.03 E-value: 3.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKsaaiAR 80
Cdd:PRK09452 9 SSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----AE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 KGIVRS-FQISAVFPHMTALENIRVALQTAegssysfwKSGNSlhKLNERCMELLESVGLAEFANTTTVELAYGRKRALE 159
Cdd:PRK09452 85 NRHVNTvFQSYALFPHMTVFENVAFGLRMQ--------KTPAA--EITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 160 LATTLAMEPQLLLLDEP--------TQGMGSEdvdrVVELVRKAaqGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:PRK09452 155 IARAVVNKPKVLLLDESlsaldyklRKQMQNE----LKALQRKL--GITFVFVTHDQEEALTMSDRIVVMRDG 221
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
7-224 |
5.41e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 102.47 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEF-KGFV----AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARk 81
Cdd:COG1101 2 LELKNLSKTFnPGTVnekrALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 givrsfQISAVF--------PHMTALENIrvALQTAEGSSYSFwKSGNSlHKLNERCMELLESVGLA-EFANTTTVELAY 152
Cdd:COG1101 81 ------YIGRVFqdpmmgtaPSMTIEENL--ALAYRRGKRRGL-RRGLT-KKRRELFRELLATLGLGlENRLDTKVGLLS 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 153 GRKR-ALelatTLAM----EPQLLLLDEPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:COG1101 151 GGQRqAL----SLLMatltKPKLLLLDEHTAALDPKTAALVLELTEKivEENNLTTLMVTHNMEQALDYGNRLIMMHEG 225
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
22-230 |
5.74e-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: 5.74e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYR------GEDITPLKSaaiaRKGIVRSFQISAVFPH 95
Cdd:COG1119 19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRLfgerrgGEDVWELRK----RIGLVSPALQLRFPRD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 96 MTALEnirVALqTAEGSSYSFWKSGNSLHKlnERCMELLESVGLAEFANTTTVELAYG-RKRALeLATTLAMEPQLLLLD 174
Cdd:COG1119 95 ETVLD---VVL-SGFFDSIGLYREPTDEQR--ERARELLELLGLAHLADRPFGTLSQGeQRRVL-IARALVKDPELLILD 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 175 EPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:COG1119 168 EPTAGLDLGARELLLALLDKLAAegAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAG 225
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
7-231 |
9.33e-26 |
|
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: 100.29 E-value: 9.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKF--LIPTRGQILYRGEDITPLKSAAIARKGIV 84
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDLPPEERARLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 RSFQISAVFPHMTALENIRvalqtaeGSSYSFwkSGnslhklnercmellesvglaefantttvelayGRKRALELATTL 164
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLR-------YVNEGF--SG--------------------------------GEKKRNEILQLL 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKL-CDRITVLAQGAVLTEGD 231
Cdd:cd03217 120 LLEPDLAILDEPDSGLDIDALRLVAEVINKlREEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGD 188
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
22-226 |
1.22e-25 |
|
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: 100.02 E-value: 1.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITP---LKSAAIARKGIVRSFQISAVFphmta 98
Cdd:cd03226 16 LDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKAkerRKSIGYVMQDVDYQLFTDSVR----- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 99 lENIRVALQTAEGSsysfwksgnslhklNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQ 178
Cdd:cd03226 91 -EELLLGLKELDAG--------------NEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTS 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504233768 179 GMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:cd03226 156 GLDYKNMERVGELIRElAAQGKAVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
10-230 |
1.27e-25 |
|
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: 105.87 E-value: 1.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 10 RNLVKEFK--GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplKSAAIARKGIVRSF 87
Cdd:TIGR01257 932 KNLVKIFEpsGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIE--TNLDAVRQSLGMCP 1009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 88 QISAVFPHMTALENIRVALQTaegssysfwkSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAME 167
Cdd:TIGR01257 1010 QHNILFHHLTVAEHILFYAQL----------KGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGD 1079
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 168 PQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:TIGR01257 1080 AKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
6-240 |
1.37e-25 |
|
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: 105.15 E-value: 1.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF---KG--------FVAVNDVNLQIRQGDIHALIGPNGAGKTTV-FNLLTkfLIPTRGQILYRGEDITPL 73
Cdd:COG4172 275 LLEARDLKVWFpikRGlfrrtvghVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLR--LIPSEGEIRFDGQDLDGL 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 74 KSAaiARKGIVRSFQIsaVF--------PHMTALENIrvalqtAEGssYSFWKSGNSLHKLNERCMELLESVGL-AEFAN 144
Cdd:COG4172 353 SRR--ALRPLRRRMQV--VFqdpfgslsPRMTVGQII------AEG--LRVHGPGLSAAERRARVAEALEEVGLdPAARH 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 145 TTTVELAYG-RKRaLELATTLAMEPQLLLLDEPTQGMgsedvDR-----VVELVRK--AAQGRTVLMVEHNLSVVSKLCD 216
Cdd:COG4172 421 RYPHEFSGGqRQR-IAIARALILEPKLLVLDEPTSAL-----DVsvqaqILDLLRDlqREHGLAYLFISHDLAVVRALAH 494
|
250 260
....*....|....*....|....
gi 504233768 217 RITVLAQGAVLTEGDYQTVSADPR 240
Cdd:COG4172 495 RVMVMKDGKVVEQGPTEQVFDAPQ 518
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
21-231 |
1.71e-25 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 100.86 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTT---VFNLLTkflIPTRGQILYRG------EDITPLKSAAIARK-GIVrsFQIS 90
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSllrVLNLLE---MPRSGTLNIAGnhfdfsKTPSDKAIRELRRNvGMV--FQQY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 91 AVFPHMTALEN-----IRVAlqtaegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:PRK11124 92 NLWPHLTVQQNlieapCRVL--------------GLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENGHIVEQGD 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
19-231 |
3.79e-25 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 99.77 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 19 FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEdITPLksaaiarkgivrsFQISAVF-PHMT 97
Cdd:COG1134 39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL-------------LELGAGFhPELT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 98 ALENIRVAlqtaeGSSYsfwksGNSLHKLNERCMELLESVGLAEFANT---T-----TVELAYGrkraleLATtlAMEPQ 169
Cdd:COG1134 105 GRENIYLN-----GRLL-----GLSRKEIDEKFDEIVEFAELGDFIDQpvkTyssgmRARLAFA------VAT--AVDPD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 170 LLLLDEptqGMGSEDV-------DRVVELVRkaaQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:COG1134 167 ILLVDE---VLAVGDAafqkkclARIRELRE---SGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGD 229
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-240 |
3.93e-25 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 100.26 E-value: 3.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQ--YVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVF---NLLTkflIPTRGQILYRGEDIT---- 71
Cdd:COG4598 1 MTDTapPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLrciNLLE---TPDSGEIRVGGEEIRlkpd 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 72 ------PLKSAAIARkgiVRSfQISAVF------PHMTALENIRVAlqtaegssysfwksgnSLHKLN-------ERCME 132
Cdd:COG4598 78 rdgelvPADRRQLQR---IRT-RLGMVFqsfnlwSHMTVLENVIEA----------------PVHVLGrpkaeaiERAEA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 133 LLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVV 211
Cdd:COG4598 138 LLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDlAEEGRTMLVVTHEMGFA 217
|
250 260
....*....|....*....|....*....
gi 504233768 212 SKLCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:COG4598 218 RDVSSHVVFLHQGRIEEQGPPAEVFGNPK 246
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
20-221 |
3.27e-24 |
|
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: 101.21 E-value: 3.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLkSAAIARKGIVRSFQISAVFPHmTAL 99
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADA-DADSWRDQIAWVPQHPFLFAG-TIA 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIRVALQTAEGSSYSfwksgnslhklnercmELLESVGLAEFANTTT-----------VELAYGRKRALELATTLAMEP 168
Cdd:TIGR02857 414 ENIRLARPDASDAEIR----------------EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDA 477
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504233768 169 QLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVsKLCDRITVL 221
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGRTVLLVTHRLALA-ALADRIVVL 529
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
8-245 |
5.46e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 97.08 E-value: 5.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVR- 85
Cdd:COG4604 3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRlAILRq 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISA---V--------FPHmtalenirvalqtaegssysfwkSGNSL----HKLNERCMELLEsvgLAEFANTTTVEL 150
Cdd:COG4604 83 ENHINSrltVrelvafgrFPY-----------------------SKGRLtaedREIIDEAIAYLD---LEDLADRYLDEL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 151 AYG-RKRALeLATTLAMEPQLLLLDEPTQGMgseDVDRVVE---LVRKAA--QGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:COG4604 137 SGGqRQRAF-IAMVLAQDTDYVLLDEPLNNL---DMKHSVQmmkLLRRLAdeLGKTVVIVLHDINFASCYADHIVAMKDG 212
|
250 260
....*....|....*....|.
gi 504233768 225 AVLTEGDYQTVSADPRVREVY 245
Cdd:COG4604 213 RVVAQGTPEEIITPEVLSDIY 233
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-240 |
9.70e-24 |
|
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443332 [Multi-domain] Cd Length: 533 Bit Score: 99.76 E-value: 9.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVKEFKG----FVAVNDVNLQIRQGDIHALIGPNGAGKT----TVFNLLTKFLIPTRGQILYRGEDITP 72
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 73 LKSAAIARkgiVRSFQISAVF--PhMTALeN--IRVALQTAEGSSysfwksgnsLHK------LNERCMELLESVGLAEF 142
Cdd:COG4172 81 LSERELRR---IRGNRIAMIFqeP-MTSL-NplHTIGKQIAEVLR---------LHRglsgaaARARALELLERVGIPDP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 143 ANTTTV---ELAYG-RKRALeLATTLAMEPQLLLLDEPTQGMgseDV---DRVVELVR--KAAQGRTVLMVEHNLSVVSK 213
Cdd:COG4172 147 ERRLDAyphQLSGGqRQRVM-IAMALANEPDLLIADEPTTAL---DVtvqAQILDLLKdlQRELGMALLLITHDLGVVRR 222
|
250 260
....*....|....*....|....*..
gi 504233768 214 LCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:COG4172 223 FADRVAVMRQGEIVEQGPTAELFAAPQ 249
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
7-224 |
1.41e-23 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 99.22 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRS 86
Cdd:PRK11288 5 LSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAAGVAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVAlqtaegssySFWKSGNSLHK--LNERCMELLESVGLAEFANTTTVELAYGRKRALELATTL 164
Cdd:PRK11288 85 YQELHLVPEMTVAENLYLG---------QLPHKGGIVNRrlLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRElRAEGRVILYVSHRMEEIFALCDAITVFKDG 216
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-208 |
1.50e-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: 99.36 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKgIVRSFQISAVFpHMTAL 99
Cdd:TIGR02868 349 PVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR-VSVCAQDAHLF-DTTVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIRVALQTAEGssysfwksgnslhklnERCMELLESVGLAEF-------ANTTTVE----LAYGRKRALELATTLAMEP 168
Cdd:TIGR02868 427 ENLRLARPDATD----------------EELWAALERVGLADWlralpdgLDTVLGEggarLSGGERQRLALARALLADA 490
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504233768 169 QLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNL 208
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGRTVVLITHHL 530
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
21-233 |
2.56e-23 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 94.60 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVRsfQISAVFpHMTAL 99
Cdd:cd03251 17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQiGLVS--QDVFLF-NDTVA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANTTT-----------VELAYGRKRALELATTLAMEP 168
Cdd:cd03251 94 ENIAYGRPGAT----------------REEVEEAARAANAHEFIMELPegydtvigergVKLSGGQRQRIAIARALLKDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 169 QLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQ 233
Cdd:cd03251 158 PILILDEATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHE 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-238 |
2.98e-23 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 98.36 E-value: 2.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKfLIPT---RGQILYRGEditPLKSAAIA--- 79
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGS---PLKASNIRdte 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 RKGIVRSFQISAVFPHMTALENIRVALQ-TAEGSSYSFwksgnslHKLNERCMELLESVGLAEFANTTTV-ELAYGRKRA 157
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGNEiTLPGGRMAY-------NAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVS 236
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDlKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMS 229
|
..
gi 504233768 237 AD 238
Cdd:TIGR02633 230 ED 231
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
22-239 |
3.61e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 3.61e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPL---KSAAIARKGIVRSFQisavFPHMTA 98
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPEtgnKNLKKLRKKVSLVFQ----FPEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 99 LENirVALQTAEGSSYSFwksGNSLHKLNERCMELLESVGLAE-FANTTTVELAYGRKRALELATTLAMEPQLLLLDEPT 177
Cdd:PRK13641 99 FEN--TVLKDVEFGPKNF---GFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPA 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 178 QGMGSEDVDRVVEL-VRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADP 239
Cdd:PRK13641 174 AGLDPEGRKEMMQLfKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDK 236
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-214 |
4.55e-23 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 94.11 E-value: 4.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 2 SEQYVLETRNLVKEFK-GFV---AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAA 77
Cdd:PRK11629 1 MNKILLQCDNLCKRYQeGSVqtdVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 78 iarKGIVRS------FQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELA 151
Cdd:PRK11629 81 ---KAELRNqklgfiYQFHHLLPDFTALENVAMPLLIG----------KKKPAEINSRALEMLAAVGLEHRANHRPSELS 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 152 YGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKL 214
Cdd:PRK11629 148 GGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGElnRLQGTAFLVVTHDLQLAKRM 212
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
21-230 |
4.57e-23 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 97.93 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVrsFQISAVFpHMTAL 99
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQiGVV--PQDTFLF-SGTIR 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANT------TTV-----ELAYGRKRALELATTLAMEP 168
Cdd:COG1132 432 ENIRYGRPDAT----------------DEEVEEAAKAAQAHEFIEAlpdgydTVVgergvNLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 169 QLLLLDEPTqgmgSEdVDRVVE-LVRKA----AQGRTVLMVEHNLSVVsKLCDRITVLAQGAVLTEG 230
Cdd:COG1132 496 PILILDEAT----SA-LDTETEaLIQEAlerlMKGRTTIVIAHRLSTI-RNADRILVLDDGRIVEQG 556
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
1-240 |
4.91e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 94.65 E-value: 4.91e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETrNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPL------- 73
Cdd:PRK10619 1 MSENKLNVI-DLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgql 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 74 -----KSAAIARKGIVRSFQISAVFPHMTALENIRVA-LQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTT- 146
Cdd:PRK10619 80 kvadkNQLRLLRTRLTMVFQHFNLWSHMTVLENVMEApIQVL----------GLSKQEARERAVKYLAKVGIDERAQGKy 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 147 TVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGA 225
Cdd:PRK10619 150 PVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQlAEEGKTMVVVTHEMGFARHVSSHVIFLHQGK 229
|
250
....*....|....*
gi 504233768 226 VLTEGDYQTVSADPR 240
Cdd:PRK10619 230 IEEEGAPEQLFGNPQ 244
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-245 |
9.98e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 96.82 E-value: 9.98e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKGIVRSFQISAVFPHmTALE 100
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL-RQAISVVSQRVHLFSA-TLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 101 NIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFA------NTTTVE----LAYGRKRALELATTLAMEPQL 170
Cdd:PRK11160 433 NLLLAAPNAS----------------DEALIEVLQQVGLEKLLeddkglNAWLGEggrqLSGGEQRRLGIARALLHDAPL 496
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 171 LLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLcDRITVLAQGAVLTEGDYQT-VSADPRVREVY 245
Cdd:PRK11160 497 LLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQElLAQQGRYYQLK 571
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-240 |
1.32e-22 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 93.44 E-value: 1.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 4 QYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKF--LIP---TRGQILYRGEDITPLKSAAI 78
Cdd:PRK14247 1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIFKMDVIEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 79 aRKGIVRSFQISAVFPHMTALENIRVALQTAegssysfwKSGNSLHKLNERCMELLESVGLAEFA----NTTTVELAYGR 154
Cdd:PRK14247 81 -RRRVQMVFQIPNPIPNLSIFENVALGLKLN--------RLVKSKKELQERVRWALEKAQLWDEVkdrlDAPAGKLSGGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 155 KRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQT 234
Cdd:PRK14247 152 QQRLCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTRE 231
|
....*.
gi 504233768 235 VSADPR 240
Cdd:PRK14247 232 VFTNPR 237
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-248 |
6.69e-22 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 93.21 E-value: 6.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEqyvLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLksaAIAR 80
Cdd:COG3839 1 MAS---LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDL---PPKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 KGI--VrsFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYG-RKR- 156
Cdd:COG3839 75 RNIamV--FQSYALYPHMTVYENIAFPLKLR----------KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGqRQRv 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 157 AleLATTLAMEPQLLLLDEPTQGmgsedVD---RV---VELVR-KAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTE 229
Cdd:COG3839 143 A--LGRALVREPKVFLLDEPLSN-----LDaklRVemrAEIKRlHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQV 215
|
250 260
....*....|....*....|.
gi 504233768 230 GDYQTVSADPRVREV--YMGS 248
Cdd:COG3839 216 GTPEELYDRPANLFVagFIGS 236
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-231 |
8.39e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 91.72 E-value: 8.39e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 5 YVLETRNLVKEFK-GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-G 82
Cdd:PRK13647 3 NIIEVEDLHFRYKdGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKvG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVrsFQI--SAVFPhMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:PRK13647 83 LV--FQDpdDQVFS-STVWDDVAFGPVNM----------GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAI 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 161 ATTLAMEPQLLLLDEPTQGMGSEDVDRVVE-LVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:PRK13647 150 AGVLAMDPDVIVLDEPMAYLDPRGQETLMEiLDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGD 221
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-237 |
8.79e-22 |
|
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: 94.10 E-value: 8.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLL--TKFLIPTRGQILYR------------------ 66
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIIYHvalcekcgyverpskvge 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 67 -----GEDITPLK----------SAAIARKGIV---RSFqisAVFPHMTALENIRVALQTAEgssysfWKSGNSLhklnE 128
Cdd:TIGR03269 81 pcpvcGGTLEPEEvdfwnlsdklRRRIRKRIAImlqRTF---ALYGDDTVLDNVLEALEEIG------YEGKEAV----G 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 129 RCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMV--EH 206
Cdd:TIGR03269 148 RAVDLIEMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVltSH 227
|
250 260 270
....*....|....*....|....*....|.
gi 504233768 207 NLSVVSKLCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:TIGR03269 228 WPEVIEDLSDKAIWLENGEIKEEGTPDEVVA 258
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
25-239 |
1.03e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 94.14 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 25 VNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLiPTRGQILYRGediTPLKSAAIA--RKgivrsfQISAV-----FPHMT 97
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKING---IELRELDPEswRK------HLSWVgqnpqLPHGT 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 98 ALENIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANTTTVELAY-----------GRKRALELATTLAM 166
Cdd:PRK11174 439 LRDNVLLGNPDAS----------------DEQLQQALENAWVSEFLPLLPQGLDTpigdqaaglsvGQAQRLALARALLQ 502
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQTVSADP 239
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAG 574
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-239 |
1.14e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 91.62 E-value: 1.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSA----AIARK-GIVrsFQisavFPH 95
Cdd:PRK13634 22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNkklkPLRKKvGIV--FQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 96 MTALENIrVALQTAEGSSySFwksGNSLHKLNERCMELLESVGLAE-FANTTTVELAYGRKRALELATTLAMEPQLLLLD 174
Cdd:PRK13634 96 HQLFEET-VEKDICFGPM-NF---GVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 175 EPTQGM---GSEDV-DRVVELVRKaaQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADP 239
Cdd:PRK13634 171 EPTAGLdpkGRKEMmEMFYKLHKE--KGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
13-230 |
2.07e-21 |
|
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: 89.51 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 13 VKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAiarkgivrSFQisav 92
Cdd:cd03220 29 KGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLGLGG--------GFN---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 93 fPHMTALENIRVALqtaegssysfwksgnSLHKLNERCM-----ELLESVGLAEFANTTTVELAYGRKRALELATTLAME 167
Cdd:cd03220 97 -PELTGRENIYLNG---------------RLLGLSRKEIdekidEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALE 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 168 PQLLLLDEptqGMGSEDV-------DRVVELVRkaaQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03220 161 PDILLIDE---VLAVGDAafqekcqRRLRELLK---QGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
20-235 |
3.00e-21 |
|
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: 89.47 E-value: 3.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVrsFQISAVFpHMTA 98
Cdd:cd03252 16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQvGVV--LQENVLF-NRSI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 99 LENIrvALqTAEGSSYSFWKSGNSLHKLNERCMELLEsvGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQ 178
Cdd:cd03252 93 RDNI--AL-ADPGMSMERVIEAAKLAGAHDFISELPE--GYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 179 GMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVsKLCDRITVLAQGAVLTEGDYQTV 235
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDEL 223
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
24-226 |
3.10e-21 |
|
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: 89.07 E-value: 3.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKgIVRSFQISAVFPHmTALENIR 103
Cdd:cd03248 32 DVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSK-VSLVGQEPVLFAR-SLQDNIA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 104 VALQTAEGSSYSFWKSGNSLHKLnercMELLESvGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSE 183
Cdd:cd03248 110 YGLQSCSFECVKEAAQKAHAHSF----ISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504233768 184 DVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAV 226
Cdd:cd03248 185 SEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
21-230 |
5.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 89.79 E-value: 5.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQI---------LYRGEDITPLKSaaiaRKGIVRSFQISA 91
Cdd:PRK13643 21 ALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdivvssTSKQKEIKPVRK----KVGVVFQFPESQ 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 92 VFPHmTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLA-EFANTTTVELAYGRKRALELATTLAMEPQL 170
Cdd:PRK13643 97 LFEE-TVLKDVAFGPQNF----------GIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEV 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 171 LLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK13643 166 LVLDEPTAGLDPKARIEMMQLFESIHQsGQTVVLVTHLMDDVADYADYVYLLEKGHIISCG 226
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
14-230 |
5.95e-21 |
|
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: 88.12 E-value: 5.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 14 KEFKGFvavndvNLQIR---QGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGediTPLKSAAIA------RKGIV 84
Cdd:cd03297 8 KRLPDF------TLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRKKinlppqQRKIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 RSFQISAVFPHMTALENIRVALQTAEGSsysfwksgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTL 164
Cdd:cd03297 79 LVFQQYALFPHLNVRENLAFGLKRKRNR------------EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03297 147 AAQPELLLLDEPFSALDRALRLQLLPELKQIKKnlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-235 |
6.52e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 89.42 E-value: 6.52e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPL---KSAAIARK--GIVRSFQISAVFPH 95
Cdd:PRK13649 22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsknKDIKQIRKkvGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 96 mTALENIRVALQtaegssySFwksGNSLHKLNERCMELLESVGLAE-FANTTTVELAYGRKRALELATTLAMEPQLLLLD 174
Cdd:PRK13649 102 -TVLKDVAFGPQ-------NF---GVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 175 EPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTV 235
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKLHQsGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
6-238 |
7.63e-21 |
|
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: 91.40 E-value: 7.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF----KGFV-AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYR-GEDITPLKSAAIA 79
Cdd:TIGR03269 279 IIKVRNVSKRYisvdRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPD 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 RKGIVRS-----FQISAVFPHMTALENIRVALqtaegssysfwksgnSLHKLNE----RCMELLESVGLAE-----FANT 145
Cdd:TIGR03269 359 GRGRAKRyigilHQEYDLYPHRTVLDNLTEAI---------------GLELPDElarmKAVITLKMVGFDEekaeeILDK 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 146 TTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQ 223
Cdd:TIGR03269 424 YPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREemEQTFIIVSHDMDFVLDVCDRAALMRD 503
|
250
....*....|....*
gi 504233768 224 GAVLTEGDYQTVSAD 238
Cdd:TIGR03269 504 GKIVKIGDPEEIVEE 518
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-240 |
8.00e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 88.57 E-value: 8.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFL------IPTRGQILYRGEDITPLKSAAIaRKGIVRSFQISAVFPH 95
Cdd:PRK14246 26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKL-RKEVGMVFQQPNPFPH 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 96 MTALENIRVALQTAEgssysfWKSGNSLHKLNERCmelLESVGL----AEFANTTTVELAYGRKRALELATTLAMEPQLL 171
Cdd:PRK14246 105 LSIYDNIAYPLKSHG------IKEKREIKKIVEEC---LRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 172 LLDEPTQGM---GSEDVDRVVELVRKAAqgrTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:PRK14246 176 LMDEPTSMIdivNSQAIEKLITELKNEI---AIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPK 244
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-259 |
9.02e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 88.53 E-value: 9.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 4 QYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFL---------IPTRGQILYRGEDITPLK 74
Cdd:PRK09984 2 QTIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdksagshIELLGRTVQREGRLARDI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 75 SAAIARKGIVrsFQISAVFPHMTALENIRVAlqtAEGSSySFWKSGNSL--HKLNERCMELLESVGLAEFANTTTVELAY 152
Cdd:PRK09984 82 RKSRANTGYI--FQQFNLVNRLSVLENVLIG---ALGST-PFWRTCFSWftREQKQRALQALTRVGMVHFAHQRVSTLSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 153 GRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK09984 156 GQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQndGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
|
250 260
....*....|....*....|....*....
gi 504233768 231 DYQTVSADpRVREVYMGSDgSGERGSQAA 259
Cdd:PRK09984 236 SSQQFDNE-RFDHLYRSIN-RVEENAKAA 262
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-230 |
9.11e-21 |
|
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: 86.84 E-value: 9.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVA------VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIP--TRGQILYRGEDITPLKSAA 77
Cdd:cd03213 3 TLSFRNLTVTVKSSPSksgkqlLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 78 IArkGIVRsfQISAVFPHMTALENIRVALQtaegssysfwksgnslhklnercmelLESVGLAEfantttvelaygRKRa 157
Cdd:cd03213 83 II--GYVP--QDDILHPTLTVRETLMFAAK--------------------------LRGLSGGE------------RKR- 119
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLS-VVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03213 120 VSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADtGRTIICSIHQPSsEIFELFDKLLLLSQGRVIYFG 194
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
19-230 |
9.17e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 88.91 E-value: 9.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 19 FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQIL---YR-GEDITPLKSAAIARKGIVRSFQisavFP 94
Cdd:PRK13645 24 FKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIvgdYAiPANLKKIKEVKRLRKEIGLVFQ----FP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 95 HMTALEnirvalQTAEGS-SYSFWKSGNSLHKLNERCMELLESVGLA-EFANTTTVELAYGRKRALELATTLAMEPQLLL 172
Cdd:PRK13645 100 EYQLFQ------ETIEKDiAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 173 LDEPTQGM---GSEDVDRVVELVRKaAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK13645 174 LDEPTGGLdpkGEEDFINLFERLNK-EYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIG 233
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
18-224 |
1.25e-20 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 87.24 E-value: 1.25e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 18 GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIA--RKGIVRSFQISAVFPH 95
Cdd:PRK10908 14 GRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPflRRQIGMIFQDHHLLMD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 96 MTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDE 175
Cdd:PRK10908 94 RTVYDNVAIPLIIA----------GASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 504233768 176 PTQGMG---SEDVDRVVELVRKAaqGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:PRK10908 164 PTGNLDdalSEGILRLFEEFNRV--GVTVLMATHDIGLISRRSYRMLTLSDG 213
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
26-234 |
1.61e-20 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 87.33 E-value: 1.61e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 26 NLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplkSAAIARKGIVRSFQISAVFPHMTALENIrva 105
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHT---TTPPSRRPVSMLFQENNLFSHLTVAQNI--- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 106 lqtaegssysfwksGNSLH---KLNERCMELLES----VGLAEFANTTTVELAYG-RKRAlELATTLAMEPQLLLLDEPT 177
Cdd:PRK10771 93 --------------GLGLNpglKLNAAQREKLHAiarqMGIEDLLARLPGQLSGGqRQRV-ALARCLVREQPILLLDEPF 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 178 QGMGSEDVDRVVELVRKAAQGR--TVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQT 234
Cdd:PRK10771 158 SALDPALRQEMLTLVSQVCQERqlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDE 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-238 |
1.86e-20 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 90.11 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVR 85
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAEGSSYsfwKSGNSLHKLNERcMELLESVGLAEFANTTTVELAYGRKRalelattla 165
Cdd:PRK15439 91 VPQEPLLFPNLSVKENILFGLPKRQASMQ---KMKQLLAALGCQ-LDLDSSAGSLEVADRQIVEILRGLMR--------- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 166 mEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:PRK15439 158 -DSRILILDEPTASLTPAETERLFSRIRElLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTD 230
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-221 |
3.66e-20 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 85.36 E-value: 3.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 16 FKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEditplksaaiARKGIVrsFQISAV--- 92
Cdd:NF040873 2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYV--PQRSEVpds 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 93 FPhmtalenIRVAlqtaEGSSYSFWKSGNSLHKLN----ERCMELLESVGLAEFANTTTVELAYG-RKRALeLATTLAME 167
Cdd:NF040873 70 LP-------LTVR----DLVAMGRWARRGLWRRLTrddrAAVDDALERVGLADLAGRQLGELSGGqRQRAL-LAQGLAQE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 168 PQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSkLCDRITVL 221
Cdd:NF040873 138 ADLLLLDEPTTGLDAESRERIIALLAEeHARGATVVVVTHDLELVR-RADPCVLL 191
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
6-231 |
6.05e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.60 E-value: 6.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIA-RKGIV 84
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRGLLAlRQQVA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 RSFQISAVFPHMTALENirvalqtaeGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTL 164
Cdd:PRK13638 81 TVFQDPEQQIFYTDIDS---------DIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGAL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:PRK13638 152 VLQARYLLLDEPTAGLDPAGRTQMIAIIRRiVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
9.97e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 86.83 E-value: 9.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLV-----KEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQI----LYRGEDIT 71
Cdd:PRK13631 16 LSDDIILRVKNLYcvfdeKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 72 PLKSAAIARKGIVRSFQ-----ISAVFphmtalenirvalQTAEgssYSFWKS-------------GNSLHKLNERCMEL 133
Cdd:PRK13631 96 NHELITNPYSKKIKNFKelrrrVSMVF-------------QFPE---YQLFKDtiekdimfgpvalGVKKSEAKKLAKFY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 134 LESVGLAE-FANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKA-AQGRTVLMVEHNLSVV 211
Cdd:PRK13631 160 LNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAkANNKTVFVITHTMEHV 239
|
250 260
....*....|....*....|....*...
gi 504233768 212 SKLCDRITVLAQGAVLTEGDYQTVSADP 239
Cdd:PRK13631 240 LEVADEVIVMDKGKILKTGTPYEIFTDQ 267
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-240 |
1.02e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 85.66 E-value: 1.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 4 QYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTV---FNLLTKFLIPTR--GQILYRGEDITPLKSAAI 78
Cdd:PRK14267 2 KFAIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLLELNEEARveGEVRLFGRNIYSPDVDPI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 79 -ARKGIVRSFQISAVFPHMTALENIRVALQtaegssysFWKSGNSLHKLNERCMELLESVGLAEFA----NTTTVELAYG 153
Cdd:PRK14267 82 eVRREVGMVFQYPNPFPHLTIYDNVAIGVK--------LNGLVKSKKELDERVEWALKKAALWDEVkdrlNDYPSNLSGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 154 RKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQ 233
Cdd:PRK14267 154 QRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233
|
....*..
gi 504233768 234 TVSADPR 240
Cdd:PRK14267 234 KVFENPE 240
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
7-208 |
1.12e-19 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 85.52 E-value: 1.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDItplkSAAIARKGIVrs 86
Cdd:PRK11248 2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV----EGPGAERGVV-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:PRK11248 76 FQNEGLLPWRNVQDNVAFGLQLA----------GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAA 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNL 208
Cdd:PRK11248 146 NPQLLLLDEPFGALDAFTREQMQTLLLKlwQETGKQVLLITHDI 189
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-208 |
1.13e-19 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 85.47 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 2 SEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTT---VFNLLTKfLIP---TRGQILYRGEDI-TPLK 74
Cdd:COG1117 7 TLEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTllrCLNRMND-LIPgarVEGEILLDGEDIyDPDV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 75 SAAIARK--GIVrsFQISAVFPhMTALENIRVALQTAEgssysfWKSGnslHKLNERCMELLESVGLAEfantttvE--- 149
Cdd:COG1117 86 DVVELRRrvGMV--FQKPNPFP-KSIYDNVAYGLRLHG------IKSK---SELDEIVEESLRKAALWD-------Evkd 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 150 -LaygRKRALEL----------ATTLAMEPQLLLLDEPTQGmgsedVD-----RVVELVRKAAQGRTVLMVEHNL 208
Cdd:COG1117 147 rL---KKSALGLsggqqqrlciARALAVEPEVLLMDEPTSA-----LDpistaKIEELILELKKDYTIVIVTHNM 213
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
22-242 |
1.31e-19 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.51 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIA--RKGIVRSFQ--ISAVFPHMT 97
Cdd:PRK10419 28 LNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKafRRDIQMVFQdsISAVNPRKT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 98 ALENIRVALQtaegssysfwksgnSLHKLNE-----RCMELLESVGLA-EFANTTTVELAYGRKRALELATTLAMEPQLL 171
Cdd:PRK10419 108 VREIIREPLR--------------HLLSLDKaerlaRASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 172 LLDEPTQgmgseDVDRVVE-----LVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEgdyQTVSADPRVR 242
Cdd:PRK10419 174 ILDEAVS-----NLDLVLQagvirLLKKLQQqfGTACLFITHDLRLVERFCQRVMVMDNGQIVET---QPVGDKLTFS 243
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
18-244 |
1.75e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 1.75e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 18 GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK--GIVrsFQISAV-FP 94
Cdd:PRK13644 14 GTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQGIRKlvGIV--FQNPETqFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 95 HMTALENI-----RVALQTAEgssysfwksgnsLHKLNERCmelLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQ 169
Cdd:PRK13644 92 GRTVEEDLafgpeNLCLPPIE------------IRKRVDRA---LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 170 LLLLDEPTQGMGSEDVDRVVELVRKA-AQGRTVLMVEHNLSVVsKLCDRITVLAQGAVLTEGDYQTVSADPRVREV 244
Cdd:PRK13644 157 CLIFDEVTSMLDPDSGIAVLERIKKLhEKGKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
24-239 |
4.55e-19 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 86.31 E-value: 4.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKgiVRSFQISAVFPHMTALENIR 103
Cdd:TIGR00958 499 GLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQ--VALVGQEPVLFSGSVRENIA 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 104 VALQTAEgssysfwksgnslhklnercMELLESVGLAEFANT---------------TTVELAYGRKRALELATTLAMEP 168
Cdd:TIGR00958 577 YGLTDTP--------------------DEEIMAAAKAANAHDfimefpngydtevgeKGSQLSGGQKQRIAIARALVRKP 636
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 169 QLLLLDEPTQGMGSEdVDRVVELVRKAAqGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQTVSADP 239
Cdd:TIGR00958 637 RVLILDEATSALDAE-CEQLLQESRSRA-SRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
7-206 |
4.66e-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: 82.41 E-value: 4.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplKSAAIARKGIVRS 86
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA--EQRDEPHENILYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRvalqtaegssysFWKSGNSLHKLNerCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:TIGR01189 79 GHLPGLKPELSALENLH------------FWAAIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLS 144
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504233768 167 EPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEH 206
Cdd:TIGR01189 145 RRPLWILDEPTTALDKAGVALLAGLLRAhLARGGIVLLTTH 185
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
18-230 |
6.37e-19 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 83.05 E-value: 6.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 18 GFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVRsfQISAVFpHM 96
Cdd:cd03253 13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAiGVVP--QDTVLF-ND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 97 TALENIRVALQTA-EGSSYSFWKSGnslhKLNERCMELlesvglaEFANTTTV-----ELAYGRKRALELATTLAMEPQL 170
Cdd:cd03253 90 TIGYNIRYGRPDAtDEEVIEAAKAA----QIHDKIMRF-------PDGYDTIVgerglKLSGGEKQRVAIARAILKNPPI 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 171 LLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEG 230
Cdd:cd03253 159 LLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERG 217
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-233 |
7.25e-19 |
|
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: 82.97 E-value: 7.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 23 NDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVRsfQISAVFPhMTALEN 101
Cdd:cd03249 20 KGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQiGLVS--QEPVLFD-GTIAEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 102 IRvalqtaegssYSfwksgnslhkLNERCMELLESVglAEFANT------------TTV-----ELAYGRKRALELATTL 164
Cdd:cd03249 97 IR----------YG----------KPDATDEEVEEA--AKKANIhdfimslpdgydTLVgergsQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQ 233
Cdd:cd03249 155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHD 222
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
19-230 |
8.48e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 83.68 E-value: 8.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 19 FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDI---TPLKSAAIARKGIVRSFQisavFPH 95
Cdd:PRK13646 20 HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthkTKDKYIRPVRKRIGMVFQ----FPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 96 MTALENiRVALQTAEGSSySFwksGNSLHKLNERCMELLESVGLA-EFANTTTVELAYGRKRALELATTLAMEPQLLLLD 174
Cdd:PRK13646 96 SQLFED-TVEREIIFGPK-NF---KMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 175 EPTQGMGSEDVDRVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK13646 171 EPTAGLDPQSKRQVMRLLKSlqTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQT 228
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-234 |
9.02e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.39 E-value: 9.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDIT-PLKSAAIA 79
Cdd:PRK15056 2 MQQAGIVVNDVTVTWRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRqALQKNLVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 RkgIVRSFQISAVFPHMTAleniRVALQTAEGssYSFWKSGNSLHKlNERCMELLESVGLAEFANTTTVELAYGRKRALE 159
Cdd:PRK15056 82 Y--VPQSEEVDWSFPVLVE----DVVMMGRYG--HMGWLRRAKKRD-RQIVTAALARVDMVEFRHRQIGELSGGQKKRVF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 160 LATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDrITVLAQGAVLTEGDYQT 234
Cdd:PRK15056 153 LARAIAQQGQVILLDEPFTGVDVKTEARIISLLRElRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTET 227
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
11-243 |
9.03e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 83.61 E-value: 9.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 11 NLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRG-----QILYRGEDITPLKSAAIARKGIVR 85
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPhMTALENIRVALQTaegssysfwksgnslHKLNER------CMELLESVGLAEFA----NTTTVELAYGRK 155
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRA---------------HKLVPRkefrgvAQARLTEVGLWDAVkdrlSDSPFRLSGGQQ 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 156 RALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTV 235
Cdd:PRK14271 170 QLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
....*...
gi 504233768 236 SADPRVRE 243
Cdd:PRK14271 250 FSSPKHAE 257
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
22-226 |
1.47e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.86 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKgivrsfqISAVFPHMtalEN 101
Cdd:PRK13650 23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHK-------IGMVFQNP---DN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 102 IRVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGM- 180
Cdd:PRK13650 93 QFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLd 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504233768 181 --GSEDVDRVVELVRKAAQgRTVLMVEHNLSVVSkLCDRITVLAQGAV 226
Cdd:PRK13650 173 peGRLELIKTIKGIRDDYQ-MTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
7-226 |
2.01e-18 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 82.03 E-value: 2.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILyrgEDITPLksaAIARKGIVRS 86
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---AGTAPL---AEAREDTRLM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 FQISAVFPHMTALENIRVALQTAegssysfWKsgnslhklnERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM 166
Cdd:PRK11247 87 FQDARLLPWKKVIDNVGLGLKGQ-------WR---------DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIH 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 167 EPQLLLLDEPtqgMGSEDV-------DRVVELVRKaaQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:PRK11247 151 RPGLLLLDEP---LGALDAltriemqDLIESLWQQ--HGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-216 |
5.49e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 80.98 E-value: 5.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 2 SEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTV---FNLLTKfLIPT---RGQILYRGEDI-TPLK 74
Cdd:PRK14243 6 GTETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTIlrcFNRLND-LIPGfrvEGKVTFHGKNLyAPDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 75 SAAIARKGIVRSFQISAVFPHmTALENIrvalqtAEGSSYSFWKsGNsLHKLNERCME---LLESVglAEFANTTTVELA 151
Cdd:PRK14243 85 DPVEVRRRIGMVFQKPNPFPK-SIYDNI------AYGARINGYK-GD-MDELVERSLRqaaLWDEV--KDKLKQSGLSLS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 152 YGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCD 216
Cdd:PRK14243 154 GGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSD 218
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
21-230 |
6.76e-18 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 80.83 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVrsFQISavfphmtal 99
Cdd:PRK13635 22 ALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQvGMV--FQNP--------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIRVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQG 179
Cdd:PRK13635 91 DNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSM 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504233768 180 MGSEDVDRVVELVR--KAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEG 230
Cdd:PRK13635 171 LDPRGRREVLETVRqlKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
8-230 |
9.85e-18 |
|
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: 79.62 E-value: 9.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIP---TRGQILYRGEDITPLKSAaiARKGIV 84
Cdd:cd03234 9 VGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPDQFQ--KCVAYV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 RSFQISAvfPHMTALENIRVALQTAEGSSysfwKSGNSLHKLNErcMELLESVGLAEFANTTTVELAYGRKRALELATTL 164
Cdd:cd03234 87 RQDDILL--PGLTVRETLTYTAILRLPRK----SSDAIRKKRVE--DVLLRDLALTRIGGNLVKGISGGERRRVSIAVQL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHN-LSVVSKLCDRITVLAQGAVLTEG 230
Cdd:cd03234 159 LWDPKVLILDEPTSGLDSFTALNLVSTLSQlARRNRIVILTIHQpRSDLFRLFDRILLLSSGEIVYSG 226
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
20-230 |
1.11e-17 |
|
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: 78.12 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAaiarkgivRSFQISAVfphmtal 99
Cdd:cd03247 16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA--------LSSLISVL------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 eNIRVALQTAEgssysfwksgnslhklnercmeLLESVGLaefantttvELAYGRKRALELATTLAMEPQLLLLDEPTQG 179
Cdd:cd03247 81 -NQRPYLFDTT----------------------LRNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPTVG 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504233768 180 MGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLcDRITVLAQGAVLTEG 230
Cdd:cd03247 129 LDPITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-231 |
1.12e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 80.22 E-value: 1.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 25 VNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRSFQISAVfPHMTALENIRV 104
Cdd:PRK10575 30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAA-EGMTVRELVAI 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 105 ALQTAEGSSYSFWKSGNslhklnERCMELLESVGLAEFANTTTVELAYG-RKRALeLATTLAMEPQLLLLDEPTQGMG-S 182
Cdd:PRK10575 109 GRYPWHGALGRFGAADR------EKVEEAISLVGLKPLAHRLVDSLSGGeRQRAW-IAMLVAQDSRCLLLDEPTSALDiA 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504233768 183 EDVDrVVELVRKAAQGR--TVLMVEHNLSVVSKLCDRITVLAQGAVLTEGD 231
Cdd:PRK10575 182 HQVD-VLALVHRLSQERglTVIAVLHDINMAARYCDYLVALRGGEMIAQGT 231
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-240 |
1.24e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 79.97 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIAR 80
Cdd:PRK11701 1 MMDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 KGIVRSFQISAVFPHMTALENIRVALqTAEGSsysfwksgnslhkLNERCMelleSVGLAEFANT--------TTVELAY 152
Cdd:PRK11701 81 AERRRLLRTEWGFVHQHPRDGLRMQV-SAGGN-------------IGERLM----AVGARHYGDIratagdwlERVEIDA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 153 GR------------KRALELATTLAMEPQLLLLDEPTQGMgseDVD---RVVELVRK--AAQGRTVLMVEHNLSVVSKLC 215
Cdd:PRK11701 143 ARiddlpttfsggmQQRLQIARNLVTHPRLVFMDEPTGGL---DVSvqaRLLDLLRGlvRELGLAVVIVTHDLAVARLLA 219
|
250 260
....*....|....*....|....*
gi 504233768 216 DRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:PRK11701 220 HRLLVMKQGRVVESGLTDQVLDDPQ 244
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
7-206 |
1.41e-17 |
|
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: 78.69 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGediTPL-KSAAIARKGIVR 85
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNG---GPLdFQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRvalqtaegssysFWKSGNSlhklNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:cd03231 78 LGHAPGIKTTLSVLENLR------------FWHADHS----DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLL 141
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEH 206
Cdd:cd03231 142 SGRPLWILDEPTTALDKAGVARFAEAMAGhCARGGMVVLTTH 183
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
7-240 |
1.52e-17 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 80.72 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEF---KGFV-AVNDVNLQIRQGDIHALIGPNGAGKTtvfnLLTKFL---IPTRGQIL---YRGEDITPLKSA 76
Cdd:COG4170 4 LDIRNLTIEIdtpQGRVkAVDRVSLTLNEGEIRGLVGESGSGKS----LIAKAIcgiTKDNWHVTadrFRWNGIDLLKLS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 77 AIARKGIVRSfQISAVF--------PHMTALENIRVALQTAEGSSySFWKSGNSLHKlneRCMELLESVG-------LAE 141
Cdd:COG4170 80 PRERRKIIGR-EIAMIFqepsscldPSAKIGDQLIEAIPSWTFKG-KWWQRFKWRKK---RAIELLHRVGikdhkdiMNS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 142 FANtttvELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRIT 219
Cdd:COG4170 155 YPH----ELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlqGTSILLISHDLESISQWADTIT 230
|
250 260
....*....|....*....|.
gi 504233768 220 VLAQGavltegdyQTVSADPR 240
Cdd:COG4170 231 VLYCG--------QTVESGPT 243
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
20-240 |
2.13e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 81.29 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGK-TTVFNLLTkfLIPTRGQILYRGEDITPLKSAAI--ARKGIVRSFQ--ISAVFP 94
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKsTTGLALLR--LINSQGEIWFDGQPLHNLNRRQLlpVRHRIQVVFQdpNSSLNP 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 95 HMTALENIRVALQTAEGSSysfwksgnSLHKLNERCMELLESVGL-AEFANTTTVELAYGRKRALELATTLAMEPQLLLL 173
Cdd:PRK15134 378 RLNVLQIIEEGLRVHQPTL--------SAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIIL 449
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 174 DEPTQGMGSEDVDRVVELVRKAAQGRTV--LMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:PRK15134 450 DEPTSSLDKTVQAQILALLKSLQQKHQLayLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQ 518
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-186 |
2.83e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.92 E-value: 2.83e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTvfnlLTKFLI--P----TRGQILYRGEDITPLK 74
Cdd:CHL00131 2 NKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKST----LSKVIAghPaykiLEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 75 SAAIARKGIVRSFQISAVFPH-------MTALENIRVALQTAEGSSYSFWksgnslhklnERCMELLESVGLAE-FANTT 146
Cdd:CHL00131 78 PEERAHLGIFLAFQYPIEIPGvsnadflRLAYNSKRKFQGLPELDPLEFL----------EIINEKLKLVGMDPsFLSRN 147
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504233768 147 TVE-LAYGRKRALELATTLAMEPQLLLLDEPTQGMgseDVD 186
Cdd:CHL00131 148 VNEgFSGGEKKRNEILQMALLDSELAILDETDSGL---DID 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-243 |
3.03e-17 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 78.66 E-value: 3.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQyVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKF--LIP---TRGQILYRGEDI-TPLK 74
Cdd:PRK14239 1 MTEP-ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNIySPRT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 75 SAAIARKGIVRSFQISAVFPhMTALENIRVALQTaegssysfwKSGNSLHKLNERCMELLESVGL----AEFANTTTVEL 150
Cdd:PRK14239 80 DTVDLRKEIGMVFQQPNPFP-MSIYENVVYGLRL---------KGIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 151 AYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
|
250
....*....|...
gi 504233768 231 DYQTVSADPRVRE 243
Cdd:PRK14239 230 DTKQMFMNPKHKE 242
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
21-230 |
3.86e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 79.07 E-value: 3.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIP---TRGQILYRGEDITPLKSAAIARK-GIVrsFQISavfphm 96
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKTVWDIREKvGIV--FQNP------ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 97 talENIRVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEP 176
Cdd:PRK13640 94 ---DNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDES 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 177 TQGMGSEDVDRVVELVRKaaqgrtvLMVEHNLSVVS--------KLCDRITVLAQGAVLTEG 230
Cdd:PRK13640 171 TSMLDPAGKEQILKLIRK-------LKKKNNLTVISithdideaNMADQVLVLDDGKLLAQG 225
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
6-240 |
6.65e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.08 E-value: 6.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFK---GFV-AVNDVNLQIRQGDIHALIGPNGAGKTtvfnLLTKFLIPTRGQIL------YRGEDITPLKS 75
Cdd:PRK15093 3 LLDIRNLTIEFKtsdGWVkAVDRVSMTLTEGEIRGLVGESGSGKS----LIAKAICGVTKDNWrvtadrMRFDDIDLLRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 76 AAIARKGIVRSfQISAVFPH----MTALENI-RVALQTAEGSSYS--FWKSGNSLHKlneRCMELLESVGLAEFAN---T 145
Cdd:PRK15093 79 SPRERRKLVGH-NVSMIFQEpqscLDPSERVgRQLMQNIPGWTYKgrWWQRFGWRKR---RAIELLHRVGIKDHKDamrS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 146 TTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQ 223
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQnnNTTILLISHDLQMLSQWADKINVLYC 234
|
250
....*....|....*..
gi 504233768 224 GavltegdyQTVSADPR 240
Cdd:PRK15093 235 G--------QTVETAPS 243
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
21-237 |
9.22e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 79.62 E-value: 9.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKGIVRSFQISAVFPHMTAlE 100
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL-RRNIAVVFQDAGLFNRSIE-D 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 101 NIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFA-------NTTTVE----LAYGRKRALELATTLAMEPQ 169
Cdd:PRK13657 428 NIRVGRPDAT----------------DEEMRAAAERAQAHDFIerkpdgyDTVVGErgrqLSGGERQRLAIARALLKDPP 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 170 LLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELMKGRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGSFDELVA 558
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
3-230 |
1.07e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 77.82 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 3 EQYVLETRNLV------KEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSA 76
Cdd:PRK13633 1 MNEMIKCKNVSykyesnEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 77 AIARK--GIVrsFQISavfphmtalENIRVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGR 154
Cdd:PRK13633 81 WDIRNkaGMV--FQNP---------DNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 155 KRALELATTLAMEPQLLLLDEPTQGM---GSEDV-DRVVELVRKaaQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEG 230
Cdd:PRK13633 150 KQRVAIAGILAMRPECIIFDEPTAMLdpsGRREVvNTIKELNKK--YGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
7-245 |
1.20e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 77.33 E-value: 1.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKgivrs 86
Cdd:PRK10253 8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARR----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 fqISAVFPHMTALENIRVALQTAEGSS-----YSFWKSGNSlhklnERCMELLESVGLAEFANTTTVELAYGRKRALELA 161
Cdd:PRK10253 83 --IGLLAQNATTPGDITVQELVARGRYphqplFTRWRKEDE-----EAVTKAMQATGITHLADQSVDTLSGGQRQRAWIA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 162 TTLAMEPQLLLLDEPTQGMG-SEDVDrVVELVRK--AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:PRK10253 156 MVLAQETAIMLLDEPTTWLDiSHQID-LLELLSElnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTA 234
|
....*..
gi 504233768 239 PRVREVY 245
Cdd:PRK10253 235 ELIERIY 241
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
23-226 |
2.61e-16 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 78.17 E-value: 2.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 23 NDVNLQIRQGDIHALIGPNGAGKTTVFNLLTkFLIPT----RGQILYRGEDITplKSAAIARKGIVRSFQIsaVFPHMTA 98
Cdd:TIGR00955 42 KNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKgvkgSGSVLLNGMPID--AKEMRAISAYVQQDDL--FIPTLTV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 99 LENIRValqTAEgssysfWKSGNSLHKLN--ERCMELLESVGLAEFANTTT------VELAYGRKRALELATTLAMEPQL 170
Cdd:TIGR00955 117 REHLMF---QAH------LRMPRRVTKKEkrERVDEVLQALGLRKCANTRIgvpgrvKGLSGGERKRLAFASELLTDPPL 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 171 LLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSV-VSKLCDRITVLAQGAV 226
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQkGKTIICTIHQPSSeLFELFDKIILMAEGRV 245
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
6-226 |
3.10e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 77.90 E-value: 3.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKefKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLtkFLIPTR--GQILYRGEDITPlKSAAIA-RKG 82
Cdd:PRK09700 265 VFEVRNVTS--RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCL--FGVDKRagGEIRLNGKDISP-RSPLDAvKKG 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 ---IVRSFQISAVFPHMTALENIRVALQTAEGSSYSFWKSGNSL--HKLNERCMELLeSVGLAEFaNTTTVELAYGRKRA 157
Cdd:PRK09700 340 mayITESRRDNGFFPNFSIAQNMAISRSLKDGGYKGAMGLFHEVdeQRTAENQRELL-ALKCHSV-NQNITELSGGNQQK 417
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:PRK09700 418 VLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQlADDGKVILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
6-233 |
3.97e-16 |
|
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: 78.13 E-value: 3.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFV--AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDItpLKSAAIARKGI 83
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI--LTNISDVHQNM 2014
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 84 VRSFQISAVFPHMTALENIRVALQTAEGSSYSFWKSGNSLhklnercmelLESVGLAEFANTTTVELAYGRKRALELATT 163
Cdd:TIGR01257 2015 GYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWS----------IQSLGLSLYADRLAGTYSGGNKRKLSTAIA 2084
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 164 LAMEPQLLLLDEPTQGMGSEDV----DRVVELVRkaaQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQ 233
Cdd:TIGR01257 2085 LIGCPPLVLLDEPTTGMDPQARrmlwNTIVSIIR---EGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQ 2155
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
24-233 |
5.66e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.46 E-value: 5.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-----GIVrsFQISAVFPHMTA 98
Cdd:PRK10535 26 GISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQLrrehfGFI--FQRYHLLSHLTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 99 LENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQ 178
Cdd:PRK10535 104 AQNVEVPAVYA----------GLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 179 GMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQ 233
Cdd:PRK10535 174 ALDSHSGEEVMAILHQlRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIVRNPPAQ 228
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
25-245 |
7.69e-16 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 74.88 E-value: 7.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 25 VNLQIRQGDIHALIGPNGAGKTTvfnLLTKF--LIPTRGQILYRGEDITPLKSAAIARkgiVRSF---QISAVFPhMTAL 99
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKST---LLARMagLLPGQGEILLNGRPLSDWSAAELAR---HRAYlsqQQSPPFA-MPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIRVALQtaegssysfwkSGNSLHKLNERCMELLESVGLAEFANTTTVELAYG---RKR----ALELATTLAMEPQLLL 172
Cdd:COG4138 88 QYLALHQP-----------AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGewqRVRlaavLLQVWPTINPEGQLLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 173 LDEPTQGMgseDV------DRVveLVRKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVREVY 245
Cdd:COG4138 157 LDEPMNSL---DVaqqaalDRL--LRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVF 230
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
6-207 |
1.13e-15 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 73.37 E-value: 1.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDIT-PLKSAAIARKGiv 84
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDdPDVAEACHYLG-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 rsfQISAVFPHMTALENIRvalqtaegssysFWKS--GNSLHKLnercMELLESVGLAEFANTTTVELAYGRKRALELAT 162
Cdd:PRK13539 80 ---HRNAMKPALTVAENLE------------FWAAflGGEELDI----AAALEAVGLAPLAHLPFGYLSAGQKRRVALAR 140
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVR-KAAQGRTVLMVEHN 207
Cdd:PRK13539 141 LLVSNRPIWILDEPTAALDAAAVALFAELIRaHLAQGGIVIAATHI 186
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-229 |
1.20e-15 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 76.20 E-value: 1.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 4 QYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDIT---PlKSAAIAR 80
Cdd:PRK10762 2 QALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngP-KSSQEAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 KGIVRsfQISAVFPHMTALENIRVALQTAEGSSYSFWKsgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:PRK10762 81 IGIIH--QELNLIPQLTIAENIFLGREFVNRFGRIDWK------KMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 161 ATTLAMEPQLLLLDEPTQGMG---SEDVDRVVELVRkaAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTE 229
Cdd:PRK10762 153 AKVLSFESKVIIMDEPTDALTdteTESLFRVIRELK--SQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
21-235 |
1.44e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 74.40 E-value: 1.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRK--GIV-----RSFQISAV- 92
Cdd:PRK13648 24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL-RKhiGIVfqnpdNQFVGSIVk 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 93 FPHMTALENIRValqtaegssysfwksgnSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLL 172
Cdd:PRK13648 103 YDVAFGLENHAV-----------------PYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 173 LDEPTQGMGSEDVDRVVELVRKAAQGR--TVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQTV 235
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHniTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
6-233 |
2.19e-15 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 75.49 E-value: 2.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQIlYRGEDITplksaaIArkgivr 85
Cdd:COG0488 315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV-KLGETVK------IG------ 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SF-QISAVF-PHMTALENIRvalQTAEGssysfwksGNSLHKLNercmeLLESVGLA-EFANTTTVELAYGRKRALELAT 162
Cdd:COG0488 382 YFdQHQEELdPDKTVLDELR---DGAPG--------GTEQEVRG-----YLGRFLFSgDDAFKPVGVLSGGEKARLALAK 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 163 TLAMEPQLLLLDEPTQGMgseDVD--RVVELVRKAAQGrTVLMVEHNLSVVSKLCDRITVLAQGAVLT-EGDYQ 233
Cdd:COG0488 446 LLLSPPNVLLLDEPTNHL---DIEtlEALEEALDDFPG-TVLLVSHDRYFLDRVATRILEFEDGGVREyPGGYD 515
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
6-225 |
2.34e-15 |
|
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: 72.85 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF-------KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYR-GEDITPLKSA- 76
Cdd:COG4778 4 LLEVENLSKTFtlhlqggKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRhDGGWVDLAQAs 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 77 -----AIARKGIVRSFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEfantttvEL- 150
Cdd:COG4778 84 preilALRRRTIGYVSQFLRVIPRVSALDVVAEPLLER----------GVDREEARARARELLARLNLPE-------RLw 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 151 -AY------GRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKA-AQGRTVLMVEHNLSVVSKLCDRITVLA 222
Cdd:COG4778 147 dLPpatfsgGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAkARGTAIIGIFHDEEVREAVADRVVDVT 226
|
...
gi 504233768 223 QGA 225
Cdd:COG4778 227 PFS 229
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-227 |
8.04e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 74.01 E-value: 8.04e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 3 EQYVLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKG 82
Cdd:NF033858 263 DEPAIEARGLTMRFGDFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVG 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 -IVRSFqisAVFPHMTALENIRvalqtaegssysfwksgnsLH---------KLNERCMELLESVGLAEFANTTTVELAY 152
Cdd:NF033858 343 yMSQAF---SLYGELTVRQNLE-------------------LHarlfhlpaaEIAARVAEMLERFDLADVADALPDSLPL 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 153 G-RKRaLELAttLAM--EPQLLLLDEPTQGmgsedVDRV---------VELVRKaaQGRTV-----LMVEhnlsvvSKLC 215
Cdd:NF033858 401 GiRQR-LSLA--VAVihKPELLILDEPTSG-----VDPVardmfwrllIELSRE--DGVTIfisthFMNE------AERC 464
|
250
....*....|..
gi 504233768 216 DRITVLAQGAVL 227
Cdd:NF033858 465 DRISLMHAGRVL 476
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
7-239 |
1.65e-14 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 72.06 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFK---GFV-AVNDVNLQIRQGDIHALIGPNGAGKT-TVFNLLTkfLIPTRGQI----LYRGEDITPLKSAA 77
Cdd:PRK09473 13 LDVKDLRVTFStpdGDVtAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMG--LLAANGRIggsaTFNGREILNLPEKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 78 IARkgiVRSFQISAVF--PhMTALEN-IRVALQTAE--------GSSYSFwksgnslhklnERCMELLESVGLAEFANTT 146
Cdd:PRK09473 91 LNK---LRAEQISMIFqdP-MTSLNPyMRVGEQLMEvlmlhkgmSKAEAF-----------EESVRMLDAVKMPEARKRM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 147 TV---ELAYGRKRALELATTLAMEPQLLLLDEPTQGMgseDVD---RVVELVR--KAAQGRTVLMVEHNLSVVSKLCDRI 218
Cdd:PRK09473 156 KMyphEFSGGMRQRVMIAMALLCRPKLLIADEPTTAL---DVTvqaQIMTLLNelKREFNTAIIMITHDLGVVAGICDKV 232
|
250 260
....*....|....*....|.
gi 504233768 219 TVLAQGAVLTEGDYQTVSADP 239
Cdd:PRK09473 233 LVMYAGRTMEYGNARDVFYQP 253
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
9-177 |
2.50e-14 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 72.40 E-value: 2.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 9 TRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEditplksaaiARKGIVRsfQ 88
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGYLP--Q 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 89 ISAVFPHMTALEN----------IRVALQTAEGSSYSFWKSGNSLHKLNE------------RCMELLESVGLAEFANTT 146
Cdd:COG0488 69 EPPLDDDLTVLDTvldgdaelraLEAELEELEAKLAEPDEDLERLAELQEefealggweaeaRAEEILSGLGFPEEDLDR 148
|
170 180 190
....*....|....*....|....*....|..
gi 504233768 147 TV-ELAYGRKRALELATTLAMEPQLLLLDEPT 177
Cdd:COG0488 149 PVsELSGGWRRRVALARALLSEPDLLLLDEPT 180
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
23-224 |
3.23e-14 |
|
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: 69.19 E-value: 3.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 23 NDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKfliptRGQILYRGEDITplksaaIARKGIVRSFQISAVF-PHMTALE- 100
Cdd:cd03232 24 NNISGYVKPGTLTALMGESGAGKTTLLDVLAG-----RKTAGVITGEIL------INGRPLDKNFQRSTGYvEQQDVHSp 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 101 --NIRVALQtaegssYSFWKSGNSLhklnercmellesvglaefantttvelaYGRKRaLELATTLAMEPQLLLLDEPTQ 178
Cdd:cd03232 93 nlTVREALR------FSALLRGLSV----------------------------EQRKR-LTIGVELAAKPSILFLDEPTS 137
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504233768 179 GMGSEDVDRVVELVRK-AAQGRTVLMVEHNLS-VVSKLCDRITVLAQG 224
Cdd:cd03232 138 GLDSQAAYNIVRFLKKlADSGQAILCTIHQPSaSIFEKFDRLLLLKRG 185
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
6-226 |
4.33e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 71.60 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNL-VKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIv 84
Cdd:COG3845 257 VLEVENLsVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLGV- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 rSF-----QISAVFPHMTALENIrvALQTAEGSSYS--FWKSGNSLHKLNERCMEllesvglaEFA-NTTTVELAYGR-- 154
Cdd:COG3845 336 -AYipedrLGRGLVPDMSVAENL--ILGRYRRPPFSrgGFLDRKAIRAFAEELIE--------EFDvRTPGPDTPARSls 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 155 ----KRALeLATTLAMEPQLLLLDEPTQGMgseDVdRVVELVRK-----AAQGRTVLMVEHNLSVVSKLCDRITVLAQGA 225
Cdd:COG3845 405 ggnqQKVI-LARELSRDPKLLIAAQPTRGL---DV-GAIEFIHQrllelRDAGAAVLLISEDLDEILALSDRIAVMYEGR 479
|
.
gi 504233768 226 V 226
Cdd:COG3845 480 I 480
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
21-240 |
6.86e-14 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 70.12 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAI--ARKGIVRSFQ--ISAVFPHM 96
Cdd:PRK15079 36 AVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWraVRSDIQMIFQdpLASLNPRM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 97 TALENIRVALQTaegssysfWKSGNSLHKLNERCMELLESVGLAE-FANTTTVELAYGRKRALELATTLAMEPQLLLLDE 175
Cdd:PRK15079 116 TIGEIIAEPLRT--------YHPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICDE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 176 PTQGMgseDVD---RVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:PRK15079 188 PVSAL---DVSiqaQVVNLLQQLQRemGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPL 254
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
22-233 |
8.20e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 8.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKGIVRSFQISAVFPHmTALEN 101
Cdd:PRK10247 23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY-RQQVSYCAQTPTLFGD-TVYDN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 102 IRVALQTaegssysfwksgNSLHKLNERCMELLESVGLAEFANTTTV-ELAYGRKRALELATTLAMEPQLLLLDEPTQGM 180
Cdd:PRK10247 101 LIFPWQI------------RNQQPDPAIFLDDLERFALPDTILTKNIaELSGGEKQRISLIRNLQFMPKVLLLDEITSAL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 181 GSEDVDRVVELVRKAA--QGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQ 233
Cdd:PRK10247 169 DESNKHNVNEIIHRYVreQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEARYE 223
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
10-224 |
8.58e-14 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 70.53 E-value: 8.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 10 RNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRSFQI 89
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALENGISMVHQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 90 SAVFPHMTALENIRVALQTAEGssySFWKSGnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQ 169
Cdd:PRK10982 82 LNLVLQRSVMDNMWLGRYPTKG---MFVDQD----KMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 170 LLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:PRK10982 155 IVIMDEPTSSLTEKEVNHLFTIIRKlKERGCGIVYISHKMEEIFQLCDEITILRDG 210
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
21-231 |
8.88e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 69.25 E-value: 8.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK-GIVrsFQ------ISAVF 93
Cdd:PRK13632 24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKiGII--FQnpdnqfIGATV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 94 PHMTA--LENIRVALQtaegssysfwksgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLL 171
Cdd:PRK13632 102 EDDIAfgLENKKVPPK-----------------KMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEII 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 172 LLDEPTQgM----GSEDVDRVVELVRKAAQgRTVLMVEHNLSVVSkLCDRITVLAQGAVLTEGD 231
Cdd:PRK13632 165 IFDESTS-MldpkGKREIKKIMVDLRKTRK-KTLISITHDMDEAI-LADKVIVFSEGKLIAQGK 225
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-237 |
9.51e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 70.52 E-value: 9.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLkSAAIARKGIVRSFQISAVFPHmTALENIR 103
Cdd:PRK10790 359 NINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL-SHSVLRQGVAMVQQDPVVLAD-TFLANVT 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 104 VALQTAEgssysfwksgnslhklnERCMELLESVGLAEFA-------NTTTVE----LAYGRKRALELATTLAMEPQLLL 172
Cdd:PRK10790 437 LGRDISE-----------------EQVWQALETVQLAELArslpdglYTPLGEqgnnLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 173 LDEPTQGMGS---EDVDRVVELVRKAAqgrTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:PRK10790 500 LDEATANIDSgteQAIQQALAAVREHT---TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQLLA 563
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
2-240 |
1.44e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 69.22 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 2 SEQYVLETRNLVKEF---KGFV-------AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDIt 71
Cdd:PRK11308 1 SQQPLLQAIDLKKHYpvkRGLFkperlvkALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 72 pLKSAAIARKGIVRSFQIsaVFphmtalenirvalQTAEGSSYSFWKSGNSLH-------KLN-----ERCMELLESVGL 139
Cdd:PRK11308 80 -LKADPEAQKLLRQKIQI--VF-------------QNPYGSLNPRKKVGQILEepllintSLSaaerrEKALAMMAKVGL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 140 -AEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMgseDVD---RVVELVRKAAQ--GRTVLMVEHNLSVVSK 213
Cdd:PRK11308 144 rPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL---DVSvqaQVLNLMMDLQQelGLSYVFISHDLSVVEH 220
|
250 260
....*....|....*....|....*..
gi 504233768 214 LCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:PRK11308 221 IADEVMVMYLGRCVEKGTKEQIFNNPR 247
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
6-206 |
1.93e-13 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 67.14 E-value: 1.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSaaiarkgivr 85
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQ--------ISAVFPHMTALENIRVALQTAEGSSysfwksgnslhklNERCMELLESVGLAEFANTTTVELAYGRKRA 157
Cdd:PRK13538 71 EYHqdllylghQPGIKTELTALENLRFYQRLHGPGD-------------DEALWEALAQVGLAGFEDVPVRQLSAGQQRR 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 158 LELATTLAMEPQLLLLDEP-----TQGmgsedVDRVVELV-RKAAQGRTVLMVEH 206
Cdd:PRK13538 138 VALARLWLTRAPLWILDEPftaidKQG-----VARLEALLaQHAEQGGMVILTTH 187
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
10-226 |
2.13e-13 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 69.29 E-value: 2.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 10 RNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQiLYRGE----DITPlksaaiARKGIVR 85
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGD-LFIGEkrmnDVPP------AERGVGM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:PRK11000 80 VFQSYALYPHLSVAENMSFGLKLA----------GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLV 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 166 MEPQLLLLDEPTQGMGSE-DVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:PRK11000 150 AEPSVFLLDEPLSNLDAAlRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
7-230 |
2.70e-13 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 68.61 E-value: 2.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTvFNLLTKFLIPTRGQILYRgeditpLKSAAIARKGIVRS 86
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWR------F*TWCANRRALRRT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 fqISAVFPhmtalenIRVALQTAEGSSYSFWKSGNSL----HKLNERCMELLESVGLAEFANTTTVELAYGRKRALELAT 162
Cdd:NF000106 87 --IG*HRP-------VR*GRRESFSGRENLYMIGR*LdlsrKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAA 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:NF000106 158 SMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRdGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-235 |
3.37e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.53 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 17 KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQilyrgeditplksaaIARKGIVRSFQISA-VFPH 95
Cdd:PRK13546 35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGK---------------VDRNGEVSVIAISAgLSGQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 96 MTALENIRvalqtaegssYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDE 175
Cdd:PRK13546 100 LTGIENIE----------FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDE 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 176 P----TQGMGSEDVDRVVELvrkAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTV 235
Cdd:PRK13546 170 AlsvgDQTFAQKCLDKIYEF---KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
22-226 |
4.98e-13 |
|
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: 65.32 E-value: 4.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKGIVRSFQISAVFPHmTALEN 101
Cdd:cd03246 18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL-GDHVGYLPQDDELFSG-SIAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 102 IrvalqtaegssysfwksgnslhklnercmellesvglaefantttveLAYGRKRALELATTLAMEPQLLLLDEPT---Q 178
Cdd:cd03246 96 I-----------------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNshlD 128
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504233768 179 GMGSEDVDRVVELVRKAaqGRTVLMVEHNLSVVsKLCDRITVLAQGAV 226
Cdd:cd03246 129 VEGERALNQAIAALKAA--GATRIVIAHRPETL-ASADRILVLEDGRV 173
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-245 |
6.38e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.49 E-value: 6.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 25 VNLQIRQGDIHALIGPNGAGKTTvfnLLTKF--LIPTRGQILYRGEDITPLKSAAIARKGIVRSFQISAVFP----HMTA 98
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKST---LLARMagLLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAmpvfQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 99 LEnirvalQTAEGSSYSfwksgnSLHKLNERCmellESVGLAEFANTTTVELAYG---RKR----ALELATTLAMEPQLL 171
Cdd:PRK03695 92 LH------QPDKTRTEA------VASALNEVA----EALGLDDKLGRSVNQLSGGewqRVRlaavVLQVWPDINPAGQLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 172 LLDEPTQGMgseDV------DRVVELVrkAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVREVY 245
Cdd:PRK03695 156 LLDEPMNSL---DVaqqaalDRLLSEL--CQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVF 230
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
6-226 |
7.08e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 67.74 E-value: 7.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNL-VKEfkgfvAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIV 84
Cdd:COG1129 256 VLEVEGLsVGG-----VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDAIRAGIA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 -----RsfQISAVFPHMTALENIRVALQTAegssysFWKSGN-SLHKLNERCMELLESVGLAefanTTTVELAYGR---- 154
Cdd:COG1129 331 yvpedR--KGEGLVLDLSIRENITLASLDR------LSRGGLlDRRRERALAEEYIKRLRIK----TPSPEQPVGNlsgg 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 155 ---KRALelATTLAMEPQLLLLDEPTQGmgsedVD-----RVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGA 225
Cdd:COG1129 399 nqqKVVL--AKWLATDPKVLILDEPTRG-----IDvgakaEIYRLIRElAAEGKAVIVISSELPELLGLSDRILVMREGR 471
|
.
gi 504233768 226 V 226
Cdd:COG1129 472 I 472
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
6-230 |
7.09e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 67.04 E-value: 7.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVN---LQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKg 82
Cdd:PRK13642 4 ILEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRK- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 ivrsfqISAVFPHMtalENIRVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELAT 162
Cdd:PRK13642 83 ------IGMVFQNP---DNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 163 TLAMEPQLLLLDEPTQGM---GSEDVDRVVELVRKAAQgRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEG 230
Cdd:PRK13642 154 IIALRPEIIILDESTSMLdptGRQEIMRVIHEIKEKYQ-LTVLSITHDLDEAAS-SDRILVMKAGEIIKEA 222
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
6-235 |
9.71e-13 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 65.97 E-value: 9.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLT---KFLIpTRGQILYRGEDITPLKSAAIARKG 82
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgreDYEV-TGGTVEFKGKDLLELSPEDRAGEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 83 IVRSFQ-------ISAVFPHMTALENIRVALQTAEGSSYSFwksgnslHKLNERCMELLEsvgLAEFANTTTVELAY--G 153
Cdd:PRK09580 80 IFMAFQypveipgVSNQFFLQTALNAVRSYRGQEPLDRFDF-------QDLMEEKIALLK---MPEDLLTRSVNVGFsgG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 154 RKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQG-RTVLMVEHNLSVVSKL-CDRITVLAQGAVLTEGD 231
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGkRSFIIVTHYQRILDYIkPDYVHVLYQGRIVKSGD 229
|
....
gi 504233768 232 YQTV 235
Cdd:PRK09580 230 FTLV 233
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
6-240 |
1.14e-12 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 65.88 E-value: 1.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGfVAVNDVNLQIRQGDIHALIGPNGAGKT----TVFNLLTKFLIPTRGQILYRGEDITP--LKSAAIA 79
Cdd:PRK10418 4 QIELRNIALQAAQ-PLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPcaLRGRKIA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 80 rkgIVRSFQISAVFPHMT----ALENIRVALQTAEgssysfwksgnslhklNERCMELLESVGLAEFANTTTV---ELAY 152
Cdd:PRK10418 83 ---TIMQNPRSAFNPLHTmhthARETCLALGKPAD----------------DATLTAALEAVGLENAARVLKLypfEMSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 153 GRKRALELATTLAMEPQLLLLDEPTQgmgseDVDRVV---------ELVRKAAQGrtVLMVEHNLSVVSKLCDRITVLAQ 223
Cdd:PRK10418 144 GMLQRMMIALALLCEAPFIIADEPTT-----DLDVVAqarildlleSIVQKRALG--MLLVTHDMGVVARLADDVAVMSH 216
|
250
....*....|....*..
gi 504233768 224 GAVLTEGDYQTVSADPR 240
Cdd:PRK10418 217 GRIVEQGDVETLFNAPK 233
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
25-229 |
1.35e-12 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 65.57 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 25 VNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPL---KSAAIARKGIVRSFQISAVFPHMTALEN 101
Cdd:PRK10584 29 VELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMdeeARAKLRAKHVGFVFQSFMLIPTLNALEN 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 102 IRV-ALQTAEGSSYSfwksgnslhklNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGM 180
Cdd:PRK10584 109 VELpALLRGESSRQS-----------RNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504233768 181 GSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKlCDRITVLAQGAVLTE 229
Cdd:PRK10584 178 DRQTGDKIADLLFSLNRehGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
11-218 |
1.48e-12 |
|
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: 63.62 E-value: 1.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 11 NLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILyRGEDITPlksaaiarkgivrsfqis 90
Cdd:cd03221 5 NLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVT-WGSTVKI------------------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 91 AVFPHMtalenirvalqtaegssysfwkSGnslhklnercmellesvglaefantttvelayGRKRALELATTLAMEPQL 170
Cdd:cd03221 66 GYFEQL----------------------SG--------------------------------GEKMRLALAKLLLENPNL 91
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 504233768 171 LLLDEPTQGMgseDVDRVVELVR--KAAQGrTVLMVEHNLSVVSKLCDRI 218
Cdd:cd03221 92 LLLDEPTNHL---DLESIEALEEalKEYPG-TVILVSHDRYFLDQVATKI 137
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-224 |
6.60e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 65.07 E-value: 6.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEfkGFVavnDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIV- 84
Cdd:PRK15439 268 VLTVEDLTGE--GFR---NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVy 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 --RSFQISAVFPHMTALENIrVALQTAEgssYSFWKSGNSLHKLNERCMELLeSVGLAEfANTTTVELAYGRKRALELAT 162
Cdd:PRK15439 343 lpEDRQSSGLYLDAPLAWNV-CALTHNR---RGFWIKPARENAVLERYRRAL-NIKFNH-AEQAARTLSGGNQQKVLIAK 416
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 163 TLAMEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:PRK15439 417 CLEASPQLLIVDEPTRGVDVSARNDIYQLIRSiAAQNVAVLFISSDLEEIEQMADRVLVMHQG 479
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
22-216 |
8.14e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 63.52 E-value: 8.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKF-----LIPTRGQILYRGEDITPlKSAAIARkgiVRSfQISAVFPH- 95
Cdd:PRK14258 23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYE-RRVNLNR---LRR-QVSMVHPKp 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 96 ----MTALENIrvalqtAEGSSYSFWKSGNSLHKLNERCM---ELLESVglAEFANTTTVELAYGRKRALELATTLAMEP 168
Cdd:PRK14258 98 nlfpMSVYDNV------AYGVKIVGWRPKLEIDDIVESALkdaDLWDEI--KHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 504233768 169 QLLLLDEPTQGM---GSEDVDRVVELVRKAAQgRTVLMVEHNLSVVSKLCD 216
Cdd:PRK14258 170 KVLLMDEPCFGLdpiASMKVESLIQSLRLRSE-LTMVIVSHNLHQVSRLSD 219
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-239 |
9.85e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.21 E-value: 9.85e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLEtrNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGeditPLKSAAIAR 80
Cdd:PRK09544 1 MTSLVSLE--NVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----KLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 KgivrsFQISAVFPhMTALENIRVALQTAEGSsysfwksgnslhklnerCMELLESVGLAEFANTTTVELAYGRKRALEL 160
Cdd:PRK09544 75 K-----LYLDTTLP-LTVNRFLRLRPGTKKED-----------------ILPALKRVQAGHLIDAPMQKLSGGETQRVLL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 161 ATTLAMEPQLLLLDEPTQGMgseDVDRVVELVRKAAQGRT-----VLMVEHNLSVVSKLCDRITVLAQgAVLTEGDYQTV 235
Cdd:PRK09544 132 ARALLNRPQLLVLDEPTQGV---DVNGQVALYDLIDQLRReldcaVLMVSHDLHLVMAKTDEVLCLNH-HICCSGTPEVV 207
|
....
gi 504233768 236 SADP 239
Cdd:PRK09544 208 SLHP 211
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-221 |
1.11e-11 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 64.42 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 30 RQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQIlyrgeditplkSAAIARKGIVRSFQISAVFPHMTAL--ENIRVAL- 106
Cdd:COG1245 97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDY-----------DEEPSWDEVLKRFRGTELQDYFKKLanGEIKVAHk 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 107 -QTAEGSSYSFwkSGNS---LHKLNERCM--ELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPT--- 177
Cdd:COG1245 166 pQYVDLIPKVF--KGTVrelLEKVDERGKldELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSsyl 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 504233768 178 ---QGMgsedvdRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVL 221
Cdd:COG1245 244 diyQRL------NVARLIRELAEeGKYVLVVEHDLAILDYLADYVHIL 285
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-239 |
1.39e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.88 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFK---GFV------AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEditPLKSA 76
Cdd:PRK15112 4 LLEVRNLSKTFRyrtGWFrrqtveAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 77 AIArkgiVRSFQISAVFPHMTALENIR----------VALQTAEGSSysfwksgnslhKLNERCMELLESVGL-AEFANT 145
Cdd:PRK15112 81 DYS----YRSQRIRMIFQDPSTSLNPRqrisqildfpLRLNTDLEPE-----------QREKQIIETLRQVGLlPDHASY 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 146 TTVELAYGRKRALELATTLAMEPQLLLLDEP----TQGMGSEDVDRVVELVRKaaQGRTVLMVEHNLSVVSKLCDRITVL 221
Cdd:PRK15112 146 YPHMLAPGQKQRLGLARALILRPKVIIADEAlaslDMSMRSQLINLMLELQEK--QGISYIYVTQHLGMMKHISDQVLVM 223
|
250
....*....|....*...
gi 504233768 222 AQGAVLTEGDYQTVSADP 239
Cdd:PRK15112 224 HQGEVVERGSTADVLASP 241
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
29-221 |
1.64e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 64.06 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 29 IRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQilYRGEDitplksaaiARKGIVRSFQISAVFPHMTALEN--IRVAL 106
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGD--YEEEP---------SWDEVLKRFRGTELQNYFKKLYNgeIKVVH 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 107 --QTAEGSSYSF-WKSGNSLHKLNERCM--ELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMg 181
Cdd:PRK13409 165 kpQYVDLIPKVFkGKVRELLKKVDERGKldEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL- 243
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 504233768 182 seDVD---RVVELVRKAAQGRTVLMVEHNLSVVSKLCDRITVL 221
Cdd:PRK13409 244 --DIRqrlNVARLIRELAEGKYVLVVEHDLAVLDYLADNVHIA 284
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
22-240 |
2.18e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 2.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKT-TVFNLLTkfLIPT------RGQILYRGEDItpLKSAAIARKGiVRSFQISAVFP 94
Cdd:PRK15134 25 VNDVSLQIEAGETLALVGESGSGKSvTALSILR--LLPSppvvypSGDIRFHGESL--LHASEQTLRG-VRGNKIAMIFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 95 H-MTALEnirvALQTAEGSSYSFWksgnSLHKLNER------CMELLESVGLAEFANTTTV---ELAYGRKRALELATTL 164
Cdd:PRK15134 100 EpMVSLN----PLHTLEKQLYEVL----SLHRGMRReaargeILNCLDRVGIRQAAKRLTDyphQLSGGERQRVMIAMAL 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 165 AMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPR 240
Cdd:PRK15134 172 LTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPT 249
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
22-230 |
4.76e-11 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 62.59 E-value: 4.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPT--RGQILYRGEDITplkSAAIARKGIVRsfQISAVFPHMTAL 99
Cdd:PLN03211 84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNnfTGTILANNRKPT---KQILKRTGFVT--QDDILYPHLTVR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIRVAlqtaegssySFWKSGNSLHKLNErcMELLESV----GLAEFANTTTVE-----LAYGRKRALELATTLAMEPQL 170
Cdd:PLN03211 159 ETLVFC---------SLLRLPKSLTKQEK--ILVAESViselGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSL 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 171 LLLDEPTQGMGSEDVDRVVE-LVRKAAQGRTVLMVEHNLSV-VSKLCDRITVLAQGAVLTEG 230
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLVLtLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
19-240 |
1.36e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 60.53 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 19 FVAVNDVNLQIRQGDIHALIGPNGAGKTtVFNLLTKFLIPTRG-----QILYRGEDITPLKSAAiaRKGIVRSfQISAVF 93
Cdd:PRK11022 20 FRAVDRISYSVKQGEVVGIVGESGSGKS-VSSLAIMGLIDYPGrvmaeKLEFNGQDLQRISEKE--RRNLVGA-EVAMIF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 94 PH-MTALE-------NIRVALQTAEGSSYSFWKsgnslhklnERCMELLESVGLAEFANTTTV---ELAYGRKRALELAT 162
Cdd:PRK11022 96 QDpMTSLNpcytvgfQIMEAIKVHQGGNKKTRR---------QRAIDLLNQVGIPDPASRLDVyphQLSGGMSQRVMIAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 163 TLAMEPQLLLLDEPTQGMG----SEDVDRVVELVRKaaQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSAD 238
Cdd:PRK11022 167 AIACRPKLLIADEPTTALDvtiqAQIIELLLELQQK--ENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRA 244
|
..
gi 504233768 239 PR 240
Cdd:PRK11022 245 PR 246
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
21-227 |
2.16e-10 |
|
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: 59.04 E-value: 2.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplksaAIARKGIVRSF----QISAVFPHm 96
Cdd:cd03244 19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDIS-----KIGLHDLRSRIsiipQDPVLFSG- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 97 TALENIrvalqtAEGSSYSfwksgnslhklNERCMELLESVGLAEFANT------TTVE-----LAYGRKRALELATTLA 165
Cdd:cd03244 93 TIRSNL------DPFGEYS-----------DEELWQALERVGLKEFVESlpggldTVVEeggenLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVL 227
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
21-230 |
2.34e-10 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 60.42 E-value: 2.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRSFQIsavfpHM---T 97
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTLASLRNQVALVSQNV-----HLfndT 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 98 ALENIRVAlQTAEGSSYSFWKSGNSLHklnerCMELLESV--GLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDE 175
Cdd:PRK11176 433 IANNIAYA-RTEQYSREQIEEAARMAY-----AMDFINKMdnGLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDE 506
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 176 PTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEG 230
Cdd:PRK11176 507 ATSALDTESERAIQAALDELQKNRTSLVIAHRLSTIEK-ADEILVVEDGEIVERG 560
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-237 |
3.44e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 59.90 E-value: 3.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGeditplkSAAIARKGivrsfqiSAVFPHMTALE 100
Cdd:PRK13545 39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-------SAALIAIS-------SGLNGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 101 NIRValqtaEGSSYSFWKSgnslhKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEP---- 176
Cdd:PRK13545 105 NIEL-----KGLMMGLTKE-----KIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEAlsvg 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 177 TQGMGSEDVDRVVELvrkAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSA 237
Cdd:PRK13545 175 DQTFTKKCLDKMNEF---KEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVD 232
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-230 |
4.80e-10 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 58.68 E-value: 4.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFL--------IPTRGQILYRGEDITPLKSAAIARKGIVRSFQISA 91
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggaprgARVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 92 VFPhMTALENIRValqtaeGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAM----- 166
Cdd:PRK13547 95 AFA-FSAREIVLL------GRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpph 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 167 ----EPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEG 230
Cdd:PRK13547 168 daaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
6-206 |
8.88e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 56.88 E-value: 8.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplKSAAIARKGIVR 85
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK--KDLCTYQKQLCF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAEGssysfwksgnslhklNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:PRK13540 79 VGHRSGINPYLTLRENCLYDIHFSPG---------------AVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWM 143
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 504233768 166 MEPQLLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEH 206
Cdd:PRK13540 144 SKAKLWLLDEPLVALDELSLLTIITKIQEhRAKGGAVLLTSH 185
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
29-220 |
8.90e-10 |
|
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: 57.42 E-value: 8.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 29 IRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITpLKSAAIARK--GIVRSFqisavfphmtaLENIrval 106
Cdd:cd03237 22 ISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS-YKPQYIKADyeGTVRDL-----------LSSI---- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 107 qTAEGSSYSFWKSgnslhklnercmELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVD 186
Cdd:cd03237 86 -TKDFYTHPYFKT------------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152
|
170 180 190
....*....|....*....|....*....|....*.
gi 504233768 187 RVVELVRKAAQG--RTVLMVEHNLSVVSKLCDRITV 220
Cdd:cd03237 153 MASKVIRRFAENneKTAFVVEHDIIMIDYLADRLIV 188
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
21-239 |
1.23e-09 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.19 E-value: 1.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAI-ARKGIVRsfQISAVFPHMTAl 99
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWrSRLAVVS--QTPFLFSDTVA- 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 100 ENIrvALQTAEGSSYSFWKSGNsLHKLNERCMELLEsvGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQG 179
Cdd:PRK10789 407 NNI--ALGRPDATQQEIEHVAR-LASVHDDILRLPQ--GYDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 180 MGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQTVSADP 239
Cdd:PRK10789 482 VDGRTEHQILHNLRQWGEGRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
13-226 |
1.26e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 58.00 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 13 VKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIV-----RSF 87
Cdd:PRK11288 260 LDGLKGPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAGIMlcpedRKA 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 88 QisAVFPHMTALENIRVAlqtaegSSYSFWKSGNSLHKLNERcmellesvGLAEF-----------ANTTTVELAYGRKR 156
Cdd:PRK11288 340 E--GIIPVHSVADNINIS------ARRHHLRAGCLINNRWEA--------ENADRfirslniktpsREQLIMNLSGGNQQ 403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 157 ALELATTLAMEPQLLLLDEPTQGMG----SEDVDRVVELvrkAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:PRK11288 404 KAILGRWLSEDMKVILLDEPTRGIDvgakHEIYNVIYEL---AAQGVAVLFVSSDLPEVLGVADRIVVMREGRI 474
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
8-211 |
2.00e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 57.81 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEFKGFVavndvnlqiRQGDIHALIGPNGAGKTTVFNLLTKFL---IPTRGQILYRGEditPLKSAAIARKGIV 84
Cdd:TIGR00956 774 EKRVILNNVDGWV---------KPGTLTALMGASGAGKTTLLNVLAERVttgVITGGDRLVNGR---PLDSSFQRSIGYV 841
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 RSFQIsavfpHMTALeNIRVALQTAegssySFWKSGNSLHKLN-----ERCMELLEsvgLAEFANTTTVELAYG-----R 154
Cdd:TIGR00956 842 QQQDL-----HLPTS-TVRESLRFS-----AYLRQPKSVSKSEkmeyvEEVIKLLE---MESYADAVVGVPGEGlnveqR 907
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 155 KRaLELATTLAMEPQLLL-LDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVV 211
Cdd:TIGR00956 908 KR-LTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADhGQAILCTIHQPSAI 965
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
6-220 |
7.54e-09 |
|
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: 55.95 E-value: 7.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVavndvnLQIRQGDIH-----ALIGPNGAGKTTVFNLLTKFLIPTRGQIlyrgedITPLKsaaIAR 80
Cdd:COG1245 341 LVEYPDLTKSYGGFS------LEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEV------DEDLK---ISY 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 81 KGivrsfQ-ISAVFPhMTALENIRVALQTAEGSSYsfWKS----GNSLHKLNERCMEllesvglaefantttvELAYGRK 155
Cdd:COG1245 406 KP-----QyISPDYD-GTVEEFLRSANTDDFGSSY--YKTeiikPLGLEKLLDKNVK----------------DLSGGEL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 156 RALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAA--QGRTVLMVEHNLSVVSKLCDRITV 220
Cdd:COG1245 462 QRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAenRGKTAMVVDHDIYLIDYISDRLMV 528
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
21-226 |
8.26e-09 |
|
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: 54.34 E-value: 8.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 21 AVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARK------------GIVRSFQ 88
Cdd:cd03369 23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSltiipqdptlfsGTIRSNL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 89 isAVFPHMTAlENIRVALQTAEGSSysfwksgnslhklnercmellesvglaefantttvELAYGRKRALELATTLAMEP 168
Cdd:cd03369 103 --DPFDEYSD-EEIYGALRVSEGGL-----------------------------------NLSQGQRQLLCLARALLKRP 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 169 QLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAV 226
Cdd:cd03369 145 RVLVLDEATASIDYATDALIQKTIREEFTNSTILTIAHRLRTIID-YDKILVMDAGEV 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
6-220 |
8.57e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 8.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAvnDVNL-QIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQIL------YRGEDITPlksaai 78
Cdd:PRK13409 340 LVEYPDLTKKLGDFSL--EVEGgEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDpelkisYKPQYIKP------ 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 79 ARKGIVRSFqisavfphmtaLENIRVALQTaegssySFWKSgnslhklnercmELLESVGLAEFANTTTVELAYGRKRAL 158
Cdd:PRK13409 412 DYDGTVEDL-----------LRSITDDLGS------SYYKS------------EIIKPLQLERLLDKNVKDLSGGELQRV 462
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 159 ELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGR--TVLMVEHNLSVVSKLCDRITV 220
Cdd:PRK13409 463 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEReaTALVVDHDIYMIDYISDRLMV 526
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
129-218 |
1.55e-08 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 54.16 E-value: 1.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 129 RCMELLESVGLAEFA---NTTTveLAYGRKRALELATTLAME---PQLLLLDEPTQGMGSEDVDRVVE-LVRKAAQGRTV 201
Cdd:cd03271 148 RKLQTLCDVGLGYIKlgqPATT--LSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEvLQRLVDKGNTV 225
|
90
....*....|....*..
gi 504233768 202 LMVEHNLSVVsKLCDRI 218
Cdd:cd03271 226 VVIEHNLDVI-KCADWI 241
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-243 |
2.15e-08 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.52 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 30 RQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQilYRGEDitplksaaiARKGIVRSFQISAVFPHMTALEN--IRVALQ 107
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPP---------DWDEILDEFRGSELQNYFTKLLEgdVKVIVK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 108 ---------TAEGssysfwKSGNSLHKLNERCM--ELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEP 176
Cdd:cd03236 93 pqyvdlipkAVKG------KVGELLKKKDERGKldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 177 TQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSVVSKLCDRITVLAQgavlTEGDYQTVSADPRVRE 243
Cdd:cd03236 167 SSYLDIKQRLNAARLIRELAEdDNYVLVVEHDLAVLDYLSDYIHCLYG----EPGAYGVVTLPKSVRE 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
36-176 |
2.37e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.93 E-value: 2.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 36 ALI--GPNGAGKTTVFNLLTKFLIPTRGQILYRGEditPLKSAAIARKgIVRSFQISAVFPHMTALENIRVAlqtaegss 113
Cdd:PRK13543 39 ALLvqGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRF-MAYLGHLPGLKADLSTLENLHFL-------- 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 114 ysfwksgNSLHKLNERCM--ELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEP 176
Cdd:PRK13543 107 -------CGLHGRRAKQMpgSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEP 164
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
7-175 |
2.62e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 54.21 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEF--KGFvAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIaRKgiv 84
Cdd:PRK10522 323 LELRNVTFAYqdNGF-SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDY-RK--- 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 85 rsfQISAVFP------HMTALENirvalQTAEGSSYSFWksgnsLHKLnercmELLESVGLAEFANTTTvELAYGRKRAL 158
Cdd:PRK10522 398 ---LFSAVFTdfhlfdQLLGPEG-----KPANPALVEKW-----LERL-----KMAHKLELEDGRISNL-KLSKGQKKRL 458
|
170
....*....|....*..
gi 504233768 159 ELATTLAMEPQLLLLDE 175
Cdd:PRK10522 459 ALLLALAEERDILLLDE 475
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-63 |
3.30e-08 |
|
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: 53.79 E-value: 3.30e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQI 63
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI 379
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
17-227 |
4.64e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 53.83 E-value: 4.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 17 KGFVAVNDVNLQIRQG---DIHAL------------IGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDitplksaaIARK 81
Cdd:PLN03232 1232 RGSIKFEDVHLRYRPGlppVLHGLsffvspsekvgvVGRTGAGKSSMLNALFRIVELEKGRIMIDDCD--------VAKF 1303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 82 GIVRSFQISAVFPHMTAL--ENIRVALQT-AEGSSYSFWKsgnSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRAL 158
Cdd:PLN03232 1304 GLTDLRRVLSIIPQSPVLfsGTVRFNIDPfSEHNDADLWE---ALERAHIKDVIDRNPFGLDAEVSEGGENFSVGQRQLL 1380
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 159 ELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVL 227
Cdd:PLN03232 1381 SLARALLRRSKILVLDEATASVDVRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
6-240 |
6.23e-08 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 53.32 E-value: 6.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEF-----------KGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLK 74
Cdd:PRK10261 313 ILQVRNLVTRFplrsgllnrvtREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLS 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 75 SAAIA--RKGIVRSFQ--ISAVFPHMTA----LENIRV-ALQTAEGSSysfwksgnslhklnERCMELLESVGL-AEFAN 144
Cdd:PRK10261 393 PGKLQalRRDIQFIFQdpYASLDPRQTVgdsiMEPLRVhGLLPGKAAA--------------ARVAWLLERVGLlPEHAW 458
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 145 TTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVLA 222
Cdd:PRK10261 459 RYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRdfGIAYLFISHDMAVVERISHRVAVMY 538
|
250
....*....|....*...
gi 504233768 223 QGAVLTEGDYQTVSADPR 240
Cdd:PRK10261 539 LGQIVEIGPRRAVFENPQ 556
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-242 |
1.09e-07 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 52.18 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQI------LY---RGEDITPLKSaaiaRKGIVrsFQISAVFP 94
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIvlngrvLFdaeKGICLPPEKR----RIGYV--FQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 95 HMTALENIRvalqtaegssYSFWKSGNSLHklnERCMELLesvGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLD 174
Cdd:PRK11144 90 HYKVRGNLR----------YGMAKSMVAQF---DKIVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504233768 175 EPtqgMGSEDVDRVVELV----RKAAQGRT-VLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVR 242
Cdd:PRK11144 154 EP---LASLDLPRKRELLpyleRLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAMR 223
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
128-224 |
1.42e-07 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 52.32 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 128 ERCMELLESVGLAEFA---NTTTveLAYGRKRALELATTL---AMEPQLLLLDEPTQGMGSEDVDRVVELV-RKAAQGRT 200
Cdd:TIGR00630 807 SRKLQTLCDVGLGYIRlgqPATT--LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLqRLVDKGNT 884
|
90 100 110
....*....|....*....|....*....|....*.
gi 504233768 201 VLMVEHNLSVVsKLCDRI------------TVLAQG 224
Cdd:TIGR00630 885 VVVIEHNLDVI-KTADYIidlgpeggdgggTVVASG 919
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
6-206 |
1.92e-07 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 51.87 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQIlYRGediTPLKSAaiarkgivr 85
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI-HCG---TKLEVA--------- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SF-QISAVF-PHMTALENIrvalqtAEGSSySFWKSGNSLHKLNErcmellesvgLAEF------ANTTTVELAYGRKRA 157
Cdd:PRK11147 386 YFdQHRAELdPEKTVMDNL------AEGKQ-EVMVNGRPRHVLGY----------LQDFlfhpkrAMTPVKALSGGERNR 448
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504233768 158 LELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVrKAAQGrTVLMVEH 206
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDVETLELLEELL-DSYQG-TVLLVSH 495
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-239 |
2.46e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.39 E-value: 2.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETRNLVKEFKG----FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQI-------LYRGED 69
Cdd:PRK10261 7 LDARDVLAVENLNIAFMQeqqkIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVqcdkmllRRRSRQ 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 70 ITPLKSAAIARKGIVRSFQISAVFPH-MTALENI-RVALQTAEGSSYSFWKSGNSLHKLNERCMELLESVGLAEFANTTT 147
Cdd:PRK10261 87 VIELSEQSAAQMRHVRGADMAMIFQEpMTSLNPVfTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILSRYP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 148 VELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQGRT--VLMVEHNLSVVSKLCDRITVLAQGA 225
Cdd:PRK10261 167 HQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMYQGE 246
|
250
....*....|....
gi 504233768 226 VLTEGDYQTVSADP 239
Cdd:PRK10261 247 AVETGSVEQIFHAP 260
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
22-224 |
2.75e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.08 E-value: 2.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVFNLLtkF-LIPTR--GQILYRGEDI---TPLKS--AAIA-------RKGIVrs 86
Cdd:PRK13549 278 VDDVSFSLRRGEILGIAGLVGAGRTELVQCL--FgAYPGRweGEIFIDGKPVkirNPQQAiaQGIAmvpedrkRDGIV-- 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 87 fqisavfPHMTALENIRVA-LQtaegsSYSFWKSGNSLHKLN--ERCMELLEsvglaefANTTTVELAYGR------KRA 157
Cdd:PRK13549 354 -------PVMGVGKNITLAaLD-----RFTGGSRIDDAAELKtiLESIQRLK-------VKTASPELAIARlsggnqQKA 414
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504233768 158 LeLATTLAMEPQLLLLDEPTQGMgseDVDRVVELVRK----AAQGRTVLMVEHNLSVVSKLCDRITVLAQG 224
Cdd:PRK13549 415 V-LAKCLLLNPKILILDEPTRGI---DVGAKYEIYKLinqlVQQGVAIIVISSELPEVLGLSDRVLVMHEG 481
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-268 |
3.48e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 3.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 26 NLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLksaaiarkgivrSFQ-----ISAVFPH----M 96
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRL------------SFEqlqklVSDEWQRnntdM 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 97 TALENIRVALQTAEGSSYSfwksgnslHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEP 176
Cdd:PRK10938 91 LSPGEDDTGRTTAEIIQDE--------VKDPARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 177 TQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTEGDYQTVSADPRVrevymgsdgsgerg 255
Cdd:PRK10938 163 FDGLDVASRQQLAELLASlHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALV-------------- 228
|
250
....*....|...
gi 504233768 256 SQAAASENVEAAQ 268
Cdd:PRK10938 229 AQLAHSEQLEGVQ 241
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
22-226 |
4.96e-07 |
|
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: 50.21 E-value: 4.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKT-TVFNLLTKFLIPTRGQILYRGEDI---TPLKS--AAIA-------RKGIVrsfq 88
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTeLVQALFGAYPGKFEGNVFINGKPVdirNPAQAirAGIAmvpedrkRHGIV---- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 89 isavfPHMTALENIRVALQtaegSSYSFWKSGNSLHKLN--ERCMELLESVGLAEFANTTTveLAYGRKRALELATTLAM 166
Cdd:TIGR02633 352 -----PILGVGKNITLSVL----KSFCFKMRIDAAAELQiiGSAIQRLKVKTASPFLPIGR--LSGGNQQKAVLAKMLLT 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 167 EPQLLLLDEPTQGMgseDVDRVVELVR----KAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:TIGR02633 421 NPRVLILDEPTRGV---DVGAKYEIYKlinqLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
6-53 |
5.10e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 5.10e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 504233768 6 VLETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLT 53
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMIT 371
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-63 |
6.94e-07 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 49.89 E-value: 6.94e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 7 LETRNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQI 63
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
150-239 |
8.83e-07 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 49.83 E-value: 8.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 150 LAYGRKRALELATTL---AMEPQLLLLDEPTQGMGSEDVDRVVELVRKAA-QGRTVLMVEHNLSVVsKLCDRITVLA-QG 224
Cdd:PRK00635 810 LSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLThQGHTVVIIEHNMHVV-KVADYVLELGpEG 888
|
90
....*....|....*
gi 504233768 225 AVLteGDYQTVSADP 239
Cdd:PRK00635 889 GNL--GGYLLASCSP 901
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
170-224 |
1.37e-06 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 49.30 E-value: 1.37e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 170 LLLLDEPTQGMGSEDVDRVVE-LVRKAAQGRTVLMVEHNLSVVsKLCDRI------------TVLAQG 224
Cdd:PRK00349 854 LYILDEPTTGLHFEDIRKLLEvLHRLVDKGNTVVVIEHNLDVI-KTADWIidlgpeggdgggEIVATG 920
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
22-265 |
1.76e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.82 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTvfnLLTKFLiptrgqilyrGEdITPLKSAAIARKGIVRSF-QISAVFpHMTALE 100
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTS---LISAML----------GE-LSHAETSSVVIRGSVAYVpQVSWIF-NATVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 101 NIrvaLQTAEGSSYSFWKSGNSLHKLNErcMELLESVGLAEFANtTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGM 180
Cdd:PLN03232 698 NI---LFGSDFESERYWRAIDVTALQHD--LDLLPGRDLTEIGE-RGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSAL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 181 GSEDVDRVVE-LVRKAAQGRTVLMVEHNLSVVSkLCDRITVLAQGAVLTEGDYQTVSADPRVREVYMgsDGSGERGSQAA 259
Cdd:PLN03232 772 DAHVAHQVFDsCMKDELKGKTRVLVTNQLHFLP-LMDRIILVSEGMIKEEGTFAELSKSGSLFKKLM--ENAGKMDATQE 848
|
....*.
gi 504233768 260 ASENVE 265
Cdd:PLN03232 849 VNTNDE 854
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
1-210 |
4.32e-06 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 47.92 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 1 MSEQYVLETR-NLVKEFKGfvavndvnlQIRQGDIHALIGPNGAGKTTVFNLL----TKFLIptRGQILYRGediTPLKS 75
Cdd:PLN03140 883 MKEQGVTEDRlQLLREVTG---------AFRPGVLTALMGVSGAGKTTLMDVLagrkTGGYI--EGDIRISG---FPKKQ 948
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 76 AAIAR-KGIVRSFQISAvfPHMTALENI------RVALQTAEGSSYSFWksgnslhklnERCMELLE-------SVGLAE 141
Cdd:PLN03140 949 ETFARiSGYCEQNDIHS--PQVTVRESLiysaflRLPKEVSKEEKMMFV----------DEVMELVEldnlkdaIVGLPG 1016
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 142 FANTTTVElaygRKRaLELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ-GRTVLMVEHNLSV 210
Cdd:PLN03140 1017 VTGLSTEQ----RKR-LTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDtGRTVVCTIHQPSI 1081
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
27-234 |
4.96e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 47.25 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 27 LQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDIT------PLKSAAiarkGIVRSF---QISAVFPHMT 97
Cdd:PRK11147 24 LHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVarlqqdPPRNVE----GTVYDFvaeGIEEQAEYLK 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 98 ALENI--RVALQTAEgssysfwKSGNSLHKLNE------------RCMELLESVGLAefANTTTVELAYGRKRALELATT 163
Cdd:PRK11147 100 RYHDIshLVETDPSE-------KNLNELAKLQEqldhhnlwqlenRINEVLAQLGLD--PDAALSSLSGGWLRKAALGRA 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504233768 164 LAMEPQLLLLDEPTQGMgseDVDRV--VELVRKAAQGrTVLMVEHNLSVVSKLCDRITVLAQGAVLT-EGDYQT 234
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHL---DIETIewLEGFLKTFQG-SIIFISHDRSFIRNMATRIVDLDRGKLVSyPGNYDQ 240
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-226 |
4.97e-06 |
|
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: 47.44 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIAR------------KGIVRsf 87
Cdd:COG4618 346 PILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRhigylpqdvelfDGTIA-- 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 88 qisavfphmtalENI---------RV--ALQTAegssysfwksgnslhklneRCMELLES--------VGLAEFAntttv 148
Cdd:COG4618 424 ------------ENIarfgdadpeKVvaAAKLA-------------------GVHEMILRlpdgydtrIGEGGAR----- 467
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504233768 149 eLAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKA-AQGRTVLMVEHNLSVVSkLCDRITVLAQGAV 226
Cdd:COG4618 468 -LSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALkARGATVVVITHRPSLLA-AVDKLLVLRDGRV 544
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
19-229 |
5.08e-06 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 46.10 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 19 FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIarkgivrsfqISAVFPHMTA 98
Cdd:COG2401 43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASL----------IDAIGRKGDF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 99 LEnirvalqtaegssysfwksgnslhklnerCMELLESVGLAEFAN--TTTVELAYGRKRALELATTLAMEPQLLLLDEP 176
Cdd:COG2401 113 KD-----------------------------AVELLNAVGLSDAVLwlRRFKELSTGQKFRFRLALLLAERPKLLVIDEF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 177 TQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLC-DRITVLAQGAVLTE 229
Cdd:COG2401 164 CSHLDRQTAKRVARNLQKLARraGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
170-224 |
5.58e-06 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 47.33 E-value: 5.58e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504233768 170 LLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSVVsKLCDRI------------TVLAQG 224
Cdd:COG0178 850 LYILDEPTTGLHFHDIRKLLEVLHRlVDKGNTVVVIEHNLDVI-KTADWIidlgpeggdgggEIVAEG 916
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
150-218 |
7.82e-06 |
|
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: 45.01 E-value: 7.82e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504233768 150 LAYGRKRALELATTLAMEPQ--LLLLDEPTQGMGSEDVDRVVELVRK-AAQGRTVLMVEHNLSvVSKLCDRI 218
Cdd:cd03238 88 LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVIKGlIDLGNTVILIEHNLD-VLSSADWI 158
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-225 |
8.30e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 46.75 E-value: 8.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 123 LHKLNERcMELLESVGLAEFA-NTTTVELAYGRKRALELATTLAMEPQ--LLLLDEPTQGMGSEDVDRVVELVRKAA-QG 198
Cdd:PRK00635 450 LQGLKSR-LSILIDLGLPYLTpERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKLRdQG 528
|
90 100
....*....|....*....|....*..
gi 504233768 199 RTVLMVEHNLSVVSkLCDRITVLAQGA 225
Cdd:PRK00635 529 NTVLLVEHDEQMIS-LADRIIDIGPGA 554
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
8-238 |
1.04e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.15 E-value: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEFKGfVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVrsf 87
Cdd:PRK10762 255 EVRLKVDNLSG-PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANGIV--- 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 88 QIS------AVFPHMTALENIRV-ALQtaegssySFWKSGNSLHKLNER---------------CMEllESVGLAEFANT 145
Cdd:PRK10762 331 YISedrkrdGLVLGMSVKENMSLtALR-------YFSRAGGSLKHADEQqavsdfirlfniktpSME--QAIGLLSGGNQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 146 TTVELAYGrkralelattLAMEPQLLLLDEPTQGMgseDV---DRVVELVRK-AAQGRTVLMVEHNLSVVSKLCDRITVL 221
Cdd:PRK10762 402 QKVAIARG----------LMTRPKVLILDEPTRGV---DVgakKEIYQLINQfKAEGLSIILVSSEMPEVLGMSDRILVM 468
|
250
....*....|....*..
gi 504233768 222 AQGAVltEGDYQTVSAD 238
Cdd:PRK10762 469 HEGRI--SGEFTREQAT 483
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
7-176 |
1.12e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.99 E-value: 1.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 7 LETRNLVKEFKG-FVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAiarKGIVR 85
Cdd:PRK11650 4 LKLQAVRKSYDGkTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---RDIAM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 86 SFQISAVFPHMTALENIRVALQTAegssysfwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYG-RKRalelattL 164
Cdd:PRK11650 81 VFQNYALYPHMSVRENMAYGLKIR----------GMPKAEIEERVAEAARILELEPLLDRKPRELSGGqRQR-------V 143
|
170
....*....|....*...
gi 504233768 165 AM------EPQLLLLDEP 176
Cdd:PRK11650 144 AMgraivrEPAVFLFDEP 161
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
167-229 |
4.53e-05 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 44.40 E-value: 4.53e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504233768 167 EPQLLLLDEPTQGMgseDVDRVVELV----RKAAQGRTVLMVEHNLSVVSKLCDRITVLAQGAVLTE 229
Cdd:NF040905 422 DPDVLILDEPTRGI---DVGAKYEIYtiinELAAEGKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-179 |
7.32e-05 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 43.96 E-value: 7.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 20 VAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITplkSAA--------IAR--KGIVRSfqi 89
Cdd:NF033858 15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA---DARhrravcprIAYmpQGLGKN--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 90 saVFPHMTALENI----RValqtaegssysFwksGNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLA 165
Cdd:NF033858 89 --LYPTLSVFENLdffgRL-----------F---GQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALI 152
|
170
....*....|....
gi 504233768 166 MEPQLLLLDEPTQG 179
Cdd:NF033858 153 HDPDLLILDEPTTG 166
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-226 |
7.64e-05 |
|
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: 43.78 E-value: 7.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDItplksAAIARKGIvrSFQISaVFPHMTALENIR 103
Cdd:TIGR00957 1304 HINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-----AKIGLHDL--RFKIT-IIPQDPVLFSGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 104 VALQTAEGSSYS---FWKSGNSLH----------KLNERCMELLESvglaefantttveLAYGRKRALELATTLAMEPQL 170
Cdd:TIGR00957 1376 LRMNLDPFSQYSdeeVWWALELAHlktfvsalpdKLDHECAEGGEN-------------LSVGQRQLVCLARALLRKTKI 1442
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 171 LLLDEPTQGMGSEDVDRVVELVRKAAQGRTVLMVEHNLSVVSKLCdRITVLAQGAV 226
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEV 1497
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
13-176 |
1.01e-04 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 43.07 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 13 VKEFKGFvavNDVNLQIrQGDIHALIGPNGAGKTTVFNLLTKFLiPTRGQILYRGEDITplksaaIARKGIVRSFQISAV 92
Cdd:COG3593 8 IKNFRSI---KDLSIEL-SDDLTVLVGENNSGKSSILEALRLLL-GPSSSRKFDEEDFY------LGDDPDLPEIEIELT 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 93 FP-----------HMTALENIRVALQTAEG--------------SSYSFWKSGNSLH-KLNERCMELLESVGLAEFANTT 146
Cdd:COG3593 77 FGsllsrllrlllKEEDKEELEEALEELNEelkealkalnellsEYLKELLDGLDLElELSLDELEDLLKSLSLRIEDGK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 504233768 147 TVELAY---GRKRALELATTLAM-------EPQLLLLDEP 176
Cdd:COG3593 157 ELPLDRlgsGFQRLILLALLSALaelkrapANPILLIEEP 196
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
36-226 |
1.80e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.54 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 36 ALIGPNGAGKTTVFNLLTKFLIPTRGQILyrgeditplksaaiaRKGIVRSfqisAVFP--HMTALEnirvaLQTAEGSS 113
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTVF---------------RSAKVRM----AVFSqhHVDGLD-----LSSNPLLY 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 114 YSFWKSGNSLHKLNERcmelLESVGLA-EFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMgseDVDRVVELV 192
Cdd:PLN03073 595 MMRCFPGVPEQKLRAH----LGSFGVTgNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHL---DLDAVEALI 667
|
170 180 190
....*....|....*....|....*....|....*.
gi 504233768 193 RKAA--QGrTVLMVEHNLSVVSKLCDRITVLAQGAV 226
Cdd:PLN03073 668 QGLVlfQG-GVLMVSHDEHLISGSVDELWVVSEGKV 702
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
8-239 |
2.52e-04 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 42.32 E-value: 2.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 8 ETRNLVKEFKgfvavnDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYrgEDITPLKSAAI----ARKGI 83
Cdd:PTZ00265 393 DTRKDVEIYK------DLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIII--NDSHNLKDINLkwwrSKIGV 464
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 84 VRsfQISAVFPH---------MTALENIRVALQTAEGSSYSFWKSGNSLHKLNERC-------MELLESVGLAEF-ANTT 146
Cdd:PTZ00265 465 VS--QDPLLFSNsiknnikysLYSLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCagdlndmSNTTDSNELIEMrKNYQ 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 147 TVE----------------------------------LAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELV 192
Cdd:PTZ00265 543 TIKdsevvdvskkvlihdfvsalpdkyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 504233768 193 R--KAAQGRTVLMVEHNLSVVsKLCDRITVLAQGAVLTEGDYQTVSADP 239
Cdd:PTZ00265 623 NnlKGNENRITIIIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIGEDP 670
|
|
| BCA_ABC_TP_C |
pfam12399 |
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in ... |
226-249 |
3.55e-04 |
|
Branched-chain amino acid ATP-binding cassette transporter; This domain family is found in bacteria, archaea and eukaryotes, and is approximately 30 amino acids in length. The family is found in association with pfam00005. There is a conserved AYLG sequence motif. This family is the C terminal of an ATP dependent branched-chain amino acid transporter. This domain is essential for LPS transport, through critical interactions with Walker A and switch helix domains.
Pssm-ID: 463560 Cd Length: 25 Bit Score: 36.85 E-value: 3.55e-04
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
36-208 |
5.58e-04 |
|
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: 39.65 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 36 ALIGPNGAGKTTVFNLlTKFLIPTRGQILYRGEDITP-LKSAAIARKGIVRSFQISAVFPHMTALENIrvalqtaegssy 114
Cdd:cd03227 25 IITGPNGSGKSTILDA-IGLALGGAQSATRRRSGVKAgCIVAAVSAELIFTRLQLSGGEKELSALALI------------ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 115 sfwksgnslhklnercmellesVGLAEFANTTtvelaygrkralelattlamepqLLLLDEPTQGMGSEDVDRVVELVRK 194
Cdd:cd03227 92 ----------------------LALASLKPRP-----------------------LYILDEIDRGLDPRDGQALAEAILE 126
|
170
....*....|....*
gi 504233768 195 -AAQGRTVLMVEHNL 208
Cdd:cd03227 127 hLVKGAQVIVITHLP 141
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-249 |
1.39e-03 |
|
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: 39.45 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEditplksaaiarkgIVRSFQISAVFPHmTALENIR 103
Cdd:cd03291 55 NINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR--------------ISFSSQFSWIMPG-TIKENII 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 104 ValqtaeGSSYSFWKsgnslHKLNERCMELLESVG-LAEFANTTTVE----LAYGRKRALELATTLAMEPQLLLLDEPtq 178
Cdd:cd03291 120 F------GVSYDEYR-----YKSVVKACQLEEDITkFPEKDNTVLGEggitLSGGQRARISLARAVYKDADLYLLDSP-- 186
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 179 gMGSEDVDRVVEL----VRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQTV-SADPRVREVYMGSD 249
Cdd:cd03291 187 -FGYLDVFTEKEIfescVCKLMANKTRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSELqSLRPDFSSKLMGYD 260
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
10-206 |
1.62e-03 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 39.61 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 10 RNLVKEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNL------------LTKFliptrGQILYRGEDITPLK--- 74
Cdd:PRK10938 264 NNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLitgdhpqgysndLTLF-----GRRRGSGETIWDIKkhi 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 75 ---SAAIA---RKGI-VRSFQISAVFphmtalENIRVALQTAEgssysfwksgnslhKLNERCMELLESVGL-AEFANTT 146
Cdd:PRK10938 339 gyvSSSLHldyRVSTsVRNVILSGFF------DSIGIYQAVSD--------------RQQKLAQQWLDILGIdKRTADAP 398
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 147 TVELAYGRKRALELATTLAMEPQLLLLDEPTQGMgsEDVDRvvELVRK-----AAQGRT-VLMVEH 206
Cdd:PRK10938 399 FHSLSWGQQRLALIVRALVKHPTLLILDEPLQGL--DPLNR--QLVRRfvdvlISEGETqLLFVSH 460
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-265 |
1.64e-03 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 39.72 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTvfnLLTKFLiptrgqilyrGEdITPLKSAAIARKGIVRSF-QISAVFpHMTALENI 102
Cdd:PLN03130 635 NINLDVPVGSLVAIVGSTGEGKTS---LISAML----------GE-LPPRSDASVVIRGTVAYVpQVSWIF-NATVRDNI 699
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 103 rvaLQTAEGSSYSFWKS--GNSLHklneRCMELLESVGLAEFANtTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGM 180
Cdd:PLN03130 700 ---LFGSPFDPERYERAidVTALQ----HDLDLLPGGDLTEIGE-RGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSAL 771
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 181 GSEdVDRVV--ELVRKAAQGRTVLMVEHNLSVVSKLcDRITVLAQGAVLTEGDYQTVSADPRVREVYMGSDGSGERGSQA 258
Cdd:PLN03130 772 DAH-VGRQVfdKCIKDELRGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNNGPLFQKLMENAGKMEEYVEE 849
|
....*..
gi 504233768 259 AASENVE 265
Cdd:PLN03130 850 NGEEEDD 856
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
24-211 |
1.69e-03 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 38.70 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEDITPLKSAAIARKGIVRSFQISavfphMTALENIR 103
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLGLKLE-----MTVFENLK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 104 valqtaegssysFWksgNSLHKLNERCMELLESVGLAEFANTTTVELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSE 183
Cdd:PRK13541 93 ------------FW---SEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKE 157
|
170 180
....*....|....*....|....*....
gi 504233768 184 DVDRVVEL-VRKAAQGRTVLMVEHNLSVV 211
Cdd:PRK13541 158 NRDLLNNLiVMKANSGGIVLLSSHLESSI 186
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
18-209 |
1.82e-03 |
|
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: 39.35 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 18 GFVAVNDVNLQIRQGDiHALI-GPNGAGKTTVFNLLTKF--------LIPTRGQILY------------RGEDITPLKSA 76
Cdd:TIGR00954 464 GDVLIESLSFEVPSGN-NLLIcGPNGCGKSSLFRILGELwpvyggrlTKPAKGKLFYvpqrpymtlgtlRDQIIYPDSSE 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 77 AIARKGIVRSfqisavfphmtALENIRVALQtaegssysfwksgnsLHKLNERcmelleSVGLAEFANTTTVeLAYGRKR 156
Cdd:TIGR00954 543 DMKRRGLSDK-----------DLEQILDNVQ---------------LTHILER------EGGWSAVQDWMDV-LSGGEKQ 589
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 504233768 157 ALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAaqGRTVLMVEHNLS 209
Cdd:TIGR00954 590 RIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCREF--GITLFSVSHRKS 640
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
148-221 |
2.48e-03 |
|
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: 37.94 E-value: 2.48e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504233768 148 VELAYGRKRALELATTLAMEPQLLLLDEPTQGMGSEDVDRVVELVRKAAQ--GRTVLMVEHNLSVVSKLCDRITVL 221
Cdd:cd03222 70 IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEegKKTALVVEHDLAVLDYLSDRIHVF 145
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
14-67 |
2.56e-03 |
|
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: 38.22 E-value: 2.56e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 504233768 14 KEFKGFVAVNDVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRG 67
Cdd:cd03250 13 GEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG 66
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
24-254 |
3.29e-03 |
|
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: 38.74 E-value: 3.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 24 DVNLQIRQGDIHALIGPNGAGKTTVFNLLTKFLIPTRGQILYRGEditplksaaiarkgIVRSFQISAVFPHmTALENIR 103
Cdd:TIGR01271 444 NISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR--------------ISFSPQTSWIMPG-TIKDNII 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 104 VALQTAEGSSYSFWKSgnslhklnerCmELLESVG-LAEFANTTTVE----LAYGRKRALELATTLAMEPQLLLLDEPtq 178
Cdd:TIGR01271 509 FGLSYDEYRYTSVIKA----------C-QLEEDIAlFPEKDKTVLGEggitLSGGQRARISLARAVYKDADLYLLDSP-- 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504233768 179 gMGSEDVDRVVEL----VRKAAQGRTVLMVEHNLSVVSKlCDRITVLAQGAVLTEGDYQTVSAD-PRVREVYMGSDG--- 250
Cdd:TIGR01271 576 -FTHLDVVTEKEIfescLCKLMSNKTRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSELQAKrPDFSSLLLGLEAfdn 653
|
....*
gi 504233768 251 -SGER 254
Cdd:TIGR01271 654 fSAER 658
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
22-49 |
5.26e-03 |
|
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: 36.75 E-value: 5.26e-03
10 20
....*....|....*....|....*...
gi 504233768 22 VNDVNLQIRQGDIHALIGPNGAGKTTVF 49
Cdd:cd03223 17 LKDLSFEIKPGDRLLITGPSGTGKSSLF 44
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
150-221 |
5.28e-03 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 38.09 E-value: 5.28e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504233768 150 LAYGRKRALELATTLAMEPQLLLLDEPTQGMGSED---VDRVVELVRKAAQgRTVLMVEHNLSVVsKLCDRITVL 221
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSeklIEKTIVDIKDKAD-KTIITIAHRIASI-KRSDKIVVF 1431
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
13-56 |
5.59e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 37.28 E-value: 5.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 504233768 13 VKEFKGFVavndvNLQI---RQGDIHALIGPNGAGKTTVFNLLTKFL 56
Cdd:COG3950 8 IENFRGFE-----DLEIdfdNPPRLTVLVGENGSGKTTLLEAIALAL 49
|
|
| COG4637 |
COG4637 |
Predicted ATPase [General function prediction only]; |
13-56 |
9.11e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443675 [Multi-domain] Cd Length: 371 Bit Score: 36.83 E-value: 9.11e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 504233768 13 VKEFKGFVAVnDVNLqirqGDIHALIGPNGAGKTTVFNLLtKFL 56
Cdd:COG4637 7 IKNFKSLRDL-ELPL----GPLTVLIGANGSGKSNLLDAL-RFL 44
|
|
| |
