|
Name |
Accession |
Description |
Interval |
E-value |
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-221 |
1.45e-134 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 377.08 E-value: 1.45e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG1136 84 RRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:COG1136 164 KLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-218 |
1.29e-124 |
|
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: 351.41 E-value: 1.29e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVR 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIVIRDGNV 218
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELAEYADRIIELRDGKI 218
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-221 |
1.56e-100 |
|
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: 291.26 E-value: 1.56e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:COG4181 8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFMLLPRLTALQNVELPLIYAGVdkKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG4181 88 RARHVGFVFQSFQLLPTLTALENVMLPLELAGR--RDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:COG4181 166 AILFADEPTGNLDAATGEQIIDLLFELNReRGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-224 |
5.63e-99 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 286.56 E-value: 5.63e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAEsvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG2884 78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAA-ARQIVIRDGNVVQDWRG 224
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMpKRVLELEDGRLVRDEAR 221
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-221 |
4.64e-89 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 275.06 E-value: 4.64e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:PRK10535 4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:PRK10535 84 RREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRN 224
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-223 |
3.39e-83 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 248.08 E-value: 3.39e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNmsetelahv 80
Cdd:COG1116 7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG--------- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG1116 78 PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDreIGEAA--ARQIVI---RDGNVVQDWR 223
Cdd:COG1116 158 EVLLMDEPFGALDALTRERLQDELLRLwQETGKTVLFVTHD--VDEAVflADRVVVlsaRPGRIVEEID 224
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-219 |
3.01e-82 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 248.45 E-value: 3.01e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG1135 81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD----REIGEAAArqiVIRDGNVV 219
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRElGLTIVLITHEmdvvRRICDRVA---VLENGRIV 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-219 |
1.56e-79 |
|
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: 237.86 E-value: 1.56e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:cd03258 81 R-RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEAAARQIVIRDGNVV 219
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRElGLTIVLITHEMEvVKRICDRVAVMEKGEVV 220
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-223 |
1.14e-78 |
|
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: 235.06 E-value: 1.14e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNmsetelahvR 81
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03293 72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDreIGEAA--ARQIVI---RDGNVVQDWR 223
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIwRETGKTVLLVTHD--IDEAVflADRVVVlsaRPGRIVAEVE 217
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
1-216 |
2.17e-76 |
|
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]
Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 229.06 E-value: 2.17e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:TIGR02673 1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:TIGR02673 78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEA-AARQIVIRDG 216
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLVDRvAHRVIILDDG 213
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-221 |
1.57e-74 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 225.26 E-value: 1.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsNMSETELAHV 80
Cdd:COG1126 1 MIEIENLHKSF----GDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNVELPLIYA-GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNN 159
Cdd:COG1126 76 R-RKVGMVFQQFNLFPHLTVLENVTLAPIKVkKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 160 PKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHdrEIG---EAAARQIVIRDGNVVQD 221
Cdd:COG1126 155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKEGMTMVVVTH--EMGfarEVADRVVFMDGGRIVEE 217
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-221 |
8.61e-74 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 223.78 E-value: 8.61e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:COG3638 2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNV------ELPLIYA--GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAV 152
Cdd:COG3638 79 R-RRIGMIFQQFNLVPRLSVLTNVlagrlgRTSTWRSllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 153 ARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHDREIGEA-AARQIVIRDGNVVQD 221
Cdd:COG3638 158 ARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAReDGITVVVNLHQVDLARRyADRIIGLRDGRVVFD 228
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-218 |
1.82e-72 |
|
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: 219.20 E-value: 1.82e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVR 81
Cdd:cd03292 1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03292 78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAA-RQIVIRDGNV 218
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRhRVIALERGKL 214
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
2-216 |
1.98e-71 |
|
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly in the Cyanobacteria, but also in the Planctomycetes. Cyanobacterial examples are involved in heterocyst formation, by which some fraction of members of the colony undergo a developmental change and become capable of nitrogen fixation. The DevBCA proteins are thought export of either heterocyst-specific glycolipids or an enzyme essential for formation of the laminated layer found in heterocysts.
Pssm-ID: 274374 [Multi-domain] Cd Length: 220 Bit Score: 216.81 E-value: 1.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVR 81
Cdd:TIGR02982 2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRLTALQNVELPL-IYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:TIGR02982 82 -RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHDREIGEAAARQIVIRDG 216
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKeQGCTILMVTHDNRILDVADRILQMEDG 217
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-219 |
4.01e-71 |
|
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: 216.77 E-value: 4.01e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:COG1127 5 MIEVRNLTKSF----GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNVELPLI-YAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNN 159
Cdd:COG1127 81 R-RRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531755 160 PKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:COG1127 160 PEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDlDSAFAIADRVAVLADGKII 221
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
7-221 |
9.49e-71 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 215.45 E-value: 9.49e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 7 ITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEIG 86
Cdd:PRK11629 11 LCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 87 FVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILAD 166
Cdd:PRK11629 91 FIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 167 EPTGALDTKTSTQIMDLFYELN-KQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:PRK11629 171 EPTGNLDARNADSIFQLLGELNrLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAE 226
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-220 |
8.76e-70 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 216.89 E-value: 8.76e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelAHV 80
Cdd:COG3842 5 ALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----PEK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNkeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG3842 77 RN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREigEAAA---RQIVIRDGNVVQ 220
Cdd:COG3842 155 RVLLLDEPLSALDAKLREEMREELRRLQRElGITFIYVTHDQE--EALAladRIAVMNDGRIEQ 216
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
4-213 |
1.20e-69 |
|
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]
Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 211.71 E-value: 1.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNK 83
Cdd:TIGR03608 1 LKNISKKFGD----KVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFI 163
Cdd:TIGR03608 77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446531755 164 LADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVI 213
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVIEL 206
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-219 |
1.14e-68 |
|
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: 210.05 E-value: 1.14e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhV 80
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRK-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFM--LLPRLTALQNVELPLIYAGVDKKE--RRERSLAALTKVGL-ADRATHLPNELSGGQKQRVAVARA 155
Cdd:cd03257 80 RRKEIQMVFQDPMssLNPRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 156 IVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD----REIgeaAARQIVIRDGNVV 219
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDlgvvAKI---ADRVAVMYAGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-219 |
3.07e-68 |
|
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: 217.85 E-value: 3.07e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSF-QNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAH 79
Cdd:COG1123 260 LLEVRNLSKRYpVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRnKEIGFVFQN--FMLLPRLTALQNVELPL-IYAGVDKKERRERSLAALTKVGL-ADRATHLPNELSGGQKQRVAVARA 155
Cdd:COG1123 340 LR-RRVQMVFQDpySSLNPRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 156 IVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD----REIgeaAARQIVIRDGNVV 219
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDlavvRYI---ADRVAVMYDGRIV 484
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-216 |
2.79e-67 |
|
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: 205.84 E-value: 2.79e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNmSETELAHVR 81
Cdd:cd03262 1 IEIKNLHKSFGD----FHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRLTALQNVELPLIYA-GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:cd03262 76 -QKVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHdrEIG---EAAARQIVIRDG 216
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTH--EMGfarEVADRVIFMDDG 211
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-220 |
1.05e-66 |
|
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: 204.68 E-value: 1.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelAHVRNk 83
Cdd:cd03259 3 LKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVP----PERRN- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 eIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFI 163
Cdd:cd03259 74 -IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 164 LADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDREigEAAA---RQIVIRDGNVVQ 220
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELqRELGITTIYVTHDQE--EALAladRIAVMNEGRIVQ 211
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-219 |
1.11e-66 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 208.89 E-value: 1.11e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:PRK11153 1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:PRK11153 81 RRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEAAARQIVIRDGNVV 219
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRElGLTIVLITHEMDvVKRICDRVAVIDAGRLV 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
7-216 |
2.09e-66 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 204.24 E-value: 2.09e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 7 ITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEIG 86
Cdd:PRK10584 12 LKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 87 FVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILAD 166
Cdd:PRK10584 92 FVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446531755 167 EPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHDREIGEAAARQIVIRDG 216
Cdd:PRK10584 172 EPTGNLDRQTGDKIADLLFSLNReHGTTLILVTHDLQLAARCDRRLRLVNG 222
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-220 |
6.27e-66 |
|
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: 204.41 E-value: 6.27e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVQILHGI------------------DVTL--NQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGT 61
Cdd:cd03294 1 IKIKGLYKIFGKNPQKAFKLLAKgkskeeilkktgqtvgvnDVSLdvREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 62 YELAGQNISNMSETELAHVRNKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNE 141
Cdd:cd03294 81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELN-KQGSTIIMITHDREigEA---AARQIVIRDGN 217
Cdd:cd03294 161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQaELQKTIVFITHDLD--EAlrlGDRIAIMKDGR 238
|
...
gi 446531755 218 VVQ 220
Cdd:cd03294 239 LVQ 241
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
2-221 |
2.06e-65 |
|
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: 201.79 E-value: 2.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvr 81
Cdd:COG1122 1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQN-----FMLlprlTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAI 156
Cdd:COG1122 75 -RKVGLVFQNpddqlFAP----TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVL 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVVQD 221
Cdd:COG1122 150 AMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDlDLVAELADRVIVLDDGRIVAD 215
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
2-221 |
3.10e-65 |
|
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: 201.64 E-value: 3.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVR 81
Cdd:cd03256 1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRLTALQNV------ELPLIYA--GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVA 153
Cdd:cd03256 78 -RQIGMIFQQFNLIERLSVLENVlsgrlgRRSTWRSlfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIV-IRDGNVVQD 221
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLAREYADRIVgLKDGRIVFD 226
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-216 |
1.68e-64 |
|
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: 198.85 E-value: 1.68e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGAEsvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnK 83
Cdd:cd03225 2 LKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQN-----FMLlprlTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVN 158
Cdd:cd03225 76 KVGLVFQNpddqfFGP----TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 159 NPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDRE-IGEAAARQIVIRDG 216
Cdd:cd03225 152 DPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDlLLELADRVIVLEDG 210
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-200 |
3.34e-63 |
|
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: 199.12 E-value: 3.34e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLDKP--TTGTYELAGQNISNMSETEL 77
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 78 AHVRNKEIGFVFQNFM--LLPRLTALQNVELPL-IYAGVDKKERRERSLAALTKVGLADRATHL---PNELSGGQKQRVA 151
Cdd:COG0444 81 RKIRGREIQMIFQDPMtsLNPVMTVGDQIAEPLrIHGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQRVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446531755 152 VARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD 200
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHD 210
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-219 |
3.89e-63 |
|
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: 196.18 E-value: 3.89e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVR 81
Cdd:cd03261 1 IELRGLTKSF----GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKER-RERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:cd03261 77 -RRMGMLFQSGALFDSLTVFENVAFPLREHTRLSEEEiREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:cd03261 156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDlDTAFAIADRIAVLYDGKIV 216
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-221 |
6.70e-63 |
|
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]
Pssm-ID: 131368 [Multi-domain] Cd Length: 243 Bit Score: 195.98 E-value: 6.70e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:TIGR02315 1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKeIGFVFQNFMLLPRLTALQNVELPLIYA--------GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAV 152
Cdd:TIGR02315 78 RRR-IGMIFQHYNLIERLTVLENVLHGRLGYkptwrsllGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 153 ARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIV-IRDGNVVQD 221
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEdGITVIINLHQVDLAKKYADRIVgLKAGEIVFD 227
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-221 |
7.98e-63 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 195.70 E-value: 7.98e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsNMSETELAHV 80
Cdd:PRK09493 1 MIEFKNVSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNVEL-PLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNN 159
Cdd:PRK09493 76 R-QEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 160 PKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHdrEIGEA---AARQIVIRDGNVVQD 221
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH--EIGFAekvASRLIFIDKGRIAED 217
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-221 |
6.06e-61 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 190.66 E-value: 6.06e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmseTELAHVR 81
Cdd:COG1131 1 IEVRGLTKRYGD----KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVA----RDPAEVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:COG1131 73 -RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVVQD 221
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYlEEAERLCDRVAIIDKGRIVAD 212
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-220 |
8.53e-61 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 194.14 E-value: 8.53e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETElahv 80
Cdd:COG3839 3 SLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNkeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG3839 75 RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 161 KFILADEPTGALDTK----TSTQIMDLFYELnkqGSTIIMITHDREigEA---AARQIVIRDGNVVQ 220
Cdd:COG3839 153 KVFLLDEPLSNLDAKlrveMRAEIKRLHRRL---GTTTIYVTHDQV--EAmtlADRIAVMNDGRIQQ 214
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-220 |
1.09e-59 |
|
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: 187.44 E-value: 1.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMseteLAHVR 81
Cdd:cd03300 1 IELENVSKFY----GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNL----PPHKR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NkeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03300 73 P--VNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREigEAAA---RQIVIRDGNVVQ 220
Cdd:cd03300 151 VLLLDEPLGALDLKLRKDMQLELKRLQKElGITFVFVTHDQE--EALTmsdRIAVMNKGKIQQ 211
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-212 |
7.62e-59 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 186.22 E-value: 7.62e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelahv 80
Cdd:COG4525 3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 rnKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG4525 76 --ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADP 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDREigEA---AARQIV 212
Cdd:COG4525 154 RFLLMDEPFGALDALTREQMQELLLDVwQRTGKGVFLITHSVE--EAlflATRLVV 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-219 |
2.08e-58 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 184.62 E-value: 2.08e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhv 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 rnKEIGFVFQNFM--LLPRLTALQNVELPLIYAGVDkkERRERSLAALTKVGL----ADRathLPNELSGGQKQRVAVAR 154
Cdd:COG1124 79 --RRVQMVFQDPYasLHPRHTVDRILAEPLRIHGLP--DREERIAELLEQVGLppsfLDR---YPHQLSGGQRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 155 AIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEAAARQIVIRDGNVV 219
Cdd:COG1124 152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAvVAHLCDRVAVMQNGRIV 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-221 |
5.91e-57 |
|
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: 188.19 E-value: 5.91e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAesVQILHGIDVTLNQGEFTSIMGPSGSGKSTL-MNIIGCLDKP--TTGTYELAGQNISNMSEtel 77
Cdd:COG1123 4 LLEVRDLSVRYPGGD--VPAVDGVSLTIAPGETVALVGESGSGKSTLaLALMGLLPHGgrISGEVLLDGRDLLELSE--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 78 aHVRNKEIGFVFQNFML-LPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAI 156
Cdd:COG1123 79 -ALRGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMAL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD-REIGEAAARQIVIRDGNVVQD 221
Cdd:COG1123 158 ALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDlGVVAEIADRVVVMDDGRIVED 224
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-220 |
6.71e-56 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 181.11 E-value: 6.71e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNI-SNMsetelaHV 80
Cdd:COG1118 3 IEVRNISKRF----GSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNL------PP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG1118 73 RERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDREigEA---AARQIVIRDGNVVQ 220
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQE--EAlelADRVVVMNQGRIEQ 214
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-224 |
2.93e-55 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 175.83 E-value: 2.93e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQilhGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:PRK10908 1 MIRFEHVSKAYLGGRQALQ---GVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:PRK10908 78 R-RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDRE-IGEAAARQIVIRDGNVVQDWRG 224
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGlISRRSYRMLTLSDGHLHGGVGG 221
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-216 |
8.43e-54 |
|
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: 170.45 E-value: 8.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVR 81
Cdd:cd03229 1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NkeIGFVFQNFMLLPRLTALQNVELPliyagvdkkerrerslaaltkvgladrathlpneLSGGQKQRVAVARAIVNNPK 161
Cdd:cd03229 77 R--IGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPD 120
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD-REIGEAAARQIVIRDG 216
Cdd:cd03229 121 VLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDlDEAARLADRVVVLRDG 177
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-221 |
2.18e-53 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 175.52 E-value: 2.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSeTELAHVR 81
Cdd:PRK09452 15 VELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP-AENRHVN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NkeigfVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:PRK09452 90 T-----VFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREigEAAA---RQIVIRDGNVVQD 221
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKlGITFVFVTHDQE--EALTmsdRIVVMRDGRIEQD 226
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-220 |
3.67e-52 |
|
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: 168.63 E-value: 3.67e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVQilhGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvR 81
Cdd:cd03295 1 IEFENVTKRYGGGKKAVN---NLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGL-----ADRathLPNELSGGQKQRVAVARAI 156
Cdd:cd03295 75 RK-IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpaefADR---YPHELSGGQQQRVGVARAL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDreIGEA---AARQIVIRDGNVVQ 220
Cdd:cd03295 151 AADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHD--IDEAfrlADRIAIMKNGEIVQ 216
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
2-220 |
7.40e-52 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 167.88 E-value: 7.40e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIS---NMSETELA 78
Cdd:COG4161 3 IQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDfsqKPSEKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 79 HVRnKEIGFVFQNFMLLPRLTALQN-VELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:COG4161 79 LLR-QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIV-IRDGNVVQ 220
Cdd:COG4161 158 MEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVyMEKGRIIE 221
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-219 |
1.54e-51 |
|
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: 167.14 E-value: 1.54e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhv 80
Cdd:COG1120 1 MLEAENLSVGYGG----RPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 rnKEIGFVFQNFMLLPRLTALQNVEL---PLIYA-GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAI 156
Cdd:COG1120 75 --RRIAYVPQEPPAPFGLTVRELVALgryPHLGLfGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHDreIGEAAA---RQIVIRDGNVV 219
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLAReRGRTVVMVLHD--LNLAARyadRLVLLKDGRIV 217
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-200 |
3.51e-51 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 166.03 E-value: 3.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsnmsetelaHV 80
Cdd:COG1121 6 AIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP---------RR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFML---LPrLTALQNVELPLIYA----GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVA 153
Cdd:COG1121 73 ARRRIGYVPQRAEVdwdFP-ITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHD 198
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
4-218 |
4.98e-51 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 164.60 E-value: 4.98e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvRnK 83
Cdd:COG4619 3 LEGLSFRVGGK----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R-R 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPrltalQNVE--LPLIYAGVDKKERRERSLAALTKVGLADRATHLP-NELSGGQKQRVAVARAIVNNP 160
Cdd:COG4619 75 QVAYVPQEPALWG-----GTVRdnLPFPFQLRERKFDRERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQP 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEAAARQIVIRDGNV 218
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
2-220 |
3.07e-50 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 163.65 E-value: 3.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqnGAEsvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNI---SNMSETELA 78
Cdd:PRK11124 3 IQLNGINCFY--GAH--QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 79 HVRnKEIGFVFQNFMLLPRLTALQN-VELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:PRK11124 79 ELR-RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIV-IRDGNVVQ 220
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVyMENGHIVE 221
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-220 |
9.57e-50 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 162.61 E-value: 9.57e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGT-----YELAGQNISNMSET 75
Cdd:PRK11264 3 AIEVKNLVKKFHGQ----TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTirvgdITIDTARSLSQQKG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 76 ELAHVRnKEIGFVFQNFMLLPRLTALQNV-ELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVAR 154
Cdd:PRK11264 79 LIRQLR-QHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 155 AIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIG-EAAARQIVIRDGNVVQ 220
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQGRIVE 224
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-200 |
1.55e-49 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 162.28 E-value: 1.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnMSET----- 75
Cdd:COG4598 8 ALEVRDLHKSF----GDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIR-LKPDrdgel 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 76 ------ELAHVRNKeIGFVFQNFMLLPRLTALQNV-ELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQ 148
Cdd:COG4598 83 vpadrrQLQRIRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446531755 149 RVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:COG4598 162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHE 213
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
10-219 |
9.14e-49 |
|
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: 166.78 E-value: 9.14e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 10 SFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKS-TLMNIIGCLDKP---TTGTYELAGQNISNMSETELAHVRNKEI 85
Cdd:COG4172 15 AFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRIRGNRI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 86 GFVFQNFMllprlTAL--------QNVELPLIYAGVDKKERRERSLAALTKVGLADRATHL---PNELSGGQKQRVAVAR 154
Cdd:COG4172 95 AMIFQEPM-----TSLnplhtigkQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRLdayPHQLSGGQRQRVMIAM 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 155 AIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD----REIgeaAARQIVIRDGNVV 219
Cdd:COG4172 170 ALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDlgvvRRF---ADRVAVMRQGEIV 236
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-218 |
9.54e-49 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 160.23 E-value: 9.54e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYeLAGQnisnmseTELAHVRNk 83
Cdd:PRK11247 15 LNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT-------APLAEARE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTALQNVELPLiyagvdKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFI 163
Cdd:PRK11247 82 DTRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 164 LADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDreIGEAAA---RQIVIRDGNV 218
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHD--VSEAVAmadRVLLIEEGKI 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-220 |
1.32e-48 |
|
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: 159.43 E-value: 1.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMsetelaHVR 81
Cdd:cd03296 3 IEVRNVSKRF----GDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDV------PVQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRLTALQNVELPL----IYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDREIG-EAAARQIVIRDGNVVQ 220
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLhDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEQ 217
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-221 |
3.53e-48 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 159.15 E-value: 3.53e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQ-NGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:TIGR04521 1 IKLKNVSYIYQpGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQN-----FmllpRLTALQNVELPLIYAGVDKKERRERSLAALTKVGL----ADRAthlPNELSGGQKQRVA 151
Cdd:TIGR04521 81 R-KKVGLVFQFpehqlF----EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdeeyLERS---PFELSGGQMRRVA 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531755 152 VARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEAAARQIVIRDGNVVQD 221
Cdd:TIGR04521 153 IAGVLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSMEdVAEYADRVIVMHKGKIVLD 224
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-216 |
3.78e-48 |
|
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: 157.60 E-value: 3.78e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSF----QNGAEsVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGT--YELAGQ--NISNM 72
Cdd:COG4778 4 LLEVENLSKTFtlhlQGGKR-LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSilVRHDGGwvDLAQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 73 SETELAHVRNKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHL-PNELSGGQKQRVA 151
Cdd:COG4778 83 SPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPATFSGGEQQRVN 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 152 VARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAA-RQIVIRDG 216
Cdd:COG4778 163 IARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVAdRVVDVTPF 228
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
20-212 |
3.94e-48 |
|
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: 157.31 E-value: 3.94e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMsetelahvrNKEIGFVFQNFMLLP--R 97
Cdd:cd03235 14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE---------RKRIGYVPQRRSIDRdfP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LTALQNVELPLIYAGV----DKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:cd03235 85 ISVRDVVLMGLYGHKGlfrrLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164
|
170 180 190
....*....|....*....|....*....|....*....
gi 446531755 174 TKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIV 212
Cdd:cd03235 165 PKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVL 203
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-218 |
1.92e-47 |
|
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: 154.09 E-value: 1.92e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmseTELAHVR 81
Cdd:cd03230 1 IEVRNLSKRYGKK----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRLTALQNVelpliyagvdkkerrerslaaltkvgladrathlpnELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03230 73 -RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPE 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNV 218
Cdd:cd03230 116 LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHIlEEAERLCDRVAILNNGRI 173
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
11-200 |
2.65e-47 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 158.36 E-value: 2.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 11 FQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRnKEIGFVFQ 90
Cdd:COG4608 24 FGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 91 N-FMLL-PRLTALQNVELPLIYAGV-DKKERRERSLAALTKVGLadRATHL---PNELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:COG4608 103 DpYASLnPRMTVGDIIAEPLRIHGLaSKAERRERVAELLELVGL--RPEHAdryPHEFSGGQRQRIGIARALALNPKLIV 180
|
170 180 190
....*....|....*....|....*....|....*..
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD 200
Cdd:COG4608 181 CDEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHD 217
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
36-221 |
3.16e-47 |
|
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, 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 transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 158.43 E-value: 3.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 36 IMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelAHVRNkeIGFVFQNFMLLPRLTALQNVELPLIYAGVDK 115
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVP----PHLRH--INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 116 KERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTI 194
Cdd:TIGR01187 75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQlGITF 154
|
170 180
....*....|....*....|....*...
gi 446531755 195 IMITHDREIGEAAARQIVI-RDGNVVQD 221
Cdd:TIGR01187 155 VFVTHDQEEAMTMSDRIAImRKGKIAQI 182
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
2-200 |
1.84e-46 |
|
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: 153.49 E-value: 1.84e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCL-----DKPTTGTYELAGQNISNMSETE 76
Cdd:cd03260 1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 77 LAHVRnkEIGFVFQNFMLLPrLTALQNVELPLIYAGV-DKKERRERSLAALTKVGL----ADRATHLpnELSGGQKQRVA 151
Cdd:cd03260 77 LELRR--RVGMVFQKPNPFP-GSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALwdevKDRLHAL--GLSGGQQQRLC 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446531755 152 VARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQgSTIIMITHD 200
Cdd:cd03260 152 LARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHN 199
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
11-219 |
3.63e-46 |
|
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: 160.24 E-value: 3.63e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 11 FQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTL-MNIIGCLdkPTTGTYELAGQNISNMSETELAHVRnKEIGFVF 89
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLR-RRMQVVF 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 90 QNFM--LLPRLTALQNVELPLI--YAGVDKKERRERSLAALTKVGLADRATH-LPNELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:COG4172 369 QDPFgsLSPRMTVGQIIAEGLRvhGPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLV 448
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD----REIgeaAARQIVIRDGNVV 219
Cdd:COG4172 449 LDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDlavvRAL---AHRVMVMKDGKVV 505
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-220 |
4.92e-46 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 156.01 E-value: 4.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMsetelaHVR 81
Cdd:PRK10851 3 IEIANIKKSFGR----TQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL------HAR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRLTALQNVELpliyaGVDKKERRERSLAALTK---------VGLADRATHLPNELSGGQKQRVAV 152
Cdd:PRK10851 73 DRKVGFVFQHYALFRHMTVFDNIAF-----GLTVLPRRERPNAAAIKakvtqllemVQLAHLADRYPAQLSGGQKQRVAL 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 153 ARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGS-TIIMITHDREIG-EAAARQIVIRDGNVVQ 220
Cdd:PRK10851 148 ARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAmEVADRVVVMSQGNIEQ 217
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-200 |
1.34e-45 |
|
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: 151.44 E-value: 1.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqnGaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHvrnK 83
Cdd:cd03219 3 VRGLTKRF--G--GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIAR---L 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTALQNVEL--------PLIYAGVDKKER--RERSLAALTKVGLADRATHLPNELSGGQKQRVAVA 153
Cdd:cd03219 76 GIGRTFQIPRLFPELTVLENVMVaaqartgsGLLLARARREEReaRERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHD 202
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-224 |
2.06e-45 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 151.78 E-value: 2.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNG-AESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSEtelaH 79
Cdd:COG1101 1 MLELKNLSKTFNPGtVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE----Y 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRNKEIGFVFQNFML--LPRLTALQNveLPLIYA---------GVDKKERRE-RSLAALTKVGLADRATHLPNELSGGQK 147
Cdd:COG1101 77 KRAKYIGRVFQDPMMgtAPSMTIEEN--LALAYRrgkrrglrrGLTKKRRELfRELLATLGLGLENRLDTKVGLLSGGQR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 148 QRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDREigEAAA---RQIVIRDGNVVQDWR 223
Cdd:COG1101 155 QALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNME--QALDygnRLIMMHEGRIILDVS 232
|
.
gi 446531755 224 G 224
Cdd:COG1101 233 G 233
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
19-221 |
2.31e-45 |
|
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: 149.12 E-value: 2.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnKEIGFVFQnfmllprl 98
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA----RKIAYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 talqnvelpliyagvdkkerrerslaALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTST 178
Cdd:cd03214 81 --------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQI 134
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446531755 179 QIMDLFYELNKQ-GSTIIMITHDreIGEAAA---RQIVIRDGNVVQD 221
Cdd:cd03214 135 ELLELLRRLARErGKTVVMVLHD--LNLAARyadRVILLKDGRIVAQ 179
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-220 |
2.34e-45 |
|
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: 150.10 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETElahvR 81
Cdd:cd03301 1 VELENVTKRF----GNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----R 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NkeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKE--RRERSLAALTKVG-LADRathLPNELSGGQKQRVAVARAIVN 158
Cdd:cd03301 73 D--IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEidERVREVAELLQIEhLLDR---KPKQLSGGQRQRVALGRAIVR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 159 NPKFILADEPTGALDTKTSTQIMDlfyELNK----QGSTIIMITHDREIGEAAARQI-VIRDGNVVQ 220
Cdd:cd03301 148 EPKVFLMDEPLSNLDAKLRVQMRA---ELKRlqqrLGTTTIYVTHDQVEAMTMADRIaVMNDGQIQQ 211
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
20-215 |
2.72e-45 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 149.94 E-value: 2.72e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLDKP--TTGTYELAGQNISNMSetelAHVRNkeIGFVFQNFMLLP 96
Cdd:COG4136 16 LLAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP----AEQRR--IGILFQDDLLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 97 RLTALQNV--ELPliyAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDT 174
Cdd:COG4136 90 HLSVGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446531755 175 KTSTQIMDL-FYELNKQGSTIIMITHDREIGEAAARQIVIRD 215
Cdd:COG4136 167 ALRAQFREFvFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-221 |
2.77e-45 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 150.29 E-value: 2.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNgaesvQILHgIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsnmseTELA-H 79
Cdd:COG3840 1 MLRLDDLTYRYGD-----FPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-----TALPpA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRnkEIGFVFQNFMLLPRLTALQNVELpliyaGVDKK-----ERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVAR 154
Cdd:COG3840 70 ER--PVSMLFQENNLFPHLTVAQNIGL-----GLRPGlkltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALAR 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 155 AIVNNPKFILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHD-REIGEAAARQIVIRDGNVVQD 221
Cdd:COG3840 143 CLVRKRPILLLDEPFSALDPALRQEMLDLVDELCReRGLTVLMVTHDpEDAARIADRVLLVADGRIAAD 211
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-216 |
3.94e-45 |
|
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: 147.91 E-value: 3.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGItkSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvr 81
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLR--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRlTALQNVelpliyagvdkkerrerslaaltkvgladrathlpneLSGGQKQRVAVARAIVNNPK 161
Cdd:cd03228 76 -KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVIRDG 216
Cdd:cd03228 117 ILILDEATSALDPETEALILEALRAL-AKGKTVIVIAHRLSTIRDADRIIVLDDG 170
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-202 |
5.26e-45 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 150.62 E-value: 5.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAesvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelahv 80
Cdd:PRK11248 1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 rnKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:PRK11248 70 --AERGVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDRE 202
Cdd:PRK11248 148 QLLLLDEPFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIE 190
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
21-169 |
1.52e-44 |
|
ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.
Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 145.87 E-value: 1.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvrNKEIGFVFQNFMLLPRLTA 100
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 101 LQNVELPLIYAGVDKKERRERSLAALTKVGLAD----RATHLPNELSGGQKQRVAVARAIVNNPKFILADEPT 169
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-219 |
2.10e-44 |
|
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: 148.47 E-value: 2.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNisnmSETELAHV 80
Cdd:COG4555 1 MIEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNVELpliYA---GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:COG4555 73 R-RQIGVLPDERGLYDRLTVRENIRY---FAelyGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALV 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:COG4555 149 HDPKVLLLDEPTNGLDVMARRLLREILRALKKEGKTVLFSSHImQEVEALCDRVVILHKGKVV 211
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-216 |
5.63e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 144.69 E-value: 5.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnK 83
Cdd:cd00267 2 IENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR----R 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQnfmllprltalqnvelpliyagvdkkerrerslaaltkvgladrathlpneLSGGQKQRVAVARAIVNNPKFI 163
Cdd:cd00267 74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446531755 164 LADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDG 216
Cdd:cd00267 103 LLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDpELAELAADRVIVLKDG 156
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-221 |
6.02e-44 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the upstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275313 [Multi-domain] Cd Length: 268 Bit Score: 147.96 E-value: 6.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNmsETELAHVR 81
Cdd:TIGR04520 1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLD--EENLWEIR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKeIGFVFQN---------------FmllprltALQNvelpliyAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQ 146
Cdd:TIGR04520 77 KK-VGMVFQNpdnqfvgatveddvaF-------GLEN-------LGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQ 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 147 KQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHDREigEA--AARQIVIRDGNVVQD 221
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeEGITVISITHDME--EAvlADRVIVMNKGKIVAE 217
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-200 |
6.11e-44 |
|
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: 147.88 E-value: 6.11e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqnGAesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAH- 79
Cdd:COG0411 4 LLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARl 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 --VRnkeigfVFQNFMLLPRLTALQNVE---------------LPLIYAGVDKKERRERSLAALTKVGLADRATHLPNEL 142
Cdd:COG0411 80 giAR------TFQNPRLFPELTVLENVLvaaharlgrgllaalLRLPRARREEREARERAEELLERVGLADRADEPAGNL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 143 SGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHD 200
Cdd:COG0411 154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDeRGITILLIEHD 212
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-215 |
8.75e-43 |
|
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: 143.39 E-value: 8.75e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETelahv 80
Cdd:COG4133 2 MLEAENLSCRRGE----RLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFMLLPRLTALQNVELpliYAGVDKKER-RERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNN 159
Cdd:COG4133 73 YRRRLAYLGHADGLKPELTVRENLRF---WAALYGLRAdREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSP 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 160 PKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDrEIGEAAARQIVIRD 215
Cdd:COG4133 150 APLWLLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ-PLELAAARVLDLGD 204
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
21-206 |
2.73e-42 |
|
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]
Pssm-ID: 130252 [Multi-domain] Cd Length: 230 Bit Score: 142.99 E-value: 2.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnkeigfVFQNFMLLPRLTA 100
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV---------VFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 101 LQNVELPL--IYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTST 178
Cdd:TIGR01184 72 RENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180
....*....|....*....|....*....
gi 446531755 179 QIMDLFYEL-NKQGSTIIMITHDreIGEA 206
Cdd:TIGR01184 152 NLQEELMQIwEEHRVTVLMVTHD--VDEA 178
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-221 |
3.71e-42 |
|
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: 151.14 E-value: 3.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGItkSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSeteLAHVR 81
Cdd:COG2274 474 IELENV--SFRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKeIGFVFQNFMLLPRlTALQNVelpliyAGVDKKERRERSLAALTKVGLADRATHLPN-----------ELSGGQKQRV 150
Cdd:COG2274 549 RQ-IGVVLQDVFLFSG-TIRENI------TLGDPDATDEEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRL 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETEAIILENLRRL-LKGRTVIIIAHRLSTIRLADRIIVLDKGRIVED 690
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
1-220 |
8.59e-42 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 144.99 E-value: 8.59e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSEtelahv 80
Cdd:PRK11650 3 GLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP------ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLA---DRAthlPNELSGGQKQRVAVARAIV 157
Cdd:PRK11650 74 ADRDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEpllDRK---PRELSGGQRQRVAMGRAIV 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 158 NNPKFILADEPTGALDTKTSTQ----IMDLFYELnkqGSTIIMITHDREigEA---AARQIVIRDGNVVQ 220
Cdd:PRK11650 151 REPAVFLFDEPLSNLDAKLRVQmrleIQRLHRRL---KTTSLYVTHDQV--EAmtlADRVVVMNGGVAEQ 215
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-221 |
9.68e-42 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 143.69 E-value: 9.68e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESV-QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKEKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 R--------------------NKEIGFVFQ--NFMLLPrltalQNVELPLIYA----GVDKKERRERSLAALTKVGLA-- 132
Cdd:PRK13651 83 VleklviqktrfkkikkikeiRRRVGVVFQfaEYQLFE-----QTIEKDIIFGpvsmGVSKEEAKKRAAKYIELVGLDes 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 133 --DRAthlPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDRE-IGEAAAR 209
Cdd:PRK13651 158 ylQRS---PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDnVLEWTKR 234
|
250
....*....|..
gi 446531755 210 QIVIRDGNVVQD 221
Cdd:PRK13651 235 TIFFKDGKIIKD 246
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
19-221 |
2.77e-41 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 141.26 E-value: 2.77e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSET----------ELAHVRNKeIGFV 88
Cdd:PRK10619 19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknQLRLLRTR-LTMV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 89 FQNFMLLPRLTALQNV-ELPLIYAGVDKKERRERSLAALTKVGLADRAT-HLPNELSGGQKQRVAVARAIVNNPKFILAD 166
Cdd:PRK10619 98 FQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 167 EPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:PRK10619 178 EPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEE 232
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-221 |
3.43e-41 |
|
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: 139.25 E-value: 3.43e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGaesvQILHGIDVTLNQGeFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHvr 81
Cdd:cd03264 1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nkeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03264 74 ---IGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKqGSTIIMITHDREIGEAAARQI-VIRDGNVVQD 221
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGE-DRIVILSTHIVEDVESLCNQVaVLNKGKLVFE 210
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
21-220 |
3.66e-41 |
|
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: 140.16 E-value: 3.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSEtelahvRNKEIGFVFQNFMLLPRLTA 100
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPP------EKRDISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 101 LQNVELPLIYAGVDKKERRERSLAALTKVGLadraTHL----PNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKT 176
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEIERKVLEIAEMLGI----DHLlnrkPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446531755 177 STQIMDLFYELNKQ-GSTIIMITHDREigEAAA---RQIVIRDGNVVQ 220
Cdd:cd03299 165 KEKLREELKKIRKEfGVTVLHVTHDFE--EAWAladKVAIMLNGKLIQ 210
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-222 |
8.85e-41 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 145.16 E-value: 8.85e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqnGAesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSeteLAHVRNK 83
Cdd:COG1129 7 MRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRS---PRDAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTALQNV---ELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG1129 80 GIAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVVQDW 222
Cdd:COG1129 160 RVLILDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRlDEVFEIADRVTVLRDGRLVGTG 222
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
25-221 |
2.38e-40 |
|
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: 137.24 E-value: 2.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 25 DVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETElahvrnKEIGFVFQNFMLLPRLTALQNV 104
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 105 ELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLF 184
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 446531755 185 YELNKQ-GSTIIMITHDREIGEA-AARQIVIRDGNVVQD 221
Cdd:cd03298 172 LDLHAEtKMTVLMVTHQPEDAKRlAQRVVFLDNGRIAAQ 210
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-220 |
3.46e-40 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 141.71 E-value: 3.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 26 VTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEIGFVFQNFMLLPRLTALQNVE 105
Cdd:PRK10070 49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTVLDNTA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 106 LPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFY 185
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208
|
170 180 190
....*....|....*....|....*....|....*..
gi 446531755 186 ELN-KQGSTIIMITHD-REIGEAAARQIVIRDGNVVQ 220
Cdd:PRK10070 209 KLQaKHQRTIVFISHDlDEAMRIGDRIAIMQNGEVVQ 245
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
15-220 |
8.85e-40 |
|
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: 143.36 E-value: 8.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 15 AESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnKEIGFVFQNfml 94
Cdd:COG4988 347 PGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR----RQIAWVPQN--- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 lPRL---TALQNVELPLIYAGvdkkerRERSLAALTKVGLADRATHLPN-------E----LSGGQKQRVAVARAIVNNP 160
Cdd:COG4988 420 -PYLfagTIRENLRLGRPDAS------DEELEAALEAAGLDEFVAALPDgldtplgEggrgLSGGQAQRLALARALLRDA 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:COG4988 493 PLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALLAQADRILVLDDGRIVE 551
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-222 |
1.31e-39 |
|
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: 135.50 E-value: 1.31e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNqGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEIGFVFQNFMLLPRLTALQN 103
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVREN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 104 VELPLIYAGVDKKERRERSLAALTKVG-LADRATHlpnELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMD 182
Cdd:cd03297 96 LAFGLKRKRNREDRISVDELLDLLGLDhLLNRYPA---QLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446531755 183 LFYELNKQ-GSTIIMITHD-REIGEAAARQIVIRDGNVVQDW 222
Cdd:cd03297 173 ELKQIKKNlNIPVIFVTHDlSEAEYLADRIVVMEDGRLQYIG 214
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
1.80e-39 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 136.75 E-value: 1.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESvqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnMSETELAHV 80
Cdd:PRK13639 1 ILETRDLKYSYPDGTEA---LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQN---FMLLPrlTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:PRK13639 77 R-KTVGIVFQNpddQLFAP--TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQI-VIRDGNVV 219
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVyVMSDGKII 216
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-220 |
1.88e-39 |
|
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: 142.60 E-value: 1.88e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVr 81
Cdd:COG4987 334 LELEDVSFRYPGAGRPV--LDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nkeIGFVFQNfmllPRL---TALQNveLPLIYAGVDkkerRERSLAALTKVGLADRATHLPN-----------ELSGGQK 147
Cdd:COG4987 411 ---IAVVPQR----PHLfdtTLREN--LRLARPDAT----DEELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGER 477
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 148 QRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNkQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:COG4987 478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERMDRILVLEDGRIVE 549
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
18-219 |
2.00e-39 |
|
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: 135.25 E-value: 2.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelAHVRNKE-IGFVFQNFMLLP 96
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLP----PHERARAgIGYVPEGRRIFP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 97 RLTALQNVELPL-IYAGVDKKERRERSLAALTKvgLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTK 175
Cdd:cd03224 89 ELTVEENLLLGAyARRRAKRKARLERVYELFPR--LKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 176 TSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:cd03224 167 IVEEIFEAIRELRDEGVTILLVEQNaRFALEIADRAYVLERGRVV 211
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
5-219 |
2.08e-39 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 136.51 E-value: 2.08e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 5 KGITKSFQN-----GAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelAH 79
Cdd:COG4167 8 RNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD----YK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRNKEIGFVFQ--NFMLLPRLTALQNVELPLIYA-GVDKKERRERSLAALTKVGL-ADRATHLPNELSGGQKQRVAVARA 155
Cdd:COG4167 84 YRCKHIRMIFQdpNTSLNPRLNIGQILEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 156 IVNNPKFILADEPTGALDTKTSTQIMDLFYELN-KQGSTIIMITHDREIGEAAARQ-IVIRDGNVV 219
Cdd:COG4167 164 LILQPKIIIADEALAALDMSVRSQIINLMLELQeKLGISYIYVSQHLGIVKHISDKvLVMHQGEVV 229
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
18-200 |
3.15e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 137.40 E-value: 3.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRnKEIGFVFQN--FMLL 95
Cdd:PRK11308 28 VKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLR-QKIQIVFQNpyGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PRLTALQNVELPL-IYAGVDKKERRERSLAALTKVGL----ADRATHLpneLSGGQKQRVAVARAIVNNPKFILADEPTG 170
Cdd:PRK11308 107 PRKKVGQILEEPLlINTSLSAAERREKALAMMAKVGLrpehYDRYPHM---FSGGQRQRIAIARALMLDPDVVVADEPVS 183
|
170 180 190
....*....|....*....|....*....|.
gi 446531755 171 ALDTKTSTQIMDLFYELNKQ-GSTIIMITHD 200
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQElGLSYVFISHD 214
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
24-220 |
7.32e-39 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 136.41 E-value: 7.32e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNQGEFTSIMGPSGSGKS-TLMNIIGCLDKP---TTGTYELAGQNISNMSETELAHVRNKEIGFVFQNFM--LLPR 97
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDPMtsLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LT-ALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHL---PNELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK11022 106 YTvGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLdvyPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446531755 174 TKTSTQIMDLFYELNKQGS-TIIMITHDRE-IGEAAARQIVIRDGNVVQ 220
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENmALVLITHDLAlVAEAAHKIIVMYAGQVVE 234
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
4-219 |
1.52e-38 |
|
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: 132.63 E-value: 1.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmseTELAHVRnK 83
Cdd:cd03263 3 IRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAAR-Q 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTALQNVElplIYA---GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:cd03263 76 SLGYCPQFDALFDELTVREHLR---FYArlkGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVI-RDGNVV 219
Cdd:cd03263 153 SVLLLDEPTSGLDPASRRAIWDLILEV-RKGRSIILTTHSMDEAEALCDRIAImSDGKLR 211
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
4-220 |
2.99e-38 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 135.62 E-value: 2.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGAesvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelahVRNK 83
Cdd:PRK11432 9 LKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRS------IQQR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFI 163
Cdd:PRK11432 79 DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 164 LADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREigEAAARQ---IVIRDGNVVQ 220
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQS--EAFAVSdtvIVMNKGKIMQ 217
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-221 |
3.90e-38 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 133.21 E-value: 3.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCL---DKPTTGTYELAGQNISNmsETEL 77
Cdd:PRK09984 4 IIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQR--EGRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 78 AHVRNK---EIGFVFQNFMLLPRLTALQNVEL------PLIYAGVD--KKERRERSLAALTKVGLADRATHLPNELSGGQ 146
Cdd:PRK09984 78 ARDIRKsraNTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFSwfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQ 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 147 KQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIV-IRDGNVVQD 221
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNdGITVVVTLHQVDYALRYCERIVaLRQGHVFYD 234
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-220 |
4.34e-38 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 135.73 E-value: 4.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqNGAESVQilhGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETElahv 80
Cdd:PRK11607 19 LLEIRNLTKSF-DGQHAVD---DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ---- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 rnKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:PRK11607 91 --RPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 161 KFILADEPTGALDTK----TSTQIMDLfyeLNKQGSTIIMITHDREIGEAAARQIVIRD-GNVVQ 220
Cdd:PRK11607 169 KLLLLDEPMGALDKKlrdrMQLEVVDI---LERVGVTCVMVTHDQEEAMTMAGRIAIMNrGKFVQ 230
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-200 |
6.53e-38 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 134.08 E-value: 6.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKS-TLMNIIGCLDKP--TTGTYELAGQNISNMSETEL 77
Cdd:PRK09473 12 LLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKEL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 78 AHVRNKEIGFVFQNFMllprlTAL--------QNVELPLIYAGVDKKERRERSLAALTKVGLAD---RATHLPNELSGGQ 146
Cdd:PRK09473 92 NKLRAEQISMIFQDPM-----TSLnpymrvgeQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGM 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 147 KQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGST-IIMITHD 200
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHD 221
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
19-199 |
3.65e-37 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 130.16 E-value: 3.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTL------MN--IIGCLdkpTTGTYELAGQNISNmSETELAHVRnKEIGFVFQ 90
Cdd:COG1117 25 QALKDINLDIPENKVTALIGPSGCGKSTLlrclnrMNdlIPGAR---VEGEILLDGEDIYD-PDVDVVELR-RRVGMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 91 NFMLLPrLTALQNVELPLIYAGV-DKKERRERSLAALTKVGL----ADRATHLPNELSGGQKQRVAVARAIVNNPKFILA 165
Cdd:COG1117 100 KPNPFP-KSIYDNVAYGLRLHGIkSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLM 178
|
170 180 190
....*....|....*....|....*....|....
gi 446531755 166 DEPTGALDTKTSTQIMDLFYELnKQGSTIIMITH 199
Cdd:COG1117 179 DEPTSALDPISTAKIEELILEL-KKDYTIVIVTH 211
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-200 |
7.15e-37 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 129.47 E-value: 7.15e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGItkSFQNGaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLdKPTTGTYELAGQNISNMSETELAH 79
Cdd:COG4559 1 MLEAENL--SVRLG--GRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELAR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VR-----NKEIGFVFqnfmllprlTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVAR 154
Cdd:COG4559 76 RRavlpqHSSLAFPF---------TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLAR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446531755 155 AIV-------NNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:COG4559 147 VLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHD 199
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-219 |
9.16e-37 |
|
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: 128.25 E-value: 9.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmseTELAHV 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVV----KEPAEA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKeIGFVFQNFMLLPRLTALQNVELpliYAGVDKKERRErSLAALTKVG-------LADRAThlpNELSGGQKQRVAVA 153
Cdd:cd03266 77 RRR-LGFVSDSTGLYDRLTARENLEY---FAGLYGLKGDE-LTARLEELAdrlgmeeLLDRRV---GGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGKCILFSTHImQEVERLCDRVVVLHRGRVV 215
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
11-200 |
9.31e-37 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 127.15 E-value: 9.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 11 FQNGAEsvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsNMSETELAHVRnKEIGFVFQ 90
Cdd:TIGR01166 1 YPGGPE---VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPL-DYSRKGLLERR-QRVGLVFQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 91 N---FMLLPRLTalQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADE 167
Cdd:TIGR01166 76 DpddQLFAADVD--QDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDE 153
|
170 180 190
....*....|....*....|....*....|...
gi 446531755 168 PTGALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILRRLRAEGMTVVISTHD 186
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
21-220 |
1.21e-36 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 129.95 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNI-SNMSETELAHVRnKEIGFVFQnF--MLLPR 97
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQ-FpeAQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LTALQNVELPLIYAGVDKKERRERSLAALTKVGLA-DRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKT 176
Cdd:PRK13641 101 NTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 177 STQIMDLFYELNKQGSTIIMITHDR-EIGEAAARQIVIRDGNVVQ 220
Cdd:PRK13641 181 RKEMMQLFKDYQKAGHTVILVTHNMdDVAEYADDVLVLEHGKLIK 225
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-220 |
1.54e-36 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 131.31 E-value: 1.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNisnMSETELAhvr 81
Cdd:PRK11000 4 VTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKR---MNDVPPA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:PRK11000 74 ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPS 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIVIRD-GNVVQ 220
Cdd:PRK11000 154 VFLLDEPLSNLDAALRVQMRIEISRLHKRlGRTMIYVTHDQVEAMTLADKIVVLDaGRVAQ 214
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
2-215 |
1.67e-36 |
|
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: 127.49 E-value: 1.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqNGAESVQilhGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNmsetELAHVR 81
Cdd:cd03265 1 IEVENLVKKY-GDFEAVR---GVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR----EPREVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03265 73 -RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHDREIGEAAARQIVIRD 215
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEeFGMTILLTTHYMEEAEQLCDRVAIID 206
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-219 |
3.89e-36 |
|
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. The CbiMNQO family ABC transport system is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213193 [Multi-domain] Cd Length: 205 Bit Score: 126.22 E-value: 3.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGAEsvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsetelAHVRNK 83
Cdd:cd03226 2 IENISFSYKKGTE---ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-------AKERRK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQN-----FMllprltalQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVN 158
Cdd:cd03226 72 SIGYVMQDvdyqlFT--------DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLS 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531755 159 NPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDRE-IGEAAARQIVIRDGNVV 219
Cdd:cd03226 144 GKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
16-220 |
5.96e-36 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 132.98 E-value: 5.96e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 16 ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvRNKeIGFVFQNFMLL 95
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQ-IGVVPQDTFLF 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PRlTALQNVELPLIYAGvdkkerRERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:COG1132 427 SG-TIRENIRYGRPDAT------DEEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILI 499
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITH--------DReIgeaaarqIVIRDGNVVQ 220
Cdd:COG1132 500 LDEATSALDTETEALIQEALERL-MKGRTTIVIAHrlstirnaDR-I-------LVLDDGRIVE 554
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
1-221 |
6.42e-36 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 127.50 E-value: 6.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGA-----ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSET 75
Cdd:PRK10419 3 LLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 76 ELAHVRnKEIGFVFQNFM--LLPRLTALQNVELPLIY-AGVDKKERRERSLAALTKVGLADR-ATHLPNELSGGQKQRVA 151
Cdd:PRK10419 83 QRKAFR-RDIQMVFQDSIsaVNPRKTVREIIREPLRHlLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVC 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446531755 152 VARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGST-IIMITHD-REIGEAAARQIVIRDGNVVQD 221
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTaCLFITHDlRLVERFCQRVMVMDNGQIVET 233
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-219 |
1.04e-35 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 127.05 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGItkSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNisnMSETELAHVR 81
Cdd:PRK13635 6 IRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMV---LSEETVWDVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQN----FMllpRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:PRK13635 81 -RQVGMVFQNpdnqFV---GATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQGS-TIIMITHDREIGEAAARQIVIRDGNVV 219
Cdd:PRK13635 157 LQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVMNKGEIL 219
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-221 |
3.05e-35 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 125.97 E-value: 3.05e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTL--NQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNmsETELA 78
Cdd:PRK13633 4 MIKCKNVSYKYESNEESTEKLALDDVNLevKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSD--EENLW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 79 HVRNKEiGFVFQNfmllP--RLTAlQNVELPLIYA----GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAV 152
Cdd:PRK13633 82 DIRNKA-GMVFQN----PdnQIVA-TIVEEDVAFGpenlGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAI 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 153 ARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVEADRIIVMDSGKVVME 225
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-219 |
1.10e-34 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 123.65 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhv 80
Cdd:COG4604 1 MIEIKNVSKRYGG----KVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 rnKEIGFVFQNFMLLPRLTALQNVEL---PliYAG----VDKKERRERSLAALTKVGLADRatHLpNELSGGQKQRVAVA 153
Cdd:COG4604 75 --KRLAILRQENHINSRLTVRELVAFgrfP--YSKgrltAEDREIIDEAIAYLDLEDLADR--YL-DELSGGQRQRAFIA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDreIGEAA--ARQIV-IRDGNVV 219
Cdd:COG4604 148 MVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLaDELGKTVVIVLHD--INFAScyADHIVaMKDGRVV 215
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
4-219 |
1.87e-34 |
|
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: 120.61 E-value: 1.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSeteLAHVRNK 83
Cdd:cd03216 3 LRGITKRF----GGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS---PRDARRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQnfmllprltalqnvelpliyagvdkkerrerslaaltkvgladrathlpneLSGGQKQRVAVARAIVNNPKFI 163
Cdd:cd03216 76 GIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARLL 104
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 164 LADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:cd03216 105 ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRlDEVFEIADRVTVLRDGRVV 161
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
2-218 |
2.61e-34 |
|
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: 120.40 E-value: 2.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGItkSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvr 81
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELG--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPrltalqnvelpliyagvdkkerrerslaaltkvG-LADrathlpNELSGGQKQRVAVARAIVNNP 160
Cdd:cd03246 76 -DHVGYLPQDDELFS---------------------------------GsIAE------NILSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNV 218
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-220 |
2.77e-34 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 123.74 E-value: 2.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAE-SVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMS-ETELAH 79
Cdd:PRK13646 3 IRFDNVSYTYQKGTPyEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRnKEIGFVFQnfmlLPRLTALQ-NVELPLIYA----GVDKKERRERSLAALTKVGLA-DRATHLPNELSGGQKQRVAVA 153
Cdd:PRK13646 83 VR-KRIGMVFQ----FPESQLFEdTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIV 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYELN-KQGSTIIMITHD-REIGEAAARQIVIRDGNVVQ 220
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
18-219 |
2.78e-34 |
|
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: 122.01 E-value: 2.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGcLDKPTTGTYELAGQNISNMSetelAHVRNKE-IGFVFQNFMLL 95
Cdd:COG0410 16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISG-LLPPRSGSIRFDGEDITGLP----PHRIARLgIGYVPEGRRIF 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PRLTALQNVELPLiYAGVDKKERRERslaaLTKVG-----LADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTG 170
Cdd:COG0410 91 PSLTVEENLLLGA-YARRDRAEVRAD----LERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446531755 171 ALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:COG0410 166 GLAPLIVEEIFEIIRRLNREGVTILLVEQNaRFALEIADRAYVLERGRIV 215
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
9.27e-34 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 122.02 E-value: 9.27e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGItkSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmSETeLAHV 80
Cdd:PRK13632 7 MIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS--KEN-LKEI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKeIGFVFQN----FMllpRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAI 156
Cdd:PRK13632 82 RKK-IGIIFQNpdnqFI---GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGS-TIIMITHDREIGEAAARQIVIRDGNVV 219
Cdd:PRK13632 158 ALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKVIVFSEGKLI 221
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-219 |
9.73e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 125.91 E-value: 9.73e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqnGaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQ--NISNMsetelA 78
Cdd:COG3845 5 ALELRGITKRF--G--GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSP-----R 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 79 HVRNKEIGFVFQNFMLLPRLTALQNVEL---PLIYAGVDKKERRERSLAALTKVGLA---DRATHlpnELSGGQKQRVAV 152
Cdd:COG3845 76 DAIALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDvdpDAKVE---DLSVGEQQRVEI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 153 ARAIVNNPKFILADEPTGALdtkTSTQIMDLFY---ELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:COG3845 153 LKALYRGARILILDEPTAVL---TPQEADELFEilrRLAAEGKSIIFITHKlREVMAIADRVTVLRRGKVV 220
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
25-220 |
1.16e-33 |
|
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]
Pssm-ID: 130344 [Multi-domain] Cd Length: 213 Bit Score: 119.97 E-value: 1.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 25 DVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETElahvrnKEIGFVFQNFMLLPRLTALQNV 104
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 105 ELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLF 184
Cdd:TIGR01277 92 GLGLHPGLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|....*...
gi 446531755 185 YEL-NKQGSTIIMITHDREIGEAAARQI-VIRDGNVVQ 220
Cdd:TIGR01277 172 KQLcSERQRTLLMVTHHLSDARAIASQIaVVSQGKIKV 209
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
14-213 |
1.68e-33 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 118.88 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 14 GAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTyelagqnisnmseteLAHVRNKEIGFVFQNFM 93
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGT---------------VRRAGGARVAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 94 L---LPrLTALQNVEL----PLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILAD 166
Cdd:NF040873 66 VpdsLP-LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLD 144
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446531755 167 EPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVI 213
Cdd:NF040873 145 EPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELVRRADPCVLL 191
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-219 |
2.06e-33 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 122.90 E-value: 2.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNQGEF-------------TSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAG---QNisnmSETEL---AHVRNke 84
Cdd:COG4148 5 VDFRLRRGGFtldvdftlpgrgvTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQD----SARGIflpPHRRR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 85 IGFVFQNFMLLPRLTALQNVElpliYAgvDKKERRERSLAALTKV----GLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:COG4148 79 IGYVFQEARLFPHLSVRGNLL----YG--RKRAPRAERRISFDEVvellGIGHLLDRRPATLSGGERQRVAIGRALLSSP 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGST-IIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:COG4148 153 RLLLMDEPLAALDLARKAEILPYLERLRDELDIpILYVSHSlDEVARLADHVVLLEQGRVV 213
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-199 |
5.55e-33 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 119.25 E-value: 5.55e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCL-----DKPTTGTYELAGQNISNMSETE 76
Cdd:PRK14247 4 IEIRDLKVSFGQ----VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 77 LahvrNKEIGFVFQNFMLLPRLTALQNVELPLIYAGV--DKKERRERSLAALTKVGL----ADRATHLPNELSGGQKQRV 150
Cdd:PRK14247 80 L----RRRVQMVFQIPNPIPNLSIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQgSTIIMITH 199
Cdd:PRK14247 156 CIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTH 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
23-200 |
6.08e-33 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 121.35 E-value: 6.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 23 GIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGcLDKPTTGTYELAGQNISNMSETELAHVRnKEIGFVFQNFM--LLPRLT 99
Cdd:PRK15079 39 GVTLRLYEGETLGVVGESGCGKSTFARaIIG-LVKATDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQDPLasLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVELPLI--YAGVDKKERRERSLAALTKVGLadrathLPN-------ELSGGQKQRVAVARAIVNNPKFILADEPTG 170
Cdd:PRK15079 117 IGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGL------LPNlinryphEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190
....*....|....*....|....*....|.
gi 446531755 171 ALDTKTSTQIMDLFYELNKQ-GSTIIMITHD 200
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHD 221
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
21-220 |
6.43e-33 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 120.12 E-value: 6.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISN-MSETELAHVRnKEIGFVFQnF--MLLPR 97
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLR-KKVGIVFQ-FpeHQLFE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LTALQNVELPLIYAGVDKKERRERSLAALTKVGL-ADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKT 176
Cdd:PRK13634 101 ETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446531755 177 STQIMDLFYELNK-QGSTIIMITHDREIGEAAARQ-IVIRDGNVVQ 220
Cdd:PRK13634 181 RKEMMEMFYKLHKeKGLTTVLVTHSMEDAARYADQiVVMHKGTVFL 226
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-224 |
7.94e-33 |
|
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: 117.70 E-value: 7.94e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETelahvr 81
Cdd:cd03268 1 LKTNDLTKTYGKK----RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRErslaALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRIDE----VLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVVqdWRG 224
Cdd:cd03268 147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLlSEIQKVADRIGIINKGKLI--EEG 208
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
19-199 |
9.12e-33 |
|
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: 117.27 E-value: 9.12e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKP--TTGTYELAGQNISnmsetelAHVRNKEIGFVFQNFMLLP 96
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLD-------KRSFRKIIGYVPQDDILHP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 97 RLTALQNvelpLIYAgvdkkerrerslAALTKvgladrathlpneLSGGQKQRVAVARAIVNNPKFILADEPTGALDTKT 176
Cdd:cd03213 96 TLTVRET----LMFA------------AKLRG-------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSS 146
|
170 180
....*....|....*....|...
gi 446531755 177 STQIMDLFYELNKQGSTIIMITH 199
Cdd:cd03213 147 ALQVMSLLRRLADTGRTIICSIH 169
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-220 |
5.15e-32 |
|
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: 121.45 E-value: 5.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLD--KPTTG--TYELA------------ 65
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGriIYHVAlcekcgyverps 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 66 --GQNIS--------------NMSETELAHVRnKEIGFVFQ-NFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTK 128
Cdd:TIGR03269 77 kvGEPCPvcggtlepeevdfwNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 129 VGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEA 206
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsGISMVLTSHWPEvIEDL 235
|
250
....*....|....
gi 446531755 207 AARQIVIRDGNVVQ 220
Cdd:TIGR03269 236 SDKAIWLENGEIKE 249
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
24-218 |
1.02e-31 |
|
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]
Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 118.29 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEIGFVFQNFMLLPRLTALQN 103
Cdd:TIGR02142 16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRGN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 104 VELPLIYAGVDKKERRERSLAALTKVG-LADRathLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMD 182
Cdd:TIGR02142 96 LRYGMKRARPSERRISFERVIELLGIGhLLGR---LPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172
|
170 180 190
....*....|....*....|....*....|....*...
gi 446531755 183 LFYELNKQ-GSTIIMITHD-REIGEAAARQIVIRDGNV 218
Cdd:TIGR02142 173 YLERLHAEfGIPILYVSHSlQEVLRLADRVVVLEDGRV 210
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
11-220 |
2.23e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 119.81 E-value: 2.23e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 11 FQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKS-TLMNIIGCLDKP----TTGTYELAGQNISNMSETELAHVRNKEI 85
Cdd:PRK15134 15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQTLRGVRGNKI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 86 GFVFQNFMLlpRLTALQNVELPL-----IYAGVDKKERRERSLAALTKVGL---ADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:PRK15134 95 AMIFQEPMV--SLNPLHTLEKQLyevlsLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALL 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREI-GEAAARQIVIRDGNVVQ 220
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIvRKLADRVAVMQNGRCVE 237
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-221 |
3.33e-31 |
|
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: 114.41 E-value: 3.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTG-TYELAGQNisnMSETELAH 79
Cdd:COG1119 3 LLELRNVTVRR----GGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGER---RGGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRnKEIGFV---FQNFmLLPRLTALQNVelpL--------IYAGVDKKERrERSLAALTKVGLADRATHLPNELSGGQKQ 148
Cdd:COG1119 76 LR-KRIGLVspaLQLR-FPRDETVLDVV---LsgffdsigLYREPTDEQR-ERARELLELLGLAHLADRPFGTLSQGEQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 149 RVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGS-TIIMITHDRE-IGEAAARQIVIRDGNVVQD 221
Cdd:COG1119 150 RVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGApTLVLVTHHVEeIPPGITHVLLLKDGRVVAA 224
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
2-199 |
3.97e-31 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 115.23 E-value: 3.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAE-SVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSET-ELAH 79
Cdd:PRK13649 3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkDIKQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRnKEIGFVFQnfmlLPRL-----TALQNVELPLIYAGVDKKERRERSLAALTKVGLADRA-THLPNELSGGQKQRVAVA 153
Cdd:PRK13649 83 IR-KKVGLVFQ----FPESqlfeeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIA 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:PRK13649 158 GILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
2-219 |
7.29e-31 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 114.45 E-value: 7.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESvqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETElahVR 81
Cdd:PRK13647 5 IEVEDLHFRYKDGTKA---LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKW---VR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKeIGFVFQNfmllP-----RLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAI 156
Cdd:PRK13647 79 SK-VGLVFQD----PddqvfSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIG-EAAARQIVIRDGNVV 219
Cdd:PRK13647 154 AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAaEWADQVIVLKEGRVL 217
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
16-220 |
8.99e-31 |
|
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: 8.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 16 ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvRNKeIGFVFQNFMLL 95
Cdd:cd03254 14 EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RSM-IGVVLQDTFLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PRlTALQNVELPLIYAgvdkkeRRERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:cd03254 90 SG-TIMENIRLGRPNA------TDEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLLAIARAMLRDPKILI 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELNKqGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:cd03254 163 LDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLDDGKIIE 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-200 |
1.50e-30 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 113.32 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGItkSFQNGAESvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHV 80
Cdd:PRK11831 7 LVDMRGV--SFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPRLTALQNVELPLiyagvdkkerRERS-----------LAALTKVGLADRATHLPNELSGGQKQR 149
Cdd:PRK11831 83 R-KRMSMLFQSGALFTDMNVFDNVAYPL----------REHTqlpapllhstvMMKLEAVGLRGAAKLMPSELSGGMARR 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446531755 150 VAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD 200
Cdd:PRK11831 152 AALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSAlGVTCVVVSHD 203
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
6-218 |
2.27e-30 |
|
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: 111.87 E-value: 2.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 6 GITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHvrnKEI 85
Cdd:cd03218 5 NLSKRYGKR----KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR---LGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 86 GFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILA 165
Cdd:cd03218 78 GYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 166 DEPTGALDTKTSTQIMDLFYELNKQGstI-IMIT-HD-REIGEAAARQIVIRDGNV 218
Cdd:cd03218 158 DEPFAGVDPIAVQDIQKIIKILKDRG--IgVLITdHNvRETLSITDRAYIIYEGKV 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
21-221 |
2.47e-30 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 113.22 E-value: 2.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNmSETELAHVRnKEIGFVFQ--NFMLLPRl 98
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDIR-KKVGLVFQypEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 TALQNVELPLIYAGVDKKERRERSLAALTKVGL-----ADRAthlPNELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyedyKDKS---PFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446531755 174 TKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEAAARQIVIRDGNVVQD 221
Cdd:PRK13637 177 PKGRDEILNKIKELHKEyNMTIILVSHSMEdVAKLADRIIVMNKGKCELQ 226
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-221 |
2.83e-30 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 111.60 E-value: 2.83e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 25 DVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETElahvrnKEIGFVFQNFMLLPRLTALQNV 104
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 105 ELPLiYAGVDKKERRERSLAALT-KVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDL 183
Cdd:PRK10771 93 GLGL-NPGLKLNAAQREKLHAIArQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446531755 184 FYEL-NKQGSTIIMITHDREigEA---AARQIVIRDGNVVQD 221
Cdd:PRK10771 172 VSQVcQERQLTLLMVSHSLE--DAariAPRSLVVADGRIAWD 211
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
19-220 |
3.34e-30 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 116.73 E-value: 3.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKST----LMNIIgcldkPTTGTYELAGQNISNMSETELAHVRNKeIGFVFQ--NF 92
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLI-----NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQdpNS 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 93 MLLPRLTALQNVE--LPLIYAGVDKKERRERSLAALTKVGLADRATH-LPNELSGGQKQRVAVARAIVNNPKFILADEPT 169
Cdd:PRK15134 374 SLNPRLNVLQIIEegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPT 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446531755 170 GALDTKTSTQIMDLFYEL-NKQGSTIIMITHDREIGEAAARQ-IVIRDGNVVQ 220
Cdd:PRK15134 454 SSLDKTVQAQILALLKSLqQKHQLAYLFISHDLHVVRALCHQvIVLRQGEVVE 506
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
10-220 |
3.87e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 112.54 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 10 SFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvrNKEIGFVF 89
Cdd:PRK13648 14 SFQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 90 QNfmllPR-----LTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:PRK13648 90 QN----PDnqfvgSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELNKQGS-TIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAMEADHVIVMNKGTVYK 222
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-219 |
5.80e-30 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 112.51 E-value: 5.80e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLDkPTTGTYELAGQNISnmsetelAH 79
Cdd:COG4152 1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIIlGILA-PDSGEVLWDGEPLD-------PE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRNKeIGFvfqnfM-----LLPRLTALQNvelpLIY----AGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRV 150
Cdd:COG4152 69 DRRR-IGY-----LpeergLYPKMKVGEQ----LVYlarlKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIV-IRDGNVV 219
Cdd:COG4152 139 QLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIViINKGRKV 208
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
19-221 |
5.99e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 111.40 E-value: 5.99e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLdKPTTGTYELAGQNISNMSETELAHVR-----NKEIGFVFqnf 92
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELARRRavlpqHSSLSFPF--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 93 mllprlTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV------NNPKFILAD 166
Cdd:PRK13548 92 ------TVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 167 EPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDreIGEAAA---RQIVIRDGNVVQD 221
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHD--LNLAARyadRIVLLHQGRLVAD 222
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-200 |
6.13e-30 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 113.08 E-value: 6.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLDKPTTGT---YELAGQNISNMSETE 76
Cdd:COG4170 3 LLDIRNLTIEIDTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDNWHVTadrFRWNGIDLLKLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 77 LAHVRNKEIGFVFQNFM--LLPRLTALQNVE--LPLIYAGVD----KKERRERSLAALTKVGLADratH------LPNEL 142
Cdd:COG4170 83 RRKIIGREIAMIFQEPSscLDPSAKIGDQLIeaIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKD---HkdimnsYPHEL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 143 SGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNK-QGSTIIMITHD 200
Cdd:COG4170 160 TEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHD 218
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-220 |
1.06e-29 |
|
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: 110.32 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSeteLAHVRNKeIGFVFQNFMLLPR 97
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN---LRWLRSQ-IGLVSQEPVLFDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 lTALQNVELPLIYAGVDKKERrerslaALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVNNPKFILAD 166
Cdd:cd03249 92 -TIAENIRYGKPDATDEEVEE------AAKKANIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILLLD 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446531755 167 EPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:cd03249 165 EATSALDAESEKLVQEALDRA-MKGRTTIVIAHRLSTIRNADLIAVLQNGQVVE 217
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-206 |
1.29e-29 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 109.80 E-value: 1.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 15 AESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvrNKEIGFVFQNFML 94
Cdd:PRK10247 17 AGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY----RQQVSYCAQTPTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 LPRlTALQNVELPliYAGVDKKERRERSLAALTKVGLADRATHLP-NELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK10247 93 FGD-TVYDNLIFP--WQIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEITSALD 169
|
170 180 190
....*....|....*....|....*....|....*
gi 446531755 174 TKTSTQIMDLFYELNK-QGSTIIMITHDR-EIGEA 206
Cdd:PRK10247 170 ESNKHNVNEIIHRYVReQNIAVLWVTHDKdEINHA 204
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
19-199 |
1.94e-29 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 110.32 E-value: 1.94e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCL-----DKPTTGTYELAGQNISNmSETELAHVRnKEIGFVFQNFM 93
Cdd:PRK14267 18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVR-REVGMVFQYPN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 94 LLPRLTALQNVELPLIYAGV--DKKERRERSLAALTKVGL----ADRATHLPNELSGGQKQRVAVARAIVNNPKFILADE 167
Cdd:PRK14267 96 PFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDE 175
|
170 180 190
....*....|....*....|....*....|..
gi 446531755 168 PTGALDTKTSTQIMDLFYELnKQGSTIIMITH 199
Cdd:PRK14267 176 PTANIDPVGTAKIEELLFEL-KKEYTIVLVTH 206
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-213 |
3.58e-29 |
|
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: 113.92 E-value: 3.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVQilhGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelAHVR 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRPALR---PVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADAD----ADSW 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRlTALQNVELPLIYAGVDKKERrerslaALTKVGLADRATHLP-----------NELSGGQKQRV 150
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAG-TIAENIRLARPDASDAEIRE------ALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRL 467
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVI 213
Cdd:TIGR02857 468 ALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAALADRIVVL 529
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
21-199 |
5.03e-29 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 109.09 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLM---NIIGCLDK--PTTGTYELAGQNISNmSETELAHVRnKEIGFVFQNFMLL 95
Cdd:PRK14239 21 LNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLNPevTITGSIVYNGHNIYS-PRTDTVDLR-KEIGMVFQQPNPF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PrLTALQNVELPLIYAGVDKKERR----ERSLAALT-----KVGLADRAThlpnELSGGQKQRVAVARAIVNNPKFILAD 166
Cdd:PRK14239 99 P-MSIYENVVYGLRLKGIKDKQVLdeavEKSLKGASiwdevKDRLHDSAL----GLSGGQQQRVCIARVLATSPKIILLD 173
|
170 180 190
....*....|....*....|....*....|...
gi 446531755 167 EPTGALDTKTSTQIMDLFYELnKQGSTIIMITH 199
Cdd:PRK14239 174 EPTSALDPISAGKIEETLLGL-KDDYTMLLVTR 205
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
19-220 |
6.01e-29 |
|
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: 108.47 E-value: 6.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvrNKEIGFVFQNfMLLPRL 98
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSL----RRAIGVVPQD-TVLFND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 TALQNVElpliYAGVDKKErrERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVNNPKFILADE 167
Cdd:cd03253 90 TIGYNIR----YGRPDATD--EEVIEAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIARAILKNPPILLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446531755 168 PTGALDTKTSTQIMDLFYELNKqGSTIIMITHD-REIGEaAARQIVIRDGNVVQ 220
Cdd:cd03253 164 ATSALDTHTEREIQAALRDVSK-GRTTIVIAHRlSTIVN-ADKIIVLKDGRIVE 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
2-221 |
6.71e-29 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 107.68 E-value: 6.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvr 81
Cdd:cd03245 3 IEFRNVSFSYPN--QEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRlTALQNVELPLIYAgvdkkeRRERSLAALTKVGLADRATHLPN-----------ELSGGQKQRV 150
Cdd:cd03245 77 RRNIGYVPQDVTLFYG-TLRDNITLGAPLA------DDERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAV 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:cd03245 150 ALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQL-LGDKTLIIITHRPSLLDLVDRIIVMDSGRIVAD 219
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
1-218 |
8.16e-29 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 109.05 E-value: 8.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNisnMSETELAHV 80
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDL---LTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKeIGFVFQN----FMllpRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAI 156
Cdd:PRK13650 80 RHK-IGMVFQNpdnqFV---GATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIVIRDGNV 218
Cdd:PRK13650 156 AMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNGQV 218
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
5-220 |
9.17e-29 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 108.47 E-value: 9.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 5 KGITKSFQNGAEsvqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGT--YELAG---QNISNMSETELAH 79
Cdd:PRK11701 10 RGLTKLYGPRKG----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhYRMRDgqlRDLYALSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRNKEIGFVFQNFM--LLPRLTALQNVELPLIYAGVDKKER-RERSLAALTKVGL-ADRATHLPNELSGGQKQRVAVARA 155
Cdd:PRK11701 86 LLRTEWGFVHQHPRdgLRMQVSAGGNIGERLMAVGARHYGDiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARN 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 156 IVNNPKFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHDreIGEA---AARQIVIRDGNVVQ 220
Cdd:PRK11701 166 LVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHD--LAVArllAHRLLVMKQGRVVE 232
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
19-199 |
2.51e-28 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 111.68 E-value: 2.51e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTT---GTYELAGQNIsnmsETELAHVRNkeiGFVFQNFMLL 95
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPI----DAKEMRAIS---AYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PRLTALQNvelpLIY-------AGVDKKERRERSLAALTKVGL---ADRATHLPNE---LSGGQKQRVAVARAIVNNPKF 162
Cdd:TIGR00955 112 PTLTVREH----LMFqahlrmpRRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPL 187
|
170 180 190
....*....|....*....|....*....|....*..
gi 446531755 163 ILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:TIGR00955 188 LFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH 224
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
20-219 |
2.56e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 107.41 E-value: 2.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnKEIGFVFQNFMLLPRLT 99
Cdd:PRK11231 17 ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQHHLTPEGIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVEL---P-LIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTK 175
Cdd:PRK11231 93 VRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446531755 176 TSTQIMDLFYELNKQGSTIIMITHDReigEAAARQ----IVIRDGNVV 219
Cdd:PRK11231 173 HQVELMRLMRELNTQGKTVVTVLHDL---NQASRYcdhlVVLANGHVM 217
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
17-220 |
3.04e-28 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 111.74 E-value: 3.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 17 SVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsetELAHVR-NKEIGFVFQNFMLL 95
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLV-----QYDHHYlHRQVALVGQEPVLF 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PRlTALQNvelplIYAGVDKKERrERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:TIGR00958 568 SG-SVREN-----IAYGLTDTPD-EEIMAAAKAANAHDFIMEFPNgydtevgekgsQLSGGQKQRIAIARALVRKPRVLI 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 165 ADEPTGALDtktsTQIMDLFYELNKQGS-TIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:TIGR00958 641 LDEATSALD----AECEQLLQESRSRASrTVLLIAHRLSTVERADQILVLKKGSVVE 693
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
20-222 |
3.17e-28 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 105.73 E-value: 3.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVrnkeIGFvfQNFMLlPRLT 99
Cdd:PRK13539 17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY----LGH--RNAMK-PALT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVELpliYAGVdKKERRERSLAALTKVGLADrATHLP-NELSGGQKQRVAVAR-AIVNNPKFILaDEPTGALDTKTS 177
Cdd:PRK13539 90 VAENLEF---WAAF-LGGEELDIAAALEAVGLAP-LAHLPfGYLSAGQKRRVALARlLVSNRPIWIL-DEPTAALDAAAV 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 178 TQIMDLFYELNKQGSTIIMITHdREIGEAAARQIVIRDGNVVQDW 222
Cdd:PRK13539 164 ALFAELIRAHLAQGGIVIAATH-IPLGLPGARELDLGPFAAEDPA 207
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-199 |
3.67e-28 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 107.51 E-value: 3.67e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQ-NGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMS-ETELA 78
Cdd:PRK13643 1 MIKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 79 HVRnKEIGFVFQ-NFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRA-THLPNELSGGQKQRVAVARAI 156
Cdd:PRK13643 81 PVR-KKVGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGIL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQTVVLVTH 202
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
26-221 |
6.02e-28 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 105.32 E-value: 6.02e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 26 VTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNisnmsetelAHVRNKEIGFVFQ------NFMLLPRLT 99
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGAS---------PGKGWRHIGYVPQrhefawDFPISVAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALqNVELPLIyaGVDKKERRERSLA---ALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKT 176
Cdd:TIGR03771 72 VM-SGRTGHI--GWLRRPCVADFAAvrdALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPT 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 177 STQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:TIGR03771 149 QELLTELFIELAGAGTAILMTTHDLAQAMATCDRVVLLNGRVIAD 193
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-219 |
9.03e-28 |
|
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: 104.67 E-value: 9.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsetelAHVR 81
Cdd:cd03269 1 LEVENVTKRFG----RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD-------IAAR 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKeIGFVFQNFMLLPRLTALQNvelpLIY----AGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:cd03269 70 NR-IGYLPEERGLYPKMKVIDQ----LVYlaqlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVI 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDRE-IGEAAARQIVIRDGNVV 219
Cdd:cd03269 145 HDPELLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMElVEELCDRVLLLNKGRAV 207
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
12-220 |
1.68e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 106.47 E-value: 1.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 12 QNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYEL----AGQNISNMSETELAHVRN----- 82
Cdd:PRK13631 33 EKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITNPYSKKiknfk 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 83 ---KEIGFVFQ--NFMLLpRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADraTHL---PNELSGGQKQRVAVAR 154
Cdd:PRK13631 113 elrRRVSMVFQfpEYQLF-KDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDD--SYLersPFGLSGGQKRRVAIAG 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 155 AIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDRE-IGEAAARQIVIRDGNVVQ 220
Cdd:PRK13631 190 ILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEhVLEVADEVIVMDKGKILK 256
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
19-169 |
1.79e-27 |
|
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 104.53 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHvrnKEIGFVFQNFMLLPRL 98
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERAR---AGIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 99 TALQNVELPLIYAGVDKKERRERSLA---ALTKVgLADRAthlpNELSGGQKQRVAVARAIVNNPKFILADEPT 169
Cdd:TIGR03410 91 TVEENLLTGLAALPRRSRKIPDEIYElfpVLKEM-LGRRG----GDLSGGQQQQLAIARALVTRPKLLLLDEPT 159
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
20-200 |
1.87e-27 |
|
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: 108.99 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTL-MNIIGCLDkPTTGTYELAGQNISNMSETELAHVrnkeIGFVFQNfmllPRL 98
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLlATLAGLLD-PLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQD----AHL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 ---TALQNVELpliyAGVDKKErrERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:TIGR02868 421 fdtTVRENLRL----ARPDATD--EELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILL 494
|
170 180 190
....*....|....*....|....*....|....*..
gi 446531755 165 ADEPTGALDTKTSTQIM-DLFYELnkQGSTIIMITHD 200
Cdd:TIGR02868 495 LDEPTEHLDAETADELLeDLLAAL--SGRTVVLITHH 529
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-219 |
3.15e-27 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 108.21 E-value: 3.15e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETeLAHV 80
Cdd:PRK15439 11 LLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPA-KAHQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNkeIGFVFQNFMLLPRLTALQNvelplIYAGVDKKERRERSLAALtkvgLADRATHLPNELSGG-----QKQRVAVARA 155
Cdd:PRK15439 86 LG--IYLVPQEPLLFPNLSVKEN-----ILFGLPKRQASMQKMKQL----LAALGCQLDLDSSAGslevaDRQIVEILRG 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 156 IVNNPKFILADEPTGALdtkTSTQIMDLF---YELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:PRK15439 155 LMRDSRILILDEPTASL---TPAETERLFsriRELLAQGVGIVFISHKlPEIRQLADRISVMRDGTIA 219
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
10-221 |
3.35e-27 |
|
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: 103.85 E-value: 3.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 10 SFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsETELAHVRNKeIGFVF 89
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVR---DYTLASLRRQ-IGLVS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 90 QNFMLLPRlTALQNVElpliYAGVDkkERRERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVN 158
Cdd:cd03251 83 QDVFLFND-TVAENIA----YGRPG--ATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLK 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 159 NPKFILADEPTGALDTKTSTQIMDLFYELNKqGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:cd03251 156 DPPILILDEATSALDTESERLVQAALERLMK-NRTTFVIAHRLSTIENADRIVVLEDGKIVER 217
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-219 |
4.32e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 104.68 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESvqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSEteLAHV 80
Cdd:PRK13644 1 MIRLENVSYSYPDGTPA---LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSK--LQGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQN--FMLLPRLT------ALQNVELPLIyagvdkkERRERSLAALTKVGLADRATHLPNELSGGQKQRVAV 152
Cdd:PRK13644 76 R-KLVGIVFQNpeTQFVGRTVeedlafGPENLCLPPI-------EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVAL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 153 ARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVV 219
Cdd:PRK13644 148 AGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-219 |
7.21e-27 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 107.18 E-value: 7.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYelagqNISNMSETELAHV 80
Cdd:PRK09700 5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTI-----TINNINYNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKE--IGFVFQNFMLLPRLTALQNvelplIYAG------------VDKKERRERSLAALTKVGLADRATHLPNELSGGQ 146
Cdd:PRK09700 76 LAAQlgIGIIYQELSVIDELTVLEN-----LYIGrhltkkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISH 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 147 KQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:PRK09700 151 KQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKlAEIRRICDRYTVMKDGSSV 224
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
2-221 |
1.32e-26 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 106.87 E-value: 1.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNgaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHvr 81
Cdd:TIGR03375 464 IEFRNVSFAYPG--QETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRR-- 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nkEIGFVFQNfmllPRL---TALQNVELPLIYAgvdkkeRRERSLAALTKVGLADRATHLPN-----------ELSGGQK 147
Cdd:TIGR03375 540 --NIGYVPQD----PRLfygTLRDNIALGAPYA------DDEEILRAAELAGVTEFVRRHPDgldmqigergrSLSGGQR 607
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 148 QRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDlfyELNK--QGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:TIGR03375 608 QAVALARALLRDPPILLLDEPTSAMDNRSEERFKD---RLKRwlAGKTLVLVTHRTSLLDLVDRIIVMDNGRIVAD 680
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
10-221 |
1.58e-26 |
|
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: 102.18 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 10 SFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvrNKEIGFVF 89
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL----RRQVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 90 QNFMLLPRlTALQNVELpliyagVDKKERRERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVN 158
Cdd:cd03252 83 QENVLFNR-SIRDNIAL------ADPGMSMERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIAIARALIH 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 159 NPKFILADEPTGALDTKTSTQIMDLFYELNKqGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:cd03252 156 NPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLSTVKNADRIIVMEKGRIVEQ 217
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
21-219 |
1.71e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 103.16 E-value: 1.71e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNI-SNMSETELAHVRNKEIGFVFQ--NFMLLPR 97
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpANLKKIKEVKRLRKEIGLVFQfpEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 lTALQNVELPLIYAGVDKKERRERSLAALTKVGLA-DRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKT 176
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 177 STQIMDLFYELNK-QGSTIIMITHDR-EIGEAAARQIVIRDGNVV 219
Cdd:PRK13645 186 EEDFINLFERLNKeYKKRIIMVTHNMdQVLRIADEVIVMHEGKVI 230
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
4-199 |
1.93e-26 |
|
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: 101.58 E-value: 1.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKpttGTYELAGQNISNMSETELAHVRnK 83
Cdd:cd03234 6 WWDVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE---GGGTTSGQILFNGQPRKPDQFQ-K 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTalqnVELPLIYAGV-------DKKERRER-SLAALTKVGLADRATHLPNELSGGQKQRVAVARA 155
Cdd:cd03234 82 CVAYVRQDDILLPGLT----VRETLTYTAIlrlprksSDAIRKKRvEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQ 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446531755 156 IVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:cd03234 158 LLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIH 201
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
10-221 |
1.95e-26 |
|
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: 100.47 E-value: 1.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 10 SFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETelahvRNKEIGFVF 89
Cdd:cd03247 7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 90 QNFMLLPRlTALQNVELPLiyagvdkkerrerslaaltkvgladrathlpnelSGGQKQRVAVARAIVNNPKFILADEPT 169
Cdd:cd03247 82 QRPYLFDT-TLRNNLGRRF----------------------------------SGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446531755 170 GALDTKTSTQIMDLFYELNKqGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHMDKILFLENGKIIMQ 177
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
20-211 |
2.23e-26 |
|
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: 100.51 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsetELAHVRNKEIGFVFQNFMLLPRLT 99
Cdd:TIGR01189 15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKPELS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVELpliYAGVDKKERRErSLAALTKVGLADRAtHLP-NELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTST 178
Cdd:TIGR01189 90 ALENLHF---WAAIHGGAQRT-IEDALAAVGLTGFE-DLPaAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVA 164
|
170 180 190
....*....|....*....|....*....|...
gi 446531755 179 QIMDLFYELNKQGSTIIMITHdREIGEAAARQI 211
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH-QDLGLVEAREL 196
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-218 |
2.43e-26 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 104.92 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhv 80
Cdd:PRK09536 3 MIDVSDLSVEFG----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 rnKEIGFVFQNFMLLPRLTALQNVEL---PLI--YAGVDKKERR--ERSLAALTKVGLADRAThlpNELSGGQKQRVAVA 153
Cdd:PRK09536 77 --RRVASVPQDTSLSFEFDVRQVVEMgrtPHRsrFDTWTETDRAavERAMERTGVAQFADRPV---TSLSGGERQRVLLA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIgeaAARQ----IVIRDGNV 218
Cdd:PRK09536 152 RALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDL---AARYcdelVLLADGRV 217
|
|
| COG4674 |
COG4674 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
4-205 |
3.12e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443710 [Multi-domain] Cd Length: 250 Bit Score: 101.73 E-value: 3.12e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRnk 83
Cdd:COG4674 13 VEDLTVSF----DGFKALNDLSLYVDPGELRVIIGPNGAGKTTLMDVITGKTRPDSGSVLFGGTDLTGLDEHEIARLG-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 eIGFVFQNFMLLPRLTALQNVEL---------PLIYAGVDKkERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVAR 154
Cdd:COG4674 87 -IGRKFQKPTVFEELTVFENLELalkgdrgvfASLFARLTA-EERDRIEEVLETIGLTDKADRLAGLLSHGQKQWLEIGM 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 155 AIVNNPKFILADEPT-GALDTKTStQIMDLFYELNKQgSTIIMITHD----REIGE 205
Cdd:COG4674 165 LLAQDPKLLLLDEPVaGMTDAETE-RTAELLKSLAGK-HSVVVVEHDmefvRQIAR 218
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-219 |
4.04e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 102.23 E-value: 4.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESvqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsNMSETELAHV 80
Cdd:PRK13636 5 ILKVEELNYNYSDGTHA---LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQN-FMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLA---DRATHLpneLSGGQKQRVAVARAI 156
Cdd:PRK13636 81 R-ESVGMVFQDpDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEhlkDKPTHC---LSFGQKKRVAIAGVL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEA-AARQIVIRDGNVV 219
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLyCDNVFVMKEGRVI 221
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
18-221 |
7.10e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 101.32 E-value: 7.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvrNKEIGFVFQN----FM 93
Cdd:PRK13642 20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNL----RRKIGMVFQNpdnqFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 94 llpRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK13642 96 ---GATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLD 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446531755 174 TKTSTQIMDLFYEL-NKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:PRK13642 173 PTGRQEIMRVIHEIkEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-216 |
9.55e-26 |
|
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: 104.14 E-value: 9.55e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIgCLDKPtTGTYElaGQNISNMSETELAHV 80
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKIL-SGVYP-HGTWD--GEIYWSGSPLKASNI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKE---IGFVFQNFMLLPRLTALQNV----ELPLIYAGVDKKERRERSLAALTKVGLADRATHLP-NELSGGQKQRVAV 152
Cdd:TIGR02633 73 RDTEragIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 153 ARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQI-VIRDG 216
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTIcVIRDG 217
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
20-220 |
1.33e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 100.12 E-value: 1.33e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDK------PTTGTYELAGQNISNMSETELahvrNKEIGFVFQNFM 93
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydskiKVDGKVLYFGKDIFQIDAIKL----RKEVGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 94 LLPRLTALQNVELPLIYAGV-DKKERRERSLAALTKVGL----ADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEP 168
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGIkEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446531755 169 TGALDTKTSTQIMDLFYELNKQgSTIIMITHD-REIGEAAARQIVIRDGNVVQ 220
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNpQQVARVADYVAFLYNGELVE 232
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
1-224 |
1.68e-25 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 100.25 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGA-----ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSet 75
Cdd:PRK15112 4 LLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 76 elAHVRNKEIGFVFQN--FMLLPRLTALQNVELPLIY-AGVDKKERRERSLAALTKVGL-ADRATHLPNELSGGQKQRVA 151
Cdd:PRK15112 82 --YSYRSQRIRMIFQDpsTSLNPRQRISQILDFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 152 VARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELN-KQGSTIIMITHDREIGEAAARQI-VIRDGNVVQdwRG 224
Cdd:PRK15112 160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQeKQGISYIYVTQHLGMMKHISDQVlVMHQGEVVE--RG 232
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-218 |
2.17e-25 |
|
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: 98.70 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 3 NLKGITKsFQNGAES------VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnMSETE 76
Cdd:cd03248 7 HLKGIVK-FQNVTFAyptrpdTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPIS-QYEHK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 77 LAHvrnKEIGFVFQNFMLLPRLTA------LQNVELPLIYAGVDKKErrERSLAALTKVGLADRATHLPNELSGGQKQRV 150
Cdd:cd03248 85 YLH---SKVSLVGQEPVLFARSLQdniaygLQSCSFECVKEAAQKAH--AHSFISELASGYDTEVGEKGSQLSGGQKQRV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNkQGSTIIMITHDREIGEAAARQIVIRDGNV 218
Cdd:cd03248 160 AIARALIRNPQVLILDEATSALDAESEQQVQQALYDWP-ERRTVLVIAHRLSTVERADQILVLDGGRI 226
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-218 |
2.72e-25 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 98.95 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQngaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelAHV 80
Cdd:COG1137 3 TLEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLP----MHK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKE-IGF------VFQnfmllpRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVA 153
Cdd:COG1137 75 RARLgIGYlpqeasIFR------KLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGstI-IMIT-HD-REIGEAAARQIVIRDGNV 218
Cdd:COG1137 149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHLKERG--IgVLITdHNvRETLGICDRAYIISEGKV 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
20-220 |
2.79e-25 |
|
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: 102.90 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLdKPTTGTYELAGQNISNMSETELA-HvrnkeIGFvfqnfmlLPr 97
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELGrH-----IGY-------LP- 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 ltalQNVELpliYAG-----------VDkkerRERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARA 155
Cdd:COG4618 413 ----QDVEL---FDGtiaeniarfgdAD----PEKVVAAAKLAGVHEMILRLPDgydtrigeggaRLSGGQRQRIGLARA 481
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 156 IVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:COG4618 482 LYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQA 546
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-216 |
4.37e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 102.21 E-value: 4.37e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvR 81
Cdd:PRK11160 339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---R 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKeIGFVFQNFMLLPRlTALQNVELpliyagVDKKERRERSLAALTKVGLAdraTHLPNE-------------LSGGQKQ 148
Cdd:PRK11160 414 QA-ISVVSQRVHLFSA-TLRDNLLL------AAPNASDEALIEVLQQVGLE---KLLEDDkglnawlgeggrqLSGGEQR 482
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 149 RVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHdREIGEAAARQIVIRDG 216
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITH-RLTGLEQFDRICVMDN 548
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
20-218 |
5.14e-25 |
|
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 102.04 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnKEIGFVFQNFMLLPRlT 99
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVELFPG-T 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVelpliyAGVDKKERRERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVNNPKFILADEP 168
Cdd:TIGR01842 408 VAENI------ARFGENADPEKIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446531755 169 TGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNV 218
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRI 531
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-220 |
5.47e-25 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 102.24 E-value: 5.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRnKEIGFVFQN--FMLL 95
Cdd:PRK10261 337 VHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQFIFQDpyASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PRLTALQNVELPLIYAGV-DKKERRERSLAALTKVGL-ADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK10261 416 PRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALD 495
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446531755 174 TKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQI-VIRDGNVVQ 220
Cdd:PRK10261 496 VSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVaVMYLGQIVE 544
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-223 |
6.79e-25 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 101.81 E-value: 6.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYEL-AGQNIsnmsetelahvrnkeigfvfqnfMLLPrl 98
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARV-----------------------LFLP-- 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 talQNVELP-------LIYAGVDKKERRERSLAALTKVGLADRATHL------PNELSGGQKQRVAVARAIVNNPKFILA 165
Cdd:COG4178 433 ---QRPYLPlgtlreaLLYPATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 166 DEPTGALDTKTSTQIMDLFYElNKQGSTIIMITHDREIGEAAARQIVIRDGnvvQDWR 223
Cdd:COG4178 510 DEATSALDEENEAALYQLLRE-ELPGTTVISVGHRSTLAAFHDRVLELTGD---GSWQ 563
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
16-220 |
8.97e-25 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 97.45 E-value: 8.97e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 16 ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDK--PTTGTYELAGQNISNMSETELAHvrnKEIGFVFQ--- 90
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDERAR---AGIFLAFQypv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 91 ------NFMLLprLTALQNVELPLIYAGVDKKERRErslaALTKVGL----ADRAThlpNE-LSGGQKQRVAVARAIVNN 159
Cdd:COG0396 88 eipgvsVSNFL--RTALNARRGEELSAREFLKLLKE----KMKELGLdedfLDRYV---NEgFSGGEKKRNEILQMLLLE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 160 PKFILADEPTGALDTKtSTQIM-DLFYELNKQGSTIIMITHDREIGE--AAARQIVIRDGNVVQ 220
Cdd:COG0396 159 PKLAILDETDSGLDID-ALRIVaEGVNKLRSPDRGILIITHYQRILDyiKPDFVHVLVDGRIVK 221
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
20-219 |
1.07e-24 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 98.13 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnKEIGFVFQNFMLLPRLT 99
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDIT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNV------ELPLIYAGvdKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK10253 98 VQELVargrypHQPLFTRW--RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446531755 174 TKTSTQIMDLFYELNK-QGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:PRK10253 176 ISHQIDLLELLSELNReKGYTLAAVLHDlNQACRYASHLIALREGKIV 223
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-216 |
1.10e-24 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 101.16 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIgCLDKPTtGTYElaGQNISNMSETELAHVRNK 83
Cdd:PRK13549 8 MKNITKTF----GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPH-GTYE--GEIIFEGEELQASNIRDT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 E---IGFVFQNFMLLPRLTALQNVEL--PLIYAGV-DKKERRERSLAALTKVGLaDRATHLP-NELSGGQKQRVAVARAI 156
Cdd:PRK13549 80 EragIAIIHQELALVKELSVLENIFLgnEITPGGImDYDAMYLRAQKLLAQLKL-DINPATPvGNLGLGQQQLVEIAKAL 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQI-VIRDG 216
Cdd:PRK13549 159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTIcVIRDG 219
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
20-219 |
1.46e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 97.95 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKeIGFVFQN----FMll 95
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIREK-VGIVFQNpdnqFV-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 pRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTK 175
Cdd:PRK13640 99 -GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 176 TSTQIMDLFYEL-NKQGSTIIMITHDREIGEAAARQIVIRDGNVV 219
Cdd:PRK13640 178 GKEQILKLIRKLkKKNNLTVISITHDIDEANMADQVLVLDDGKLL 222
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-220 |
2.04e-24 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 100.37 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQnisnmsETELAHVR-- 81
Cdd:PRK11288 7 FDGIGKTF----PGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ------EMRFASTTaa 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 -NKEIGFVFQNFMLLPRLTALQNV---ELPLIYAGVDKKERRERSLAALTKVGLA-DRATHLpNELSGGQKQRVAVARAI 156
Cdd:PRK11288 77 lAAGVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDiDPDTPL-KYLSIGQRQMVEIAKAL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHdR--EIGEAAARQIVIRDGNVVQ 220
Cdd:PRK11288 156 ARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRVILYVSH-RmeEIFALCDAITVFKDGRYVA 220
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-224 |
3.49e-24 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 99.75 E-value: 3.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqnGAEsvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAgqnisnmsetelahvRNK 83
Cdd:COG0488 1 LENLSKSF--GGR--PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGL 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTALQNVE--LPLIYAGVDKKERRERSLA------------------------------ALTKVGL 131
Cdd:COG0488 62 RIGYLPQEPPLDDDLTVLDTVLdgDAELRALEAELEELEAKLAepdedlerlaelqeefealggweaearaeeILSGLGF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 132 ADRATHLP-NELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTstqIMDLfyE--LNKQGSTIIMITHDREIGEAAA 208
Cdd:COG0488 142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWL--EefLKNYPGTVLVVSHDRYFLDRVA 216
|
250
....*....|....*.
gi 446531755 209 RQIVIRDGNVVQDWRG 224
Cdd:COG0488 217 TRILELDRGKLTLYPG 232
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
22-199 |
4.58e-24 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 94.87 E-value: 4.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 22 HGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETelahvrnkeigfVFQNFMLL------ 95
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE------------YHQDLLYLghqpgi 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 -PRLTALQNVelpLIYAGVDKKERRERSLAALTKVGLADRAtHLP-NELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK13538 86 kTELTALENL---RFYQRLHGPGDDEALWEALAQVGLAGFE-DVPvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
|
170 180
....*....|....*....|....*.
gi 446531755 174 TKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-219 |
1.87e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.44 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELaGQNIsnmsetelahv 80
Cdd:COG0488 315 VLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 rnkEIGFVFQNFMLL-PRLTALQNVElpliYAGVDKKERRERSLA---------ALTKVGladrathlpnELSGGQKQRV 150
Cdd:COG0488 379 ---KIGYFDQHQEELdPDKTVLDELR----DGAPGGTEQEVRGYLgrflfsgddAFKPVG----------VLSGGEKARL 441
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTSTQIMDLfyeLNKQGSTIIMITHDRE-IGEAAARQIVIRDGNVV 219
Cdd:COG0488 442 ALAKLLLSPPNVLLLDEPTNHLDIETLEALEEA---LDDFPGTVLLVSHDRYfLDRVATRILEFEDGGVR 508
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
19-220 |
2.55e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 97.22 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHG-IDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLdkPTTGTYELAGQNISNMsetELAHVRnKEIGFVFQNfMLLP 96
Cdd:PRK11174 363 KTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKINGIELREL---DPESWR-KHLSWVGQN-PQLP 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 97 RLTALQNVELpliyAGVDKKErrERSLAALTKVGLADRATHLPN-----------ELSGGQKQRVAVARAIVNNPKFILA 165
Cdd:PRK11174 436 HGTLRDNVLL----GNPDASD--EQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLL 509
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 166 DEPTGALDTKTSTQIMDLFYElNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:PRK11174 510 DEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
16-219 |
4.05e-23 |
|
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: 92.20 E-value: 4.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 16 ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLD-KPTTGTYELAGQNISNMSETELAhvrNKEIGFVFQNfm 93
Cdd:cd03217 11 GGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImGHPKyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQY-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 94 llprltalqnvelPLIYAGVdKKERRERSLaaltkvgladrathlpNE-LSGGQKQRVAVARAIVNNPKFILADEPTGAL 172
Cdd:cd03217 86 -------------PPEIPGV-KNADFLRYV----------------NEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446531755 173 DTKTSTQIMDLFYELNKQGSTIIMITHDREIGEA--AARQIVIRDGNVV 219
Cdd:cd03217 136 DIDALRLVAEVINKLREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIV 184
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-205 |
7.81e-23 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 94.51 E-value: 7.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAesvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmSETELAHVR 81
Cdd:PRK13536 42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP--ARARLARAR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nkeIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:PRK13536 116 ---IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGE 205
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAE 236
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
23-200 |
9.06e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.75 E-value: 9.06e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 23 GIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrNKEIGFVFQNFMLLPRLTALQ 102
Cdd:PRK11300 23 NVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREMTVIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 103 N--------VELPLIyAGVDK--------KERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILAD 166
Cdd:PRK11300 100 NllvaqhqqLKTGLF-SGLLKtpafrraeSEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLD 178
|
170 180 190
....*....|....*....|....*....|....*
gi 446531755 167 EPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD 200
Cdd:PRK11300 179 EPAAGLNPKETKELDELIAELRNEhNVTVLLIEHD 213
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
20-220 |
1.09e-22 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 92.46 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKStlMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEIGFVFQNfmllPRlT 99
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQN----PR-S 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVELPLIYA-----GVDKKERRERSLAALTKVGLADRATHL---PNELSGGQKQRVAVARAIVNNPKFILADEPTGA 171
Cdd:PRK10418 91 AFNPLHTMHTHAretclALGKPADDATLTAALEAVGLENAARVLklyPFEMSGGMLQRMMIALALLCEAPFIIADEPTTD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446531755 172 LDTKTSTQIMDLFYEL-NKQGSTIIMITHDREIGEAAARQI-VIRDGNVVQ 220
Cdd:PRK10418 171 LDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLADDVaVMSHGRIVE 221
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
2-221 |
1.54e-22 |
|
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: 91.05 E-value: 1.54e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSF------------------QNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYE 63
Cdd:cd03220 1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 64 LAGQNISNMsetelahvrnkEIGFVFQnfmllPRLTALQNVELPLIYAGVDKKERRER-----SLAALTKVGladratHL 138
Cdd:cd03220 81 VRGRVSSLL-----------GLGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKideiiEFSELGDFI------DL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 139 P-NELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDG 216
Cdd:cd03220 139 PvKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDpSSIKRLCDRALVLEKG 218
|
....*
gi 446531755 217 NVVQD 221
Cdd:cd03220 219 KIRFD 223
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-220 |
1.55e-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: 94.87 E-value: 1.55e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYE-LAGQNISNMSET-ELAHVRNKE-IGFVFQNFML 94
Cdd:TIGR03269 297 VKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNvRVGDEWVDMTKPgPDGRGRAKRyIGILHQEYDL 376
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 LPRLTALQN------VELPLIYAgvdkkerRERSLAALTKVGLADRAT-----HLPNELSGGQKQRVAVARAIVNNPKFI 163
Cdd:TIGR03269 377 YPHRTVLDNlteaigLELPDELA-------RMKAVITLKMVGFDEEKAeeildKYPDELSEGERHRVALAQVLIKEPRIV 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 164 LADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEAAARQIVIRDGNVVQ 220
Cdd:TIGR03269 450 ILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDfVLDVCDRAALMRDGKIVK 508
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
4-221 |
4.57e-22 |
|
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: 90.47 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGA-ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGqNISnmSETELAHVRN 82
Cdd:cd03267 19 LIGSLKSLFKRKyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG-LVP--WKRRKKFLRR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 83 keIGFVF-QNFMLLPRLTALQNVEL-PLIYaGVDKKERRER--SLAALTKVGladRATHLP-NELSGGQKQRVAVARAIV 157
Cdd:cd03267 96 --IGVVFgQKTQLWWDLPVIDSFYLlAAIY-DLPPARFKKRldELSELLDLE---ELLDTPvRQLSLGQRMRAEIAAALL 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD-REIGEAAARQIVIRDGNVVQD 221
Cdd:cd03267 170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRErGTTVLLTSHYmKDIEALARRVLVIDKGRLLYD 235
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
12-216 |
5.65e-22 |
|
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: 89.07 E-value: 5.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 12 QNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLDKpTTGTYELAGQnisnmsetelahvrnkeIGFVFQ 90
Cdd:cd03250 12 SGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELEK-LSGSVSVPGS-----------------IAYVSQ 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 91 NFMLLPRlTALQNVELPLIYagvdKKERRERSLAA--------------LTKVGladrathlpnE----LSGGQKQRVAV 152
Cdd:cd03250 74 EPWIQNG-TIRENILFGKPF----DEERYEKVIKAcalepdleilpdgdLTEIG----------EkginLSGGQKQRISL 138
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 153 ARAIVNNPKFILADEPTGALDTKTSTQIMD-LFYELNKQGSTIIMITHDREIGEAAARQIVIRDG 216
Cdd:cd03250 139 ARAVYSDADIYLLDDPLSAVDAHVGRHIFEnCILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
4-220 |
5.93e-22 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 93.32 E-value: 5.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNgaesVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLdKPTtGTYElaGQNISNMSETELAHVRNK 83
Cdd:NF040905 4 MRGITKTFPG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPH-GSYE--GEILFDGEVCRFKDIRDS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 E---IGFVFQNFMLLPRLTALQNVEL---PLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIV 157
Cdd:NF040905 76 EalgIVIIHQELALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALS 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVVQ 220
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKlNEIRRVADSITVLRDGRTIE 219
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
2-205 |
6.26e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 91.41 E-value: 6.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqnGAESVqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsetELAHVR 81
Cdd:PRK13537 8 IDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVP-----SRARHA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRLTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:PRK13537 79 RQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPD 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGE 205
Cdd:PRK13537 159 VLVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAE 202
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-219 |
9.27e-22 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 90.23 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAhvrnKEIGFVFQNfmlLPRLT 99
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQ---LPAAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVELPLI--YA-----GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGAL 172
Cdd:PRK10575 99 GMTVRELVAIgrYPwhgalGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSAL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446531755 173 DTKTSTQIMDLFYELNKQ-GSTIIMITHDREIgeaAARQ----IVIRDGNVV 219
Cdd:PRK10575 179 DIAHQVDVLALVHRLSQErGLTVIAVLHDINM---AARYcdylVALRGGEMI 227
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
2-221 |
1.05e-21 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 92.88 E-value: 1.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAEsvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVR 81
Cdd:TIGR01193 474 IVINDVSYSYGYGSN---ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFI 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 N---KE----IGFVFQNFMLlprlTALQNVELPLIYAGVD----KKERRERSLAALTKvgLADRATHLpnelSGGQKQRV 150
Cdd:TIGR01193 551 NylpQEpyifSGSILENLLL----GAKENVSQDEIWAACEiaeiKDDIENMPLGYQTE--LSEEGSSI----SGGQKQRI 620
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTSTQIMDLFyeLNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:TIGR01193 621 ALARALLTDSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQ 689
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-213 |
2.14e-21 |
|
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: 92.00 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsnmsETELAHVRnKEIGFVFQNFMLLPRLTALQN 103
Cdd:TIGR01257 949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVR-QSLGMCPQHNILFHHLTVAEH 1023
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 104 VelpLIYAGVDKKERRERSL---AALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQI 180
Cdd:TIGR01257 1024 I---LFYAQLKGRSWEEAQLemeAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSI 1100
|
170 180 190
....*....|....*....|....*....|...
gi 446531755 181 MDLFYELnKQGSTIIMITHDREIGEAAARQIVI 213
Cdd:TIGR01257 1101 WDLLLKY-RSGRTIIMSTHHMDEADLLGDRIAI 1132
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-219 |
3.14e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 89.09 E-value: 3.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 17 SVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsETELAHVRnKEIGFVFQN---FM 93
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREVR-KFVGLVFQNpddQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 94 LLPrlTALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK13652 92 FSP--TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446531755 174 TKTSTQIMDLFYELNKQ-GSTIIMITHDRE-IGEAAARQIVIRDGNVV 219
Cdd:PRK13652 170 PQGVKELIDFLNDLPETyGMTVIFSTHQLDlVPEMADYIYVMDKGRIV 217
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-216 |
4.12e-21 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 90.83 E-value: 4.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIgcldkptTGTYEL-AGQNISNMSETELAHVRN 82
Cdd:PRK10762 7 LKGIDKAF----PGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVL-------TGIYTRdAGSILYLGKEVTFNGPKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 83 KE---IGFVFQNFMLLPRLTALQNV----ELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARA 155
Cdd:PRK10762 76 SQeagIGIIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 156 IVNNPKFILADEPTGAL-DTKTSTqimdLF---YELNKQGSTIIMITHD-REIGEAAARQIVIRDG 216
Cdd:PRK10762 156 LSFESKVIIMDEPTDALtDTETES----LFrviRELKSQGRGIVYISHRlKEIFEICDDVTVFRDG 217
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
20-211 |
4.75e-21 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 86.78 E-value: 4.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsetELAHVRNKEIGFVFQNFMLLPRLT 99
Cdd:cd03231 15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLD-----FQRDSIARGLLYLGHAPGIKTTLS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVELpliYAGVDKKERRERSLAALTKVGLADRATHlpnELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQ 179
Cdd:cd03231 90 VLENLRF---WHADHSDEQVEEALARVGLNGFEDRPVA---QLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
|
170 180 190
....*....|....*....|....*....|...
gi 446531755 180 IMDLFYELNKQGSTIIMITH-DREIGEAAARQI 211
Cdd:cd03231 164 FAEAMAGHCARGGMVVLTTHqDLGLSEAGAREL 196
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
21-216 |
7.19e-21 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 85.95 E-value: 7.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvRNKEIGFVfqnfmllprlta 100
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDA---IRAGIAYV------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 101 lqnvelPliyagvdkKERRERSLaaLTKVGLADRAThLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQI 180
Cdd:cd03215 81 ------P--------EDRKREGL--VLDLSVAENIA-LSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAEI 143
|
170 180 190
....*....|....*....|....*....|....*..
gi 446531755 181 MDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDG 216
Cdd:cd03215 144 YRLIRELADAGKAVLLISSElDELLGLCDRILVMYEG 180
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-216 |
9.66e-21 |
|
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: 84.42 E-value: 9.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAgqnisnmsetelahvR 81
Cdd:cd03221 1 IELENLSKTYGGK----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------S 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQnfmllprltalqnvelpliyagvdkkerrerslaaltkvgladrathlpneLSGGQKQRVAVARAIVNNPK 161
Cdd:cd03221 62 TVKIGYFEQ---------------------------------------------------LSGGEKMRLALAKLLLENPN 90
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 162 FILADEPTGALDTKTSTQIMDlfyELNKQGSTIIMITHDRE-IGEAAARQIVIRDG 216
Cdd:cd03221 91 LLLLDEPTNHLDLESIEALEE---ALKEYPGTVILVSHDRYfLDQVATKIIELEDG 143
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-220 |
9.67e-21 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.91 E-value: 9.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKS----TLMNIIgcldKPTTGTYELAGQ--------- 67
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLL----EQAGGLVQCDKMllrrrsrqv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 68 -NISNMSETELAHVRNKEIGFVFQNFM--LLPRLT-ALQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHL---PN 140
Cdd:PRK10261 88 iELSEQSAAQMRHVRGADMAMIFQEPMtsLNPVFTvGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTILsryPH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 141 ELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGST-IIMITHDRE-IGEAAARQIVIRDGNV 218
Cdd:PRK10261 168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMgVIFITHDMGvVAEIADRVLVMYQGEA 247
|
..
gi 446531755 219 VQ 220
Cdd:PRK10261 248 VE 249
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
5-199 |
9.84e-21 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 86.30 E-value: 9.84e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 5 KGITKSFQNGAesvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGqniSNMSETELahvrnKE 84
Cdd:TIGR03740 4 KNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDG---HPWTRKDL-----HK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 85 IGFVFQNFMLLPRLTALQNVELPLIYAGVDKkerrERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:TIGR03740 72 IGSLIESPPLYENLTARENLKVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLI 147
|
170 180 190
....*....|....*....|....*....|....*
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:TIGR03740 148 LDEPTNGLDPIGIQELRELIRSFPEQGITVILSSH 182
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-219 |
1.87e-20 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 88.01 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEIGFVFQNFMLLPRLTALQN 103
Cdd:PRK11144 17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 104 velpLIYaGVDKKERRE-RSLAALTKVG-LADRathLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIM 181
Cdd:PRK11144 97 ----LRY-GMAKSMVAQfDKIVALLGIEpLLDR---YPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446531755 182 DLFYELNKQGST-IIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:PRK11144 169 PYLERLAREINIpILYVSHSlDEILRLADRVVVLEQGKVK 208
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-221 |
2.04e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 87.45 E-value: 2.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSF-----QNGA------------ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLdKPTTGTY 62
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGLkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 63 ELAGQNISnmsETELAHVRNkeIGFVF-QNFMLLPRLTALQNVEL-PLIYaGVDKKERRERsLAALTKV----GLADRAT 136
Cdd:COG4586 80 RVLGYVPF---KRRKEFARR--IGVVFgQRSQLWWDLPAIDSFRLlKAIY-RIPDAEYKKR-LDELVELldlgELLDTPV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 137 HlpnELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD-REIGEAAARQIVIR 214
Cdd:COG4586 153 R---QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRErGTTILLTSHDmDDIEALCDRVIVID 229
|
....*..
gi 446531755 215 DGNVVQD 221
Cdd:COG4586 230 HGRIIYD 236
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
18-219 |
2.70e-20 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 85.70 E-value: 2.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMsetELAHVRNKEIGFVFQNFMLLPR 97
Cdd:PRK11614 18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDW---QTAKIMREAVAIVPEGRRVFSR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LTALQNVELPLIYAGVDK-KERRERSLAALTKvgLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKT 176
Cdd:PRK11614 95 MTVEENLAMGGFFAERDQfQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPII 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446531755 177 STQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:PRK11614 173 IQQIFDTIEQLREQGMTIFLVEQNaNQALKLADRGYVLENGHVV 216
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
34-221 |
2.85e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 86.30 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 34 TSIMGPSGSGKSTLMNIIGCLDKPTTG-TYE----LAGQNISNMSEteLAHVRnKEIGFVFQNFMLLPrLTALQNVELPL 108
Cdd:PRK14271 50 TSLMGPTGSGKTTFLRTLNRMNDKVSGyRYSgdvlLGGRSIFNYRD--VLEFR-RRVGMLFQRPNPFP-MSIMDNVLAGV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 109 -IYAGVDKKERRERSLAALTKVGL----ADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDL 183
Cdd:PRK14271 126 rAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEF 205
|
170 180 190
....*....|....*....|....*....|....*....
gi 446531755 184 FYELNKQgSTIIMITHD-REIGEAAARQIVIRDGNVVQD 221
Cdd:PRK14271 206 IRSLADR-LTVIIVTHNlAQAARISDRAALFFDGRLVEE 243
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
19-219 |
4.80e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 85.83 E-value: 4.80e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTL-MNIIGCLdKPTTGTYELAGQNIsNMSETELAHVRnKEIGFVFQNFMLLPR 97
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKPL-DYSKRGLLALR-QQVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LTAL-QNVELPLIYAGVDKKERRERSLAALTKVGlADRATHLPNE-LSGGQKQRVAVARAIVNNPKFILADEPTGALDTK 175
Cdd:PRK13638 92 YTDIdSDIAFSLRNLGVPEAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPA 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 176 TSTQIMDLFYELNKQGSTIIMITHDRE-IGEAAARQIVIRDGNVV 219
Cdd:PRK13638 171 GRTQMIAIIRRIVAQGNHVIISSHDIDlIYEISDAVYVLRQGQIL 215
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-200 |
5.45e-20 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 85.17 E-value: 5.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYElagqnisnmsetelaHV 80
Cdd:PRK09544 4 LVSLENVSVSFGQR----RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------------RN 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEIGFVFQNFMLLPRLtALQNVELPLIYAGVdkkeRRERSLAALTKVgladRATHLPN----ELSGGQKQRVAVARAI 156
Cdd:PRK09544 65 GKLRIGYVPQKLYLDTTL-PLTVNRFLRLRPGT----KKEDILPALKRV----QAGHLIDapmqKLSGGETQRVLLARAL 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD 200
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHD 180
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
19-219 |
5.96e-20 |
|
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 87.57 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvRnKEIGFVFQNfmllprl 98
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL---R-AAIGIVPQD------- 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 TALQN--VELPLIYA--GVDKKERRErslAAltkvgladRATH-------LPN-----------ELSGGQKQRVAVARAI 156
Cdd:COG5265 441 TVLFNdtIAYNIAYGrpDASEEEVEA---AA--------RAAQihdfiesLPDgydtrvgerglKLSGGEKQRVAIARTL 509
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 157 VNNPKFILADEPTGALDTKTSTQIMDlfyELNK--QGSTIIMITHdR--------EIgeaaarqIVIRDGNVV 219
Cdd:COG5265 510 LKNPPILIFDEATSALDSRTERAIQA---ALREvaRGRTTLVIAH-RlstivdadEI-------LVLEAGRIV 571
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
3-220 |
6.97e-20 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 87.32 E-value: 6.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 3 NLKG------ITKSFQNgaeSVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETE 76
Cdd:PRK13657 330 RVKGavefddVSFSYDN---SRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 77 LAHvrnkEIGFVFQNFMLLPRLTA--LQ-------NVELPL---IYAGVDKKERRERSLAalTKVGlaDRAthlpNELSG 144
Cdd:PRK13657 407 LRR----NIAVVFQDAGLFNRSIEdnIRvgrpdatDEEMRAaaeRAQAHDFIERKPDGYD--TVVG--ERG----RQLSG 474
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 145 GQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:PRK13657 475 GERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDEL-MKGRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-200 |
1.24e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLdkPTTGTYELAGQNISNMSETELAHVRnkeiGFVFQNFMLLPRLT 99
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHR----AYLSQQQSPPFAMP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQnvELPLIYAGVDKKERRERSLAALT-KVGLADRATHLPNELSGGQKQRVAVARAIV-----NNP--KFILADEPTGA 171
Cdd:COG4138 86 VFQ--YLALHQPAGASSEAVEQLLAQLAeALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPegQLLLLDEPMNS 163
|
170 180
....*....|....*....|....*....
gi 446531755 172 LDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:COG4138 164 LDVAQQAALDRLLRELCQQGITVVMSSHD 192
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-221 |
4.26e-19 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 82.44 E-value: 4.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQ------------------NGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTY 62
Cdd:COG1134 4 MIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 63 ELAGqNISNMseteLahvrnkEIGFVFQnfmllPRLTALQNVELP-LIYaGVDKKE--RRERSLAALTKVGladRATHLP 139
Cdd:COG1134 84 EVNG-RVSAL----L------ELGAGFH-----PELTGRENIYLNgRLL-GLSRKEidEKFDEIVEFAELG---DFIDQP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 140 -NELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDRE-IGEAAARQIVIRDGN 217
Cdd:COG1134 144 vKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGaVRRLCDRAIWLEKGR 223
|
....
gi 446531755 218 VVQD 221
Cdd:COG1134 224 LVMD 227
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
19-219 |
6.38e-19 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 82.25 E-value: 6.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHvrnKEIGFVFQNFMLLPRL 98
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 TALQNVELPL-IYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTS 177
Cdd:PRK10895 94 SVYDNLMAVLqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446531755 178 TQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:PRK10895 174 IDIKRIIEHLRDSGLGVLITDHNvRETLAVCERAYIVSQGHLI 216
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-200 |
7.76e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 82.24 E-value: 7.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESvqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISN-MSETELAHV 80
Cdd:PRK15056 7 IVVNDVTVTWRNGHTA---LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQaLQKNLVAYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 -RNKEIGFVF----QNFMLLPRLTALQNVELPliyagvdKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARA 155
Cdd:PRK15056 84 pQSEEVDWSFpvlvEDVVMMGRYGHMGWLRRA-------KKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 156 IVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:PRK15056 157 IAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHN 201
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
9-200 |
1.65e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 81.24 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 9 KSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLmniIGCLDK--------PTTGTYELAGQNISNmSETELAHV 80
Cdd:PRK14258 11 NNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTF---LKCLNRmnelesevRVEGRVEFFNQNIYE-RRVNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RnKEIGFVFQNFMLLPrLTALQNVELPLIYAGVDKK-ERRERSLAALTKVGLADRATHLPN----ELSGGQKQRVAVARA 155
Cdd:PRK14258 87 R-RQVSMVHPKPNLFP-MSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLWDEIKHKIHksalDLSGGQQQRLCIARA 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446531755 156 IVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGS-TIIMITHD 200
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHN 210
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
25-200 |
6.39e-18 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 79.83 E-value: 6.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 25 DVTLN--QGEFTSIMGPSGSGKSTL------MN--IIGCldkPTTGTYELAGQNIsNMSETELAHVRNKeIGFVFQNFML 94
Cdd:PRK14243 28 NVWLDipKNQITAFIGPSGCGKSTIlrcfnrLNdlIPGF---RVEGKVTFHGKNL-YAPDVDPVEVRRR-IGMVFQKPNP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 LPRlTALQNVEL-PLI--YAGvDKKERRERSL--AALTKvGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPT 169
Cdd:PRK14243 103 FPK-SIYDNIAYgARIngYKG-DMDELVERSLrqAALWD-EVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|.
gi 446531755 170 GALDTKTSTQIMDLFYELNKQgSTIIMITHD 200
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQ-YTIIIVTHN 209
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
1-200 |
1.22e-17 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 79.85 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKP----TTGTYELAGQNISNMSETE 76
Cdd:PRK15093 3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDnwrvTADRMRFDDIDLLRLSPRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 77 LAHVRNKEIGFVFQNfmllPR--LTALQNVELPLIYA--GVDKKE--------RRERSLAALTKVGLADRA---THLPNE 141
Cdd:PRK15093 83 RRKLVGHNVSMIFQE----PQscLDPSERVGRQLMQNipGWTYKGrwwqrfgwRKRRAIELLHRVGIKDHKdamRSFPYE 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQ-GSTIIMITHD 200
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNnNTTILLISHD 218
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-199 |
1.40e-17 |
|
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: 76.81 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNisnmsetelahvrnkeigfvfqNFMLLPRLt 99
Cdd:cd03223 16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------------------DLLFLPQR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 alqnvelPLIYAGVdkkeRRERSLAALTKVgladrathlpneLSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQ 179
Cdd:cd03223 73 -------PYLPLGT----LREQLIYPWDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129
|
170 180
....*....|....*....|
gi 446531755 180 IMDLfyeLNKQGSTIIMITH 199
Cdd:cd03223 130 LYQL---LKELGITVISVGH 146
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
20-199 |
1.46e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 80.69 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNiigcldkpttgtyELAGQ-NISNMSETELAHVRN------KEIGFVFQNF 92
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLN-------------ALAGRiQGNNFTGTILANNRKptkqilKRTGFVTQDD 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 93 MLLPRLTALQN---VELPLIYAGVDKKERRERSLAALTKVGLAD-RATHLPNE----LSGGQKQRVAVARAIVNNPKFIL 164
Cdd:PLN03211 150 ILYPHLTVRETlvfCSLLRLPKSLTKQEKILVAESVISELGLTKcENTIIGNSfirgISGGERKRVSIAHEMLINPSLLI 229
|
170 180 190
....*....|....*....|....*....|....*
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:PLN03211 230 LDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
20-216 |
1.91e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 77.69 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCL-DKPTTGTYELAGQNISNmsetelahvrnkeigfvfqnfmllpr 97
Cdd:COG2401 45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGALkGTPVAGCVDVPDNQFGR-------------------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 ltalqnvELPLI---YAGVDKKErrerSLAALTKVGLADRATHL--PNELSGGQKQRVAVARAIVNNPKFILADEPTGAL 172
Cdd:COG2401 99 -------EASLIdaiGRKGDFKD----AVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHL 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446531755 173 DTKTSTQIMDLFYELNKQ-GSTIIMITHDREIGEAAARQIVIRDG 216
Cdd:COG2401 168 DRQTAKRVARNLQKLARRaGITLVVATHHYDVIDDLQPDLLIFVG 212
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
2-224 |
4.44e-17 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 79.29 E-value: 4.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQnGAESvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsETELAHVR 81
Cdd:PRK11176 342 IEFRNVTFTYP-GKEV-PALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR---DYTLASLR 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NkEIGFVFQNFMLLPRLTAlQNVElpliYAGVDKKERRERSLAAltKVGLA-DRATHLPN-----------ELSGGQKQR 149
Cdd:PRK11176 417 N-QVALVSQNVHLFNDTIA-NNIA----YARTEQYSREQIEEAA--RMAYAmDFINKMDNgldtvigengvLLSGGQRQR 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 150 VAVARAIVNN-PKFILaDEPTGALDTKTSTQIMDLFYELNKQgSTIIMITHDREIGEAAARQIVIRDGNVVQdwRG 224
Cdd:PRK11176 489 IAIARALLRDsPILIL-DEATSALDTESERAIQAALDELQKN-RTSLVIAHRLSTIEKADEILVVEDGEIVE--RG 560
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
16-221 |
5.61e-17 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 76.92 E-value: 5.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 16 ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNII----GCldKPTTGTYELAGQNISNMSETELAHvrnKEIGFVFQN 91
Cdd:TIGR01978 11 EDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIaghpSY--EVTSGTILFKGQDLLELEPDERAR---AGLFLAFQY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 92 FMLLPRLTAL------------QNVELPLIYAGVDKKERRERSLAALTKvGLADRAThlpNE-LSGGQKQRVAVARAIVN 158
Cdd:TIGR01978 86 PEEIPGVSNLeflrsalnarrsARGEEPLDLLDFEKLLKEKLALLDMDE-EFLNRSV---NEgFSGGEKKRNEILQMALL 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 159 NPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIV--IRDGNVVQD 221
Cdd:TIGR01978 162 EPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHYQRLLNYIKPDYVhvLLDGRIVKS 226
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
27-200 |
6.60e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.51 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 27 TLNQGEFTSIMGPSGSGKSTLMN-IIGCLdkPTTGTYELAGQNISNMSETELAHVR-----NKEIGF---VFQNFML-LP 96
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKSTLLArMAGLL--PGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFampVFQYLTLhQP 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 97 RLTALQNVELPLIYagvdkkerrersLAALtkVGLADRATHLPNELSGGQKQRVAVARAI-----VNNP--KFILADEPT 169
Cdd:PRK03695 96 DKTRTEAVASALNE------------VAEA--LGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPM 161
|
170 180 190
....*....|....*....|....*....|.
gi 446531755 170 GALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:PRK03695 162 NSLDVAQQAALDRLLSELCQQGIAVVMSSHD 192
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
21-219 |
2.35e-16 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 76.98 E-value: 2.35e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETE-----LAHV---RnKEIGfvfqnf 92
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagIAYVpedR-KGEG------ 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 93 mLLPRLTALQNVELPLI--YAG---VDKKERRERSLAALTKVGL-ADRATHLPNELSGGQKQRVAVARAIVNNPKFILAD 166
Cdd:COG1129 341 -LVLDLSIRENITLASLdrLSRgglLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGNQQKVVLAKWLATDPKVLILD 419
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 167 EPTGALDTKTSTQIMDLFYELNKQGSTIIMIThdREIGEAAA---RQIVIRDGNVV 219
Cdd:COG1129 420 EPTRGIDVGAKAEIYRLIRELAAEGKAVIVIS--SELPELLGlsdRILVMREGRIV 473
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-220 |
1.27e-15 |
|
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: 72.53 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 16 ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSeteLAHVRNKeIGFVFQNfmll 95
Cdd:cd03244 15 NLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSR-ISIIPQD---- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 prltalqnvelPLIYAG-----VDKKERR--ERSLAALTKVGLADRATHLP-----------NELSGGQKQRVAVARAIV 157
Cdd:cd03244 87 -----------PVLFSGtirsnLDPFGEYsdEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 158 NNPKFILADEPTGALDTKTSTQIMDLFYELNKqGSTIIMITH--------DREigeaaarqIVIRDGNVVQ 220
Cdd:cd03244 156 RKSKILVLDEATASVDPETDALIQKTIREAFK-DCTVLTIAHrldtiidsDRI--------LVLDKGRVVE 217
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-199 |
1.29e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 75.15 E-value: 1.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 15 AESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNiigCLDKPTTGTYELAGQNISNMSETELAHVRNkeIGFVFQNFML 94
Cdd:TIGR00956 773 KEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLN---VLAERVTTGVITGGDRLVNGRPLDSSFQRS--IGYVQQQDLH 847
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 LPRLTalqnVELPLIYAG-------VDKKERR---ERSLAALTKVGLADRATHLPNE-LSGGQKQRVAVARAIVNNPKFI 163
Cdd:TIGR00956 848 LPTST----VRESLRFSAylrqpksVSKSEKMeyvEEVIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKLL 923
|
170 180 190
....*....|....*....|....*....|....*..
gi 446531755 164 L-ADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:TIGR00956 924 LfLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIH 960
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
2-220 |
1.57e-15 |
|
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: 72.06 E-value: 1.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqnGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMsetELAHVR 81
Cdd:cd03369 7 IEVENLSVRY--APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKeIGFVFQNFMLLPRlTALQNVElplIYAGVDKKERRErslaaltkvglADRATHLPNELSGGQKQRVAVARAIVNNPK 161
Cdd:cd03369 82 SS-LTIIPQDPTLFSG-TIRSNLD---PFDEYSDEEIYG-----------ALRVSEGGLNLSQGQRQLLCLARALLKRPR 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNkQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:cd03369 146 VLVLDEATASIDYATDALIQKTIREEF-TNSTILTIAHRLRTIIDYDKILVMDAGEVKE 203
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-201 |
3.60e-15 |
|
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: 73.82 E-value: 3.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGAEsvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTyELAGQNISnmsetelahvrnk 83
Cdd:TIGR03719 7 MNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE-ARPQPGIK------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 eIGFVFQNFMLLPRLTALQNVELPL------------IYAG-----------VDKKERRERSLAAL------TKVGLADR 134
Cdd:TIGR03719 70 -VGYLPQEPQLDPTKTVRENVEEGVaeikdaldrfneISAKyaepdadfdklAAEQAELQEIIDAAdawdldSQLEIAMD 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 135 ATHLP------NELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTstqIMDLFYELNKQGSTIIMITHDR 201
Cdd:TIGR03719 149 ALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES---VAWLERHLQEYPGTVVAVTHDR 218
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
20-199 |
4.62e-15 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 73.21 E-value: 4.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELahvrNKEIGFVFQNFMLLPRlT 99
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVELpliyaGVDKKErrERSLAALTKVGLADRATHLP-----------NELSGGQKQRVAVARAIVNNPKFILADEP 168
Cdd:PRK10790 431 FLANVTL-----GRDISE--EQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEA 503
|
170 180 190
....*....|....*....|....*....|.
gi 446531755 169 TGALDTKTSTQIMDLFYELNKQgSTIIMITH 199
Cdd:PRK10790 504 TANIDSGTEQAIQQALAAVREH-TTLVVIAH 533
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
21-219 |
1.05e-14 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 72.37 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETE-----LAHV---RNKEiGFVfqnf 92
Cdd:COG3845 274 LKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErrrlgVAYIpedRLGR-GLV---- 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 93 mllPRLTALQNVELPLIYAG-------VDKKERRERSLAALTKVGLADRATHLP-NELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:COG3845 349 ---PDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDVRTPGPDTPaRSLSGGNQQKVILARELSRDPKLLI 425
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:COG3845 426 AAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDlDEILALSDRIAVMYEGRIV 481
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
24-220 |
2.25e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 71.35 E-value: 2.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETE-----LAHV--RNKEIGFvFQNFMLLP 96
Cdd:PRK09700 282 ISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgMAYIteSRRDNGF-FPNFSIAQ 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 97 RLTALQNVELPLiYAGV-----DKKERR----ERSLAALTKVGLADRAThlpnELSGGQKQRVAVARAIVNNPKFILADE 167
Cdd:PRK09700 361 NMAISRSLKDGG-YKGAmglfhEVDEQRtaenQRELLALKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446531755 168 PTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVVQ 220
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKVILMVSSElPEIITVCDRIAVFCEGRLTQ 489
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
16-199 |
7.13e-14 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.06 E-value: 7.13e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 16 ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGtyELAGQNISNMSETELAHVRNKeIGFVFQNFML- 94
Cdd:PTZ00265 396 KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEG--DIIINDSHNLKDINLKWWRSK-IGVVSQDPLLf 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 --------------LPRLTALQNVELPLIYAGVDKKERRERSLAALT--------------------------------- 127
Cdd:PTZ00265 473 snsiknnikyslysLKDLEALSNYYNEDGNDSQENKNKRNSCRAKCAgdlndmsnttdsneliemrknyqtikdsevvdv 552
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 128 --KVGLADRATHLPNE-----------LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTI 194
Cdd:PTZ00265 553 skKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRI 632
|
....*.
gi 446531755 195 -IMITH 199
Cdd:PTZ00265 633 tIIIAH 638
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
21-200 |
1.65e-13 |
|
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: 67.39 E-value: 1.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTlNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAG---QNISNMSETEL----AHVRNKEIGFVF--QN 91
Cdd:cd03236 17 LHRLPVP-REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdEILDEFRGSELqnyfTKLLEGDVKVIVkpQY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 92 FMLLPRlTALQNVELPLiyAGVDKKERRERSLAALTKVGLADRAThlpNELSGGQKQRVAVARAIVNNPKFILADEPTGA 171
Cdd:cd03236 96 VDLIPK-AVKGKVGELL--KKKDERGKLDELVDQLELRHVLDRNI---DQLSGGELQRVAIAAALARDADFYFFDEPSSY 169
|
170 180
....*....|....*....|....*....
gi 446531755 172 LDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:cd03236 170 LDIKQRLNAARLIRELAEDDNYVLVVEHD 198
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-173 |
1.70e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 1.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelahvRNKEIGFVFQNFMLLPRLT 99
Cdd:PRK13543 26 VFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLS 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446531755 100 ALQNVELpliYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALD 173
Cdd:PRK13543 99 TLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
17-199 |
3.88e-13 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 66.59 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 17 SVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGclDKP----TTGTYELAGQNISNMSETELAHvrnKEIGFVFQNF 92
Cdd:CHL00131 19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIA--GHPaykiLEGDILFKGESILDLEPEERAH---LGIFLAFQYP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 93 MLLPRLTalqNVE-LPLIYAGVDKKERR---------ERSLAALTKVGLADRATHLP-NE-LSGGQKQRVAVARAIVNNP 160
Cdd:CHL00131 94 IEIPGVS---NADfLRLAYNSKRKFQGLpeldpleflEIINEKLKLVGMDPSFLSRNvNEgFSGGEKKRNEILQMALLDS 170
|
170 180 190
....*....|....*....|....*....|....*....
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH 209
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
4-180 |
5.21e-13 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 67.44 E-value: 5.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGAES--VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGC------LDKPTTGTYE-LAGQNISNMSE 74
Cdd:TIGR00956 58 LTRGFRKLKKFRDTktFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgfhIGVEGVITYDgITPEEIKKHYR 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 75 TELAHVRNKEIGF----VFQNFMLLPRLTALQNVelpliYAGVDKKERRERSLA-ALTKVGLAD-RATHLPNEL----SG 144
Cdd:TIGR00956 138 GDVVYNAETDVHFphltVGETLDFAARCKTPQNR-----PDGVSREEYAKHIADvYMATYGLSHtRNTKVGNDFvrgvSG 212
|
170 180 190
....*....|....*....|....*....|....*.
gi 446531755 145 GQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQI 180
Cdd:TIGR00956 213 GERKRVSIAEASLGGAKIQCWDNATRGLDSATALEF 248
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
26-213 |
6.14e-13 |
|
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: 67.35 E-value: 6.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 26 VTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNI-SNMSEtelahvrnkeigfVFQNFMLLPRLTALQNV 104
Cdd:TIGR01257 1960 VGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISD-------------VHQNMGYCPQFDAIDDL 2026
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 105 ----ELPLIYA---GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTS 177
Cdd:TIGR01257 2027 ltgrEHLYLYArlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQAR 2106
|
170 180 190
....*....|....*....|....*....|....*.
gi 446531755 178 TQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVI 213
Cdd:TIGR01257 2107 RMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAI 2142
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
21-211 |
1.01e-12 |
|
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: 63.88 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNiigcldkpttgtyelagqnisnmsETELAHVRNKEIGFvfqnfmlLPRlta 100
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------------------EGLYASGKARLISF-------LPK--- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 101 lqNVELPLIYAGvdkkerrerSLAALTKVGLadraTHLP-----NELSGGQKQRVAVARAIVNNPK---FILaDEPTGAL 172
Cdd:cd03238 57 --FSRNKLIFID---------QLQFLIDVGL----GYLTlgqklSTLSGGELQRVKLASELFSEPPgtlFIL-DEPSTGL 120
|
170 180 190
....*....|....*....|....*....|....*....
gi 446531755 173 DTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQI 211
Cdd:cd03238 121 HQQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWII 159
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
19-199 |
2.11e-12 |
|
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: 63.42 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGclDKPTTGTYE----LAGQnisnmsetELAHVRNKEIGFVFQNFML 94
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVITgeilINGR--------PLDKNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 LPRLTalqnVELPLIYAgvdkkerrerslAALtkvgladrathlpNELSGGQKQRVAVARAIVNNPKFILADEPTGALDT 174
Cdd:cd03232 91 SPNLT----VREALRFS------------ALL-------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180
....*....|....*....|....*
gi 446531755 175 KTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIH 166
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-221 |
2.26e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.46 E-value: 2.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLDKP-------TTGTYELAGQNISNMSETELAHVR-----NKEIG 86
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGgaprgarVTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 87 FVF--QNFMLLPRLTALQNvelpliyAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVN------ 158
Cdd:PRK13547 96 FAFsaREIVLLGRYPHARR-------AGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphd 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 159 ---NPKFILADEPTGALDTKTSTQIMDLFYELNKQGST-IIMITHDREIGEAAARQIV-IRDGNVVQD 221
Cdd:PRK13547 169 aaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAmLADGAIVAH 236
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
20-201 |
2.48e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 63.43 E-value: 2.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsnmsETELAhVRNKEIGFVFQNFMLLPRLT 99
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLC-TYQKQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 ALQNVELPLIYA----GVDKkerrersLAALTKVG-LADRATHLpneLSGGQKQRVAVARAIVNNPKFILADEPTGALDT 174
Cdd:PRK13540 91 LRENCLYDIHFSpgavGITE-------LCRLFSLEhLIDYPCGL---LSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*..
gi 446531755 175 KTSTQIMDLFYELNKQGSTIIMITHDR 201
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSHQD 187
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-224 |
2.49e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 65.36 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 25 DVTLNQGEFTSIMGPSGSGKSTLMNIIG---CLD--------------------KPTTGT-YELAGQNISNMSET----- 75
Cdd:PRK11147 23 ELHIEDNERVCLVGRNGAGKSTLMKILNgevLLDdgriiyeqdlivarlqqdppRNVEGTvYDFVAEGIEEQAEYlkryh 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 76 ELAHVrnkeigfVFQNFM--LLPRLTALQNVelpLIYAGVDKKERRERSLaaLTKVGLaDRATHLpNELSGGQKQRVAVA 153
Cdd:PRK11147 103 DISHL-------VETDPSekNLNELAKLQEQ---LDHHNLWQLENRINEV--LAQLGL-DPDAAL-SSLSGGWLRKAALG 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMDLFyeLNKQGStIIMITHDREIGEAAARQIVIRDGNVVQDWRG 224
Cdd:PRK11147 169 RALVSNPDVLLLDEPTNHLDIETIEWLEGFL--KTFQGS-IIFISHDRSFIRNMATRIVDLDRGKLVSYPG 236
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
30-199 |
4.27e-12 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 64.76 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 30 QGEFTSIMGPSGSGKSTLMNII-GCLDkPTTGTYELAGQNI--SNMSetelahVRnKEIGFVFQNFMLLPRLTALQNVEL 106
Cdd:NF033858 291 RGEIFGFLGSNGCGKSTTMKMLtGLLP-ASEGEAWLFGQPVdaGDIA------TR-RRVGYMSQAFSLYGELTVRQNLEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 107 pliYA---GVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDtktsTQIMDL 183
Cdd:NF033858 363 ---HArlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD----PVARDM 435
|
170 180
....*....|....*....|.
gi 446531755 184 FYEL-----NKQGSTIIMITH 199
Cdd:NF033858 436 FWRLlielsREDGVTIFISTH 456
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
21-200 |
1.11e-11 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 62.53 E-value: 1.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYElagqnisnmsetelahvRNKEIGFVFQNFMLLPRLTA 100
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAGLSGQLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 101 LQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQI 180
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|
gi 446531755 181 MDLFYELNKQGSTIIMITHD 200
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHN 202
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
21-216 |
1.28e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNII-GCLDKpTTGTYELAGQNISNMSETE-----LAHVRN--KEIGFVF--- 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPQDglangIVYISEdrKRDGLVLgms 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 90 --QNFmllpRLTALQNvelpLIYAGVDKKERRERsLAALTKVGLADRAThlPN------ELSGGQKQRVAVARAIVNNPK 161
Cdd:PRK10762 347 vkENM----SLTALRY----FSRAGGSLKHADEQ-QAVSDFIRLFNIKT--PSmeqaigLLSGGNQQKVAIARGLMTRPK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDR-EIGEAAARQIVIRDG 216
Cdd:PRK10762 416 VLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMpEVLGMSDRILVMHEG 471
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-203 |
1.64e-11 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 63.33 E-value: 1.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 18 VQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIigcLDKPTTGTYELAGQNISNMSETELAHVRNKeiGFVFQNFMLLPR 97
Cdd:PLN03140 893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDV---LAGRKTGGYIEGDIRISGFPKKQETFARIS--GYCEQNDIHSPQ 967
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LTalqnVELPLIYAG-------VDKKERR---ERSLAALTKVGLADRATHLP--NELSGGQKQRVAVARAIVNNPKFILA 165
Cdd:PLN03140 968 VT----VRESLIYSAflrlpkeVSKEEKMmfvDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFM 1043
|
170 180 190
....*....|....*....|....*....|....*...
gi 446531755 166 DEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREI 203
Cdd:PLN03140 1044 DEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHQPSI 1081
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-217 |
2.28e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 62.68 E-value: 2.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVQilhGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsnmSETELAHVR 81
Cdd:PRK10522 323 LELRNVTFAYQDNGFSVG---PINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPV---TAEQPEDYR 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRLTALQNVELPliyagvdkKERRERSLAAL---TKVGLAD-RATHLpnELSGGQKQRVAVARAIV 157
Cdd:PRK10522 397 -KLFSAVFTDFHLFDQLLGPEGKPAN--------PALVEKWLERLkmaHKLELEDgRISNL--KLSKGQKKRLALLLALA 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 158 NNPKFILADEPTGALDtktsTQIMDLFY-----ELNKQGSTIIMITHDREIGEAAARQIVIRDGN 217
Cdd:PRK10522 466 EERDILLLDEWAADQD----PHFRREFYqvllpLLQEMGKTIFAISHDDHYFIHADRLLEMRNGQ 526
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-220 |
3.93e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 3.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 9 KSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMsetELAHVRNK----- 83
Cdd:PRK10789 319 RQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRlavvs 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNfmllprlTALQNVELPLIYAGVDKKERRERsLAAL------------TKVGlaDRATHLpnelSGGQKQRVA 151
Cdd:PRK10789 396 QTPFLFSD-------TVANNIALGRPDATQQEIEHVAR-LASVhddilrlpqgydTEVG--ERGVML----SGGQKQRIS 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 152 VARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELnKQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:PRK10789 462 IARALLLNAEILILDDALSAVDGRTEHQILHNLRQW-GEGRTVIISAHRLSALTEASEILVMQHGHIAQ 529
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
7-216 |
4.20e-11 |
|
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 60.42 E-value: 4.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 7 ITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLM-NIIGCLDKpTTGTYELAGQNISNMSETELAHVRNKEI 85
Cdd:cd03290 3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 86 GFVFQNFMLLPrltalQNVELPLIYAGVDKKERRERSLAALT------------KVGLADRATHLpnelSGGQKQRVAVA 153
Cdd:cd03290 82 AYAAQKPWLLN-----ATVEENITFGSPFNKQRYKAVTDACSlqpdidllpfgdQTEIGERGINL----SGGQRQRICVA 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 154 RAIVNNPKFILADEPTGALDTKTSTQIMD--LFYELNKQGSTIIMITHDREIGEAAARQIVIRDG 216
Cdd:cd03290 153 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-201 |
4.65e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGAEsvqilhgIDVtlnqgeftsiMGPSGSGKSTLMNIIGCLDKPTTGTYELAgQNISnmsetelahvrnk 83
Cdd:PRK11819 23 LKDISLSFFPGAK-------IGV----------LGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGIK------------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 eIGFVFQNFMLLPRLTALQNVELPL------------IYAG-----------VDKKERRERSLAAL------TKVGLADR 134
Cdd:PRK11819 72 -VGYLPQEPQLDPEKTVRENVEEGVaevkaaldrfneIYAAyaepdadfdalAAEQGELQEIIDAAdawdldSQLEIAMD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 135 ATHLP------NELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKtSTQIMDLFyeLNKQGSTIIMITHDR 201
Cdd:PRK11819 151 ALRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAE-SVAWLEQF--LHDYPGTVVAVTHDR 220
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
2-221 |
6.63e-11 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 60.97 E-value: 6.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVQ-ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIsnmSETELAHV 80
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPV---TADNREAY 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKeigF--VFQNFMLLPRLTALQNVELPliyagvdkkERRERSLAAL---TKVGLADRA--ThlpNELSGGQKQRVAVA 153
Cdd:COG4615 405 RQL---FsaVFSDFHLFDRLLGLDGEADP---------ARARELLERLeldHKVSVEDGRfsT---TDLSQGQRKRLALL 469
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 154 RAIVNNPKFILADE------PtgaldtktstQIMDLFY-----ELNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:COG4615 470 VALLEDRPILVFDEwaadqdP----------EFRRVFYtellpELKARGKTVIAISHDDRYFDLADRVLKMDYGKLVEL 538
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
21-218 |
1.02e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLDKpTTGTYELAG-----------QNISNMSETELAHVRN-KEIGF 87
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGsvayvpqqawiQNDSLRENILFGKALNeKYYQQ 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 88 VFQNFMLLPRLTALqnvelpliyAGVDKKERRERSLaaltkvgladrathlpnELSGGQKQRVAVARAIVNNPKFILADE 167
Cdd:TIGR00957 733 VLEACALLPDLEIL---------PSGDRTEIGEKGV-----------------NLSGGQKQRVSLARAVYSNADIYLFDD 786
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446531755 168 PTGALDTKTSTQIMD--LFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNV 218
Cdd:TIGR00957 787 PLSAVDAHVGKHIFEhvIGPEGVLKNKTRILVTHGISYLPQVDVIIVMSGGKI 839
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
24-219 |
1.03e-10 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 60.70 E-value: 1.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISnmsetelahVRNKeIGFVFQNFMLLPR------ 97
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID---------IRSP-RDAIRAGIMLCPEdrkaeg 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LTALQNVELPL--------IYAGVDKKERRERSLA----ALTKVGLADRATHLPNeLSGGQKQRVAVARAIVNNPKFILA 165
Cdd:PRK11288 342 IIPVHSVADNInisarrhhLRAGCLINNRWEAENAdrfiRSLNIKTPSREQLIMN-LSGGNQQKAILGRWLSEDMKVILL 420
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446531755 166 DEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVV 219
Cdd:PRK11288 421 DEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDlPEVLGVADRIVVMREGRIA 475
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
21-199 |
1.41e-10 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 60.29 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGqnisnmSETELAhvrnkeIGFVFQNfmllpRLTA 100
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIA------ISSGLNG-----QLTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 101 LQNVELPLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQI 180
Cdd:PRK13545 103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182
|
170
....*....|....*....
gi 446531755 181 MDLFYELNKQGSTIIMITH 199
Cdd:PRK13545 183 LDKMNEFKEQGKTIFFISH 201
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
113-221 |
1.71e-10 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 59.75 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 113 VDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGS 192
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA 195
|
90 100 110
....*....|....*....|....*....|
gi 446531755 193 TIIMITHDREIGEAAARQIVIRD-GNVVQD 221
Cdd:NF000106 196 TVLLTTQYMEEAEQLAHELTVIDrGRVIAD 225
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
20-173 |
2.11e-10 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 59.64 E-value: 2.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIgcldkptTGTYElagQNISNmSETELAHVR---------NKEIGFVFQ 90
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI-------TGDHP---QGYSN-DLTLFGRRRgsgetiwdiKKHIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 91 NFMLLPRL-TALQNVELP------LIYAGVDKkerRERSLAA--LTKVGLADRATHLP-NELSGGQKQRVAVARAIVNNP 160
Cdd:PRK10938 344 SLHLDYRVsTSVRNVILSgffdsiGIYQAVSD---RQQKLAQqwLDILGIDKRTADAPfHSLSWGQQRLALIVRALVKHP 420
|
170
....*....|...
gi 446531755 161 KFILADEPTGALD 173
Cdd:PRK10938 421 TLLILDEPLQGLD 433
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
142-220 |
2.98e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 59.66 E-value: 2.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYEL-NKQGSTIIMITHdREIGEAAARQIVI-----RD 215
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIkDKADKTIITIAH-RIASIKRSDKIVVfnnpdRT 1437
|
....*
gi 446531755 216 GNVVQ 220
Cdd:PTZ00265 1438 GSFVQ 1442
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-219 |
4.90e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.02 E-value: 4.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 16 ESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNiigcldkpttgtyelagqniSNMSETELAHVR---NKEIGFVFQNF 92
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKSTLLQ--------------------SLLSQFEISEGRvwaERSIAYVPQQA 730
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 93 MLLpRLTALQNVelpLIYagvdkKERRERSLAALTKVG-----LADRATHLPNE-------LSGGQKQRVAVARAIVNNP 160
Cdd:PTZ00243 731 WIM-NATVRGNI---LFF-----DEEDAARLADAVRVSqleadLAQLGGGLETEigekgvnLSGGQKARVSLARAVYANR 801
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVV 219
Cdd:PTZ00243 802 DVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVE 860
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
21-207 |
7.44e-10 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 56.88 E-value: 7.44e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLM---------------------NIIGCLDKPTTgtyelagQNISNMSETeLAh 79
Cdd:cd03270 11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDV-------DSIEGLSPA-IA- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRNKEIGfvfQNfmllPRLTALQNVE----LPLIYAGVDKKERrersLAALTKVGLA----DRAThlpNELSGGQKQRVA 151
Cdd:cd03270 82 IDQKTTS---RN----PRSTVGTVTEiydyLRLLFARVGIRER----LGFLVDVGLGyltlSRSA---PTLSGGEAQRIR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446531755 152 VARAIVNNPK---FILaDEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAA 207
Cdd:cd03270 148 LATQIGSGLTgvlYVL-DEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAA 205
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-221 |
1.51e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLDKPTTGTYELAGQ--NISNMSETELAHVR-NKEIGFVFQN--FML 94
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGSvaYVPQVSWIFNATVReNILFGSDFESerYWR 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 LPRLTALQNvELPLiYAGVDKKERRERSLaaltkvgladrathlpnELSGGQKQRVAVARAIVNNPKFILADEPTGALDT 174
Cdd:PLN03232 713 AIDVTALQH-DLDL-LPGRDLTEIGERGV-----------------NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446531755 175 KTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQD 221
Cdd:PLN03232 774 HVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEGMIKEE 820
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-216 |
2.09e-09 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 56.66 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETElahVRNK 83
Cdd:PRK10982 1 MSNISKSF----PGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE---ALEN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 84 EIGFVFQNFMLLPRLTALQNVEL---PLIYAGVDKKERRERSLAALTKVGLADRATHLPNELSGGQKQRVAVARAIVNNP 160
Cdd:PRK10982 74 GISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 161 KFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDG 216
Cdd:PRK10982 154 KIVIMDEPTSSLTEKEVNHLFTIIRKLKERGCGIVYISHKmEEIFQLCDEITILRDG 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-201 |
2.48e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.44 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 1 MINLKGITKSFqnGAESvqILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGtyelagqNISNMSETELAHV 80
Cdd:PRK15064 1 MLSTANITMQF--GAKP--LFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAG-------NVSLDPNERLGKL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 81 RNKEigFVFQNFMLLP-----------------RLTALQNV---------ELPLIYAGVDKKERRERSLAALTKVGLA-D 133
Cdd:PRK15064 70 RQDQ--FAFEEFTVLDtvimghtelwevkqerdRIYALPEMseedgmkvaDLEVKFAEMDGYTAEARAGELLLGVGIPeE 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 134 RATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTstqIMDLFYELNKQGSTIIMITHDR 201
Cdd:PRK15064 148 QHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT---IRWLEDVLNERNSTMIIISHDR 212
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
30-200 |
2.52e-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: 56.33 E-value: 2.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 30 QGEFTSIMGPSGSGKSTLMNIigcldkpttgtyeLAGQNISNMSETE--------LAHVRNKEIGFVFQnfmllpRL--- 98
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKI-------------LSGELKPNLGDYDeepswdevLKRFRGTELQDYFK------KLang 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 ---TAL--QNVEL-PLIYAGV-----DKKERRERSLAALTKVGLA---DRAThlpNELSGGQKQRVAVARAIVNNPKFIL 164
Cdd:COG1245 159 eikVAHkpQYVDLiPKVFKGTvrellEKVDERGKLDELAEKLGLEnilDRDI---SELSGGELQRVAIAAALLRDADFYF 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 446531755 165 ADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:COG1245 236 FDEPSSYLDIYQRLNVARLIRELAEEGKYVLVVEHD 271
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
7-180 |
5.77e-09 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 54.19 E-value: 5.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 7 ITKSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGcldkPTTGTYELAGQNIS--NMSETELAHVRNKE 84
Cdd:cd03233 9 ISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA----NRTEGNVSVEGDIHynGIPYKEFAEKYPGE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 85 IGFVFQNFMLLPRLTALQNVELPLIYAGvdkkerrerslaaltkvgladrathlpNE----LSGGQKQRVAVARAIVNNP 160
Cdd:cd03233 85 IIYVSEEDVHFPTLTVRETLDFALRCKG---------------------------NEfvrgISGGERKRVSIAEALVSRA 137
|
170 180
....*....|....*....|
gi 446531755 161 KFILADEPTGALDTKTSTQI 180
Cdd:cd03233 138 SVLCWDNSTRGLDSSTALEI 157
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
20-182 |
6.30e-09 |
|
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: 54.86 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTL-MNIIGCLDkPTTGTYELAGQnisnmsetelahvrnkeIGFVFQNFMLLPRl 98
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLlMLILGELE-PSEGKIKHSGR-----------------ISFSSQFSWIMPG- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 TALQNvelplIYAGVDKKERRERSLAALTKvgLADRATHLPNE-----------LSGGQKQRVAVARAIVNNPKFILADE 167
Cdd:cd03291 113 TIKEN-----IIFGVSYDEYRYKSVVKACQ--LEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185
|
170
....*....|....*
gi 446531755 168 PTGALDTKTSTQIMD 182
Cdd:cd03291 186 PFGYLDVFTEKEIFE 200
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
24-216 |
8.09e-09 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 55.06 E-value: 8.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSetelahVRNK-EIGFVFqnfmlLP--RLTA 100
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS------TAQRlARGLVY-----LPedRQSS 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 101 LQNVELPLIYAGVD------------KKERR--ERSLAAL-TKVGLADRAThlpNELSGGQKQRVAVARAIVNNPKFILA 165
Cdd:PRK15439 351 GLYLDAPLAWNVCAlthnrrgfwikpARENAvlERYRRALnIKFNHAEQAA---RTLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446531755 166 DEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDG 216
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDlEEIEQMADRVLVMHQG 479
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
23-214 |
9.69e-09 |
|
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: 52.75 E-value: 9.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 23 GIDVTLNQGEFTSIMGPSGSGKSTLMNIIGcldkpttgtyelagqnisnmsetelahvrnkeIGFVFQNFMLLPRLTALQ 102
Cdd:cd03227 13 PNDVTFGEGSLTIITGPNGSGKSTILDAIG--------------------------------LALGGAQSATRRRSGVKA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 103 NVELPLIYAGvdkkerrerslAALTKVGLadrathlpnelSGGQKQRVAVARAI----VNNPKFILADEPTGALDTKTST 178
Cdd:cd03227 61 GCIVAAVSAE-----------LIFTRLQL-----------SGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQ 118
|
170 180 190
....*....|....*....|....*....|....*.
gi 446531755 179 QIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIR 214
Cdd:cd03227 119 ALAEAILEHLVKGAQVIVITHLPELAELADKLIHIK 154
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
17-169 |
1.50e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 54.36 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 17 SVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNmsetelAHVRNK---EIGFVFQ--- 90
Cdd:NF033858 13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD------ARHRRAvcpRIAYMPQglg 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 91 -NfmLLPRLTALQNVELpliYA---GVDKKERRERsLAALTK-VGLADRATHLPNELSGGQKQRVAVARAIVNNPKFILA 165
Cdd:NF033858 87 kN--LYPTLSVFENLDF---FGrlfGQDAAERRRR-IDELLRaTGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLIL 160
|
....
gi 446531755 166 DEPT 169
Cdd:NF033858 161 DEPT 164
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
19-197 |
2.24e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 19 QILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEigfvFQ---NFMLL 95
Cdd:PRK10938 17 KTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDE----WQrnnTDMLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 P------RLTAlqnvelPLIYAGVDKKERRERsLAALTKVG--LADRATHlpneLSGGQKQRVAVARAIVNNPKFILADE 167
Cdd:PRK10938 93 PgeddtgRTTA------EIIQDEVKDPARCEQ-LAQQFGITalLDRRFKY----LSTGETRKTLLCQALMSEPDLLILDE 161
|
170 180 190
....*....|....*....|....*....|
gi 446531755 168 PTGALDTKTSTQIMDLFYELNKQGSTIIMI 197
Cdd:PRK10938 162 PFDGLDVASRQQLAELLASLHQSGITLVLV 191
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
20-182 |
2.68e-08 |
|
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: 53.76 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTL-MNIIGCLDkPTTGTYELAGQnisnmsetelahvrnkeIGFVFQNFMLLPRl 98
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLlMMIMGELE-PSEGKIKHSGR-----------------ISFSPQTSWIMPG- 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 TALQNvelplIYAGVDKKERRERSLaaLTKVGLADRATHLPNE-----------LSGGQKQRVAVARAIVNNPKFILADE 167
Cdd:TIGR01271 502 TIKDN-----IIFGLSYDEYRYTSV--IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDS 574
|
170
....*....|....*
gi 446531755 168 PTGALDTKTSTQIMD 182
Cdd:TIGR01271 575 PFTHLDVVTEKEIFE 589
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
9-203 |
2.82e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 52.49 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 9 KSFQNGAESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLD--KPTTGTYELAGQNISNMSETE-------LAH 79
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDragegifMAF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRNKEIGFVFQNFMLLPRLTALQNvelpliYAGVDKKERRERSLAALTKVGL----ADRATHLPNE-LSGGQKQRVAVAR 154
Cdd:PRK09580 85 QYPVEIPGVSNQFFLQTALNAVRS------YRGQEPLDRFDFQDLMEEKIALlkmpEDLLTRSVNVgFSGGEKKRNDILQ 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446531755 155 AIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREI 203
Cdd:PRK09580 159 MAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRI 207
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
33-217 |
3.11e-08 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 51.84 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 33 FTSIMGPSGSGKSTlmnIIGCLDKPTTGtyELAGQNISNMSETELAHVrNKEIGFVFQNFmllprltalqnvelpliYAG 112
Cdd:cd03240 24 LTLIVGQNGAGKTT---IIEALKYALTG--ELPPNSKGGAHDPKLIRE-GEVRAQVKLAF-----------------ENA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 113 VDKKERRERSLAALTKV------GLADRATHLPNELSGGQKQ------RVAVARAIVNNPKFILADEPTGALDT-KTSTQ 179
Cdd:cd03240 81 NGKKYTITRSLAILENVifchqgESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEES 160
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446531755 180 IMDLFYELNKQG-STIIMITHDREIGEAAARQI-VIRDGN 217
Cdd:cd03240 161 LAEIIEERKSQKnFQLIVITHDEELVDAADHIYrVEKDGR 200
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
35-218 |
5.31e-08 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.55 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 35 SIMGPSGSGKSTLMNIIGCLDKPTTGT-YELAGQNISNMSEtelAHVrnkeigfvfqnfmllprlTALQNVELPLIY--- 110
Cdd:PLN03073 539 AMVGPNGIGKSTILKLISGELQPSSGTvFRSAKVRMAVFSQ---HHV------------------DGLDLSSNPLLYmmr 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 111 --AGVDKKERRerslAALTKVGLADRATHLP-NELSGGQKQRVAVARAIVNNPKFILADEPTGALD---TKTSTQIMDLF 184
Cdd:PLN03073 598 cfPGVPEQKLR----AHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDldaVEALIQGLVLF 673
|
170 180 190
....*....|....*....|....*....|....*
gi 446531755 185 yelnkQGStIIMITHDREIGEAAARQI-VIRDGNV 218
Cdd:PLN03073 674 -----QGG-VLMVSHDEHLISGSVDELwVVSEGKV 702
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-201 |
5.79e-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: 52.24 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFqngaESVQILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAgqnisnmsETelahVR 81
Cdd:TIGR03719 323 IEAENLTKAF----GDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG--------ET----VK 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nkeIGFVFQNFMLL-PRLTALQNVELPLIYAGVDKKERRERSLAAL---------TKVGladrathlpnELSGGQKQRVA 151
Cdd:TIGR03719 387 ---LAYVDQSRDALdPNKTVWEEISGGLDIIKLGKREIPSRAYVGRfnfkgsdqqKKVG----------QLSGGERNRVH 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446531755 152 VARAIVNNPKFILADEPTGALDTKTSTQIMDLFyeLNKQGSTIImITHDR 201
Cdd:TIGR03719 454 LAKTLKSGGNVLLLDEPTNDLDVETLRALEEAL--LNFAGCAVV-ISHDR 500
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
30-217 |
7.71e-08 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 50.06 E-value: 7.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 30 QGEFTSIMGPSGSGKSTLMN-IIGCLDKPTTGTYELAGQNISNMSETELAHVRNKEIGfvfqnfmllprltalqnvelpl 108
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 109 iyagvdkkerrerslaaltkvgladrathlpNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMD------ 182
Cdd:smart00382 59 -------------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrl 107
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446531755 183 LFYELNKQGSTIIMITH------DREIGEAAARQIVIRDGN 217
Cdd:smart00382 108 LLLLKSEKNLTVILTTNdekdlgPALLRRRFDRRIVLLLIL 148
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-200 |
1.13e-07 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 51.73 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 27 TLNQGEFTSIMGPSGSGKSTLMNIigcldkpttgtyeLAGQNISNMSETE--------LAHVRNKEIGFVFQnfmllpRL 98
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTTAVKI-------------LSGELIPNLGDYEeepswdevLKRFRGTELQNYFK------KL 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 TA--------LQNVEL-PLIYAG--------VDKKERRERSLAALTKVGLADRAThlpNELSGGQKQRVAVARAIVNNPK 161
Cdd:PRK13409 156 YNgeikvvhkPQYVDLiPKVFKGkvrellkkVDERGKLDEVVERLGLENILDRDI---SELSGGELQRVAIAAALLRDAD 232
|
170 180 190
....*....|....*....|....*....|....*....
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFYELNKqGSTIIMITHD 200
Cdd:PRK13409 233 FYFFDEPTSYLDIRQRLNVARLIRELAE-GKYVLVVEHD 270
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-218 |
3.14e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 50.51 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLDKPTTGTYELAGQ--NISNMSETELAHVR-NKEIGFVFQ--NFML 94
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGTvaYVPQVSWIFNATVRdNILFGSPFDpeRYER 712
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 95 LPRLTALQNvELPLIyAGVDKKERRERSLaaltkvgladrathlpnELSGGQKQRVAVARAIVNNPKFILADEPTGALDT 174
Cdd:PLN03130 713 AIDVTALQH-DLDLL-PGGDLTEIGERGV-----------------NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDA 773
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446531755 175 KTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNV 218
Cdd:PLN03130 774 HVGRQVFDKCIKDELRGKTRVLVTNQLHFLSQVDRIILVHEGMI 817
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
142-221 |
3.37e-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: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD-REIGEAAARQIVIRDGNVVQ 220
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSElAEVLGLSDRVLVIGEGKLKG 483
|
.
gi 446531755 221 D 221
Cdd:TIGR02633 484 D 484
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
142-197 |
3.48e-07 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 49.93 E-value: 3.48e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMI 197
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVI 461
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
36-199 |
3.79e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 50.13 E-value: 3.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 36 IMGPSGSGKSTLMNIIG--------CLDKP--------------TTGTyeLAGQNISNMSETELahvrnKEIGFVFQNFM 93
Cdd:TIGR00954 483 ICGPNGCGKSSLFRILGelwpvyggRLTKPakgklfyvpqrpymTLGT--LRDQIIYPDSSEDM-----KRRGLSDKDLE 555
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 94 LLprltaLQNVELPLIYagvdkkeRRERSLAALtkvglADRAthlpNELSGGQKQRVAVARAIVNNPKFILADEPTGALd 173
Cdd:TIGR00954 556 QI-----LDNVQLTHIL-------EREGGWSAV-----QDWM----DVLSGGEKQRIAMARLFYHKPQFAILDECTSAV- 613
|
170 180
....*....|....*....|....*..
gi 446531755 174 tktSTQIMDLFYELNKQ-GSTIIMITH 199
Cdd:TIGR00954 614 ---SVDVEGYMYRLCREfGITLFSVSH 637
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-200 |
4.97e-07 |
|
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: 48.94 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 27 TLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNIS--------NMSETELAHVRNKEIGFVFQNFMllprl 98
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGTVRDLLSSITKDFYTHPYF----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 talqNVELpliyagvdkkerrersLAALTKVGLADRAThlpNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKT-- 176
Cdd:cd03237 96 ----KTEI----------------AKPLQIEQILDREV---PELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQrl 152
|
170 180
....*....|....*....|....*
gi 446531755 177 -STQIMDLFYELNKqgSTIIMITHD 200
Cdd:cd03237 153 mASKVIRRFAENNE--KTAFVVEHD 175
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
2-220 |
5.39e-07 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 49.08 E-value: 5.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKpTTGTYELAGQNISNMSETELahvr 81
Cdd:cd03289 3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKW---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 NKEIGFVFQNFMLLPRlTALQNVElPLiyagvdKKERRERSLAALTKVGLADRATHLPNEL-----------SGGQKQRV 150
Cdd:cd03289 76 RKAFGVIPQKVFIFSG-TFRKNLD-PY------GKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLM 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTStQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVVQ 220
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITY-QVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQ 216
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
140-207 |
1.17e-06 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.74 E-value: 1.17e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 140 NELSGGQKQ------RVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTI---IMITHDREIGEAA 207
Cdd:PRK01156 800 DSLSGGEKTavafalRVAVAQFLNNDKSLLIMDEPTAFLDEDRRTNLKDIIEYSLKDSSDIpqvIMISHHRELLSVA 876
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
123-216 |
3.64e-06 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 47.13 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 123 LAALTKVGLA----DRAThlpNELSGGQKQRVAVAR---AIVNNPKFILaDEPTGALDTKTSTQIMDLFYELNKQGSTII 195
Cdd:PRK00635 457 LSILIDLGLPyltpERAL---ATLSGGEQERTALAKhlgAELIGITYIL-DEPSIGLHPQDTHKLINVIKKLRDQGNTVL 532
|
90 100
....*....|....*....|.
gi 446531755 196 MITHDREIGEAAARQIVIRDG 216
Cdd:PRK00635 533 LVEHDEQMISLADRIIDIGPG 553
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
142-198 |
4.18e-06 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 46.65 E-value: 4.18e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMIT 198
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIIS 448
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-218 |
5.58e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 46.86 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELAGQNISNMSeteLAHVRNKeIGFVFQNfmllprlt 99
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIG---LHDLRFK-ITIIPQD-------- 1368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 100 alqnvelPLIYAGVDK-------KERRERSLAALTKVGLADRATHLPNEL-----------SGGQKQRVAVARAIVNNPK 161
Cdd:TIGR00957 1369 -------PVLFSGSLRmnldpfsQYSDEEVWWALELAHLKTFVSALPDKLdhecaeggenlSVGQRQLVCLARALLRKTK 1441
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446531755 162 FILADEPTGALDTKTSTQIMDLFyELNKQGSTIIMITHDREIGEAAARQIVIRDGNV 218
Cdd:TIGR00957 1442 ILVLDEATAAVDLETDNLIQSTI-RTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
21-203 |
7.53e-06 |
|
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: 45.68 E-value: 7.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMNII--GCLDKPTTGTYELAG--QNISNMSETE-LAHVRNKEIGFVfqnfmll 95
Cdd:cd03271 11 LKNIDVDIPLGVLTCVTGVSGSGKSSLINDTlyPALARRLHLKKEQPGnhDRIEGLEHIDkVIVIDQSPIGRT------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 96 PRltalQNvelPLIYAGV-------------DKKERRE---------------------------------RSLAALTKV 129
Cdd:cd03271 84 PR----SN---PATYTGVfdeirelfcevckGKRYNREtlevrykgksiadvldmtveealeffenipkiaRKLQTLCDV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 130 GL-----ADRAThlpnELSGGQKQRVAVARAIVNNPK----FILaDEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHD 200
Cdd:cd03271 157 GLgyiklGQPAT----TLSGGEAQRIKLAKELSKRSTgktlYIL-DEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHN 231
|
...
gi 446531755 201 REI 203
Cdd:cd03271 232 LDV 234
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
24-214 |
9.62e-06 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 44.95 E-value: 9.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 24 IDVT-LNQGEFTSIMGPSGSGKSTLMNIIgcldkpttgTYELAGQNISNMSETELAHVRNK-----EIGFVFQNFMLLPR 97
Cdd:cd03279 20 IDFTgLDNNGLFLICGPTGAGKSTILDAI---------TYALYGKTPRYGRQENLRSVFAPgedtaEVSFTFQLGGKKYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 98 LTAlqnvelpliYAGVDKKERRErslAALTKVGLADRATHLPNE-LSGGQKQRVAVARAI-----VNNPK-------FIl 164
Cdd:cd03279 91 VER---------SRGLDYDQFTR---IVLLPQGEFDRFLARPVStLSGGETFLASLSLALalsevLQNRGgarlealFI- 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446531755 165 aDEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIR 214
Cdd:cd03279 158 -DEGFGTLDPEALEAVATALELIRTENRMVGVISHVEELKERIPQRLEVI 206
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
2-202 |
1.05e-05 |
|
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: 46.06 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 2 INLKGITKSFQNGAESVqiLHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLdKPTTGTYELAGQNISNMSeteLAHVR 81
Cdd:TIGR01271 1218 MDVQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT---LQTWR 1291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 82 nKEIGFVFQNFMLLPRlTALQNVelpliyagvDKKER--RERSLAALTKVGLADRATHLPNEL-----------SGGQKQ 148
Cdd:TIGR01271 1292 -KAFGVIPQKVFIFSG-TFRKNL---------DPYEQwsDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQ 1360
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446531755 149 RVAVARAIVNNPKFILADEPTGALDTKTsTQIMDLFYELNKQGSTIIMITHDRE 202
Cdd:TIGR01271 1361 LMCLARSILSKAKILLLDEPSAHLDPVT-LQIIRKTLKQSFSNCTVILSEHRVE 1413
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
4-224 |
1.20e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 45.27 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 4 LKGITKSFQNGaesvQILHGIDVTLNQGEFTSIMGPSGSGKSTLMN-IIGCLdKPTTGTYELAgqnisnmsetelahvRN 82
Cdd:PRK15064 322 VENLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGEL-EPDSGTVKWS---------------EN 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 83 KEIGFV-------FQNFMLLprltalqnVELPLIYAGVDKKERRERS-LAALtkvgL--ADRATHLPNELSGGQKQRVAV 152
Cdd:PRK15064 382 ANIGYYaqdhaydFENDLTL--------FDWMSQWRQEGDDEQAVRGtLGRL----LfsQDDIKKSVKVLSGGEKGRMLF 449
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 153 ARAIVNNPKFILADEPTGALDTKTstqIMDLFYELNKQGSTIIMITHDRE-IGEAAARQIVIRDGNVVqDWRG 224
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMES---IESLNMALEKYEGTLIFVSHDREfVSSLATRIIEITPDGVV-DFSG 518
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
21-199 |
1.76e-05 |
|
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: 45.00 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMN-----------------------IIGC--LDK------------PTT--GT 61
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINdtlypalanrlngaktvpgrytsIEGLehLDKvihidqspigrtPRSnpAT 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 62 YELAGQNISNM-SETELAHVRNKEIG-FVFQnfMLLPRLTALQ-----NVE---LPLIYAGVD----KKERRE------- 120
Cdd:TIGR00630 704 YTGVFDEIRELfAETPEAKVRGYTPGrFSFN--VKGGRCEACQgdgviKIEmhfLPDVYVPCEvckgKRYNREtlevkyk 781
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 121 --------------------------RSLAALTKVGL-----ADRAThlpnELSGGQKQRVAVARAI---VNNPKFILAD 166
Cdd:TIGR00630 782 gkniadvldmtveeayeffeavpsisRKLQTLCDVGLgyirlGQPAT----TLSGGEAQRIKLAKELskrSTGRTLYILD 857
|
250 260 270
....*....|....*....|....*....|...
gi 446531755 167 EPTGALDTKTSTQIMDLFYELNKQGSTIIMITH 199
Cdd:TIGR00630 858 EPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEH 890
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
140-224 |
2.03e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 140 NELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTstqIMDLFYELNKQGSTIIMITHDREIGEAAARQIVIRDGNVV 219
Cdd:PLN03073 343 KTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA---VLWLETYLLKWPKTFIVVSHAREFLNTVVTDILHLHGQKL 419
|
....*
gi 446531755 220 QDWRG 224
Cdd:PLN03073 420 VTYKG 424
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
20-203 |
2.48e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 44.39 E-value: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 20 ILHGIDVTLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELA-GQNISNMSETELAHVRNKEigfvfqnfmllprl 98
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRADE-------------- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 99 TALQNVelpliyAGVDKKERRERSLAALTKVGL-ADRATHLPNELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTS 177
Cdd:PRK10636 393 SPLQHL------ARLAPQELEQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMR 466
|
170 180
....*....|....*....|....*.
gi 446531755 178 TQIMDLFYELNkqgSTIIMITHDREI 203
Cdd:PRK10636 467 QALTEALIDFE---GALVVVSHDRHL 489
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
21-49 |
2.56e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 2.56e-05
10 20
....*....|....*....|....*....
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMN 49
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
21-49 |
2.81e-05 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 44.29 E-value: 2.81e-05
10 20
....*....|....*....|....*....
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTLMN 49
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
125-203 |
4.94e-05 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 44.05 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 125 ALTKVGLadraTHLP-----NELSGGQKQRVAVARAIVN---NPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIM 196
Cdd:PRK00635 792 ALCSLGL----DYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVI 867
|
....*..
gi 446531755 197 ITHDREI 203
Cdd:PRK00635 868 IEHNMHV 874
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
142-202 |
7.83e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.02 E-value: 7.83e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTstqiMDLFYEL--NKQGsTIIMITHDRE 202
Cdd:PRK11147 441 LSGGERNRLLLARLFLKPSNLLILDEPTNDLDVET----LELLEELldSYQG-TVLLVSHDRQ 498
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
116-213 |
2.19e-04 |
|
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: 41.92 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 116 KERRERsLAALTKVGLA----DRAThlpNELSGGQKQRVAVARAI---VNNPKFILaDEPTGALDTKTSTQIMDLFYELN 188
Cdd:TIGR00630 463 KEIRER-LGFLIDVGLDylslSRAA---GTLSGGEAQRIRLATQIgsgLTGVLYVL-DEPSIGLHQRDNRRLINTLKRLR 537
|
90 100
....*....|....*....|....*
gi 446531755 189 KQGSTIIMITHDREIGEAAARQIVI 213
Cdd:TIGR00630 538 DLGNTLIVVEHDEDTIRAADYVIDI 562
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
21-47 |
3.91e-04 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 41.17 E-value: 3.91e-04
10 20
....*....|....*....|....*..
gi 446531755 21 LHGIDVTLNQGEFTSIMGPSGSGKSTL 47
Cdd:COG0178 16 LKNIDVDIPRNKLVVITGLSGSGKSSL 42
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
141-200 |
4.86e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 4.86e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446531755 141 ELSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGS-TIIMITHD 200
Cdd:cd03222 71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHD 131
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-200 |
6.31e-04 |
|
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: 40.15 E-value: 6.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 27 TLNQGEFTSIMGPSGSGKSTLMNIIGCLDKPTTGTYELA------GQNISNMS----ETELAHVRNKEIGfvfqnfmllp 96
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisykPQYISPDYdgtvEEFLRSANTDDFG---------- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 97 rlTALQNVEL--PLiyaGVDKkeRRERSLaaltkvgladrathlpNELSGGQKQRVAVARAIVNNPKFILADEPTGALD- 173
Cdd:COG1245 432 --SSYYKTEIikPL---GLEK--LLDKNV----------------KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDv 488
|
170 180 190
....*....|....*....|....*....|...
gi 446531755 174 ------TKTSTQIMDlfyelnKQGSTIIMITHD 200
Cdd:COG1245 489 eqrlavAKAIRRFAE------NRGKTAMVVDHD 515
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
17-202 |
6.40e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 40.15 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 17 SVQILHGIDV-------TLNQGEFTSIMGPSGSGKSTLMNII--------GCLDKPttGTYELA--GQNISNMSETELAH 79
Cdd:PRK10636 6 SLQIRRGVRVlldnataTINPGQKVGLVGKNGCGKSTLLALLkneisadgGSYTFP--GNWQLAwvNQETPALPQPALEY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 80 VRNKEigfvfQNFMLLPRLTALQNVE-----LPLIYAGVDKKER---RERSLAALTKVGLADRATHLP-NELSGGQKQRV 150
Cdd:PRK10636 84 VIDGD-----REYRQLEAQLHDANERndghaIATIHGKLDAIDAwtiRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446531755 151 AVARAIVNNPKFILADEPTGALDTKTstqIMDLFYELNKQGSTIIMITHDRE 202
Cdd:PRK10636 159 NLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLKSYQGTLILISHDRD 207
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
140-200 |
2.34e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 38.64 E-value: 2.34e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 140 NELSGGQKQRVAVARAIVNNPKFILADEPTGALD-------TKTSTQIMDlfyelnKQGSTIIMITHD 200
Cdd:PRK13409 452 KDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDveqrlavAKAIRRIAE------EREATALVVDHD 513
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
117-200 |
2.79e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 117 ERRERSLAALTKVGLAdratHLP-----NELSGGQKQRVAVARAIVNNPK---FILADEPTGALDTKTSTQIMDLFYELN 188
Cdd:PRK00635 1674 KKIQKPLQALIDNGLG----YLPlgqnlSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLV 1749
|
90
....*....|..
gi 446531755 189 KQGSTIIMITHD 200
Cdd:PRK00635 1750 SLGHSVIYIDHD 1761
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
33-213 |
2.88e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 37.29 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 33 FTSIMGPSGSGKSTLMNIIgcldkpttgTYELAGQNISNMSETELAHVrnkeigfvfqnfmllprltalqnvelpliyag 112
Cdd:cd03239 24 FNAIVGPNGSGKSNIVDAI---------CFVLGGKAAKLRRGSLLFLA-------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446531755 113 vdKKERRERSLAALTKVGLADRATHLPNE-----LSGGQKQRVAVA-----RAIVNNPKFILaDEPTGALDTKTSTQIMD 182
Cdd:cd03239 63 --GGGVKAGINSASVEITFDKSYFLVLQGkveqiLSGGEKSLSALAlifalQEIKPSPFYVL-DEIDAALDPTNRRRVSD 139
|
170 180 190
....*....|....*....|....*....|.
gi 446531755 183 LFYELNKQGSTIIMITHDREIGEAAARQIVI 213
Cdd:cd03239 140 MIKEMAKHTSQFIVITLKKEMFENADKLIGV 170
|
|
| AAA_29 |
pfam13555 |
P-loop containing region of AAA domain; |
22-48 |
3.11e-03 |
|
P-loop containing region of AAA domain;
Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.88 E-value: 3.11e-03
10 20
....*....|....*....|....*..
gi 446531755 22 HGIDVTLNQGEFTSIMGPSGSGKSTLM 48
Cdd:pfam13555 13 DGHTIPIDPRGNTLLTGPSGSGKSTLL 39
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
142-181 |
4.12e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 37.90 E-value: 4.12e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIM 181
Cdd:PLN03140 337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIV 376
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
139-203 |
4.59e-03 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 37.37 E-value: 4.59e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446531755 139 PNELSGGQKQ---RVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMITHDREI 203
Cdd:pfam13304 234 AFELSDGTKRllaLLAALLSALPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLL 301
|
|
| ABC_SMC1_euk |
cd03275 |
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of ... |
32-51 |
5.12e-03 |
|
ATP-binding cassette domain of eukaryotic SMC1 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213242 [Multi-domain] Cd Length: 247 Bit Score: 37.17 E-value: 5.12e-03
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
142-197 |
9.49e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 36.69 E-value: 9.49e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 446531755 142 LSGGQKQRVAVARAIVNNPKFILADEPTGALDTKTSTQIMDLFYELNKQGSTIIMI 197
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVI 460
|
|
| |
