|
Name |
Accession |
Description |
Interval |
E-value |
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
3-217 |
2.44e-125 |
|
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: 354.43 E-value: 2.44e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 3 STPIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGR 82
Cdd:COG4181 5 SAPIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ARLRAEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTR 162
Cdd:COG4181 85 ARLRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 163 PSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:COG4181 165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRL 219
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
4-217 |
7.74e-107 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 307.36 E-value: 7.74e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRA 83
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 84 RLRAEQVGFVFQSFLLLPTLSALENVMLPAELRGETR--CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMT 161
Cdd:COG1136 82 RLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRkeRRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 162 RPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRL 217
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
7-217 |
6.29e-100 |
|
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: 289.78 E-value: 6.29e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLR 86
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 AEQVGFVFQSFLLLPTLSALENVMLPAELRGETR--CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKkeRRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIEL 213
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-215 |
2.50e-91 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 268.19 E-value: 2.50e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEE 80
Cdd:PRK10584 1 MPAENIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 GRARLRAEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPR--ARELLAAVGLGERLHHLPPRLSGGEQQRVAIARA 158
Cdd:PRK10584 81 ARAKLRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRngAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARA 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 780224413 159 FMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQL 215
Cdd:PRK10584 161 FNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
6-217 |
5.28e-80 |
|
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]
Pssm-ID: 131266 [Multi-domain] Cd Length: 221 Bit Score: 239.18 E-value: 5.28e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARL 85
Cdd:TIGR02211 1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEP--RARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:TIGR02211 81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAkeRAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEM 214
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
6-216 |
3.94e-72 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 219.15 E-value: 3.94e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQEsltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARL 85
Cdd:COG2884 1 MIRFENVSKRYPGGRE---ALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RaEQVGFVFQSFLLLPTLSALENVMLPAELRGETR--CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:COG2884 78 R-RRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRkeIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQRCQRQLV 216
Cdd:COG2884 157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVL 208
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
2-217 |
1.13e-63 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 198.12 E-value: 1.13e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEG 81
Cdd:PRK11629 1 MNKILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 82 RARLRAEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEP--RARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAF 159
Cdd:PRK11629 81 KAELRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEInsRALEMLAAVGLEHRANHRPSELSGGERQRVAIARAL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 160 MTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK11629 161 VNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEM 218
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-217 |
1.18e-62 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 196.46 E-value: 1.18e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNST-PIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDE 79
Cdd:COG1116 1 MSAAaPALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 80 EgrarlraeqVGFVFQSFLLLPTLSALENVMLPAELRGETR--CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIAR 157
Cdd:COG1116 81 D---------RGVVFQEPALLPWLTVLDNVALGLELRGVPKaeRRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAR 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780224413 158 AFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD-HE---LAQRCqrqLVM 217
Cdd:COG1116 152 ALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvDEavfLADRV---VVL 212
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
5-213 |
1.33e-62 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 196.05 E-value: 1.33e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLGKTVRLGQeslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRAR 84
Cdd:COG3638 1 PMLELRNLSKRYPGGT---PALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LRAeQVGFVFQSFLLLPTLSALENV----------------MLPAELRgetrcePRARELLAAVGLGERLHHLPPRLSGG 148
Cdd:COG3638 78 LRR-RIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsllgLFPPEDR------ERALEALERVGLADKAYQRADQLSGG 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 149 EQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQR 213
Cdd:COG3638 151 QQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADR 216
|
|
| FtsE |
TIGR02673 |
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ... |
25-210 |
1.10e-59 |
|
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: 187.46 E-value: 1.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRaEQVGFVFQSFLLLPTLS 104
Cdd:TIGR02673 17 ALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLLR-RRIGVVFQDFRLLPDRT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRG--ETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGER 182
Cdd:TIGR02673 96 VYENVALPLEVRGkkEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSER 175
|
170 180
....*....|....*....|....*...
gi 780224413 183 VIELLFELNReHGTTLVVVTHDHELAQR 210
Cdd:TIGR02673 176 ILDLLKRLNK-RGTTVIVATHDLSLVDR 202
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
6-204 |
1.99e-58 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 184.81 E-value: 1.99e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKtvRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLqLDEEGRARL 85
Cdd:COG1126 1 MIEIENLHK--SFG--DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAEqVGFVFQSFLLLPTLSALENVML-PAELRGETR--CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTR 162
Cdd:COG1126 76 RRK-VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKaeAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 780224413 163 PSLLLADEPTGNLD-SKTGErVIELLFELNREhGTTLVVVTHD 204
Cdd:COG1126 155 PKVMLFDEPTSALDpELVGE-VLDVMRDLAKE-GMTMVVVTHE 195
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
4-213 |
3.51e-58 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 194.94 E-value: 3.51e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRA 83
Cdd:PRK10535 2 TALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 84 RLRAEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMT 161
Cdd:PRK10535 82 QLRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQrlLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMN 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 780224413 162 RPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQRCQR 213
Cdd:PRK10535 162 GGQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAER 212
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
7-210 |
3.52e-57 |
|
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: 181.13 E-value: 3.52e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldeEGRARlr 86
Cdd:cd03293 1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPV-----TGPGP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeQVGFVFQSFLLLPTLSALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:cd03293 74 --DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEarERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD-HE---LAQR 210
Cdd:cd03293 152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDiDEavfLADR 201
|
|
| heterocyst_DevA |
TIGR02982 |
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ... |
6-205 |
1.73e-56 |
|
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: 179.44 E-value: 1.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARL 85
Cdd:TIGR02982 1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RaEQVGFVFQSFLLLPTLSALENVMLPAEL-----RGETRCepRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFM 160
Cdd:TIGR02982 81 R-RRIGYIFQAHNLLGFLTARQNVQMALELqpnlsYQEARE--RARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALV 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 780224413 161 TRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDH 205
Cdd:TIGR02982 158 HHPKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDN 202
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-217 |
2.10e-56 |
|
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: 179.70 E-value: 2.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARL 85
Cdd:cd03258 1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAeQVGFVFQSFLLLPTLSALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:cd03258 81 RR-RIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEieERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03258 160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVM 214
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
6-217 |
1.77e-55 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 180.66 E-value: 1.77e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARL 85
Cdd:COG1135 1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAeQVGFVFQSFLLLPTLSALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:COG1135 81 RR-KIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEirKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG1135 160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVL 214
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-204 |
5.43e-54 |
|
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: 173.63 E-value: 5.43e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 3 STPIINVKGLgkTVRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGR 82
Cdd:COG1127 2 SEPMIEVRNL--TKSFG--DRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ARLRAeQVGFVFQSFLLLPTLSALENVMLPaeLR-----GETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIAR 157
Cdd:COG1127 78 YELRR-RIGMLFQGGALFDSLTVFENVAFP--LRehtdlSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALAR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 780224413 158 AFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:COG1127 155 ALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHD 201
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
6-217 |
6.02e-54 |
|
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: 173.08 E-value: 6.02e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRaRL 85
Cdd:cd03257 1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLR-KI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAEQVGFVFQ-SFLLL-PTLSALENVMLPAELRG--ETRCEPRARELLAAVGLG---ERLHHLPPRLSGGEQQRVAIARA 158
Cdd:cd03257 80 RRKEIQMVFQdPMSSLnPRMTIGEQIAEPLRIHGklSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 159 FMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKiADRVAVM 219
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
7-209 |
6.48e-54 |
|
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: 172.71 E-value: 6.48e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKtvRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQlDEEGRARLR 86
Cdd:cd03262 1 IEIKNLHK--SFG--DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 AEqVGFVFQSFLLLPTLSALENVML-PAELRGETRCEP--RARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:cd03262 76 QK-VGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAeeRALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQ 209
Cdd:cd03262 155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAR 199
|
|
| L_ocin_972_ABC |
TIGR03608 |
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ... |
24-213 |
1.19e-53 |
|
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: 171.64 E-value: 1.19e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRAEQVGFVFQSFLLLPTL 103
Cdd:TIGR03608 12 VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRREKLGYLFQNFALIENE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:TIGR03608 92 TVEENLDLGLKYKKLSKKEKREKkkEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRD 171
|
170 180 190
....*....|....*....|....*....|..
gi 780224413 182 RVIELLFELNREhGTTLVVVTHDHELAQRCQR 213
Cdd:TIGR03608 172 EVLDLLLELNDE-GKTIIIVTHDPEVAKQADR 202
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
6-216 |
1.94e-53 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 172.20 E-value: 1.94e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKtvRLGQesLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLqlDEEGRARL 85
Cdd:PRK09493 1 MIEFKNVSK--HFGP--TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN--DPKVDERL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAEQVGFVFQSFLLLPTLSALENVML-PAELRGETRCEPR--ARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTR 162
Cdd:PRK09493 75 IRQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEkqARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 780224413 163 PSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQRCQRQLV 216
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLI 207
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
2-217 |
3.31e-51 |
|
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: 173.94 E-value: 3.31e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKTVRL-GQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEE 80
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 GRARLRAeQVGFVFQ----SflLLPTLSALENVMLPAELRGETR---CEPRARELLAAVGLGERLHHLPPR-LSGGEQQR 152
Cdd:COG1123 336 SLRELRR-RVQMVFQdpysS--LNPRMTVGDIIAEPLRLHGLLSraeRRERVAELLERVGLPPDLADRYPHeLSGGQRQR 412
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 153 VAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG1123 413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVM 478
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
3-206 |
4.88e-51 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 169.51 E-value: 4.88e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 3 STPIINVKGLGKtvRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldeegr 82
Cdd:COG3842 2 AMPALELENVSK--RYG--DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDV-------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ARLRAEQ--VGFVFQSFLLLPTLSALENVMLPAELRGETR--CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARA 158
Cdd:COG3842 70 TGLPPEKrnVGMVFQDYALFPHLTVAENVAFGLRMRGVPKaeIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARA 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 159 FMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHE 206
Cdd:COG3842 150 LAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE 197
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
7-213 |
5.24e-51 |
|
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: 166.20 E-value: 5.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQeslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLR 86
Cdd:cd03256 1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 AeQVGFVFQSFLLLPTLSALENVM---------LPAELRGETRCE-PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIA 156
Cdd:cd03256 78 R-QIGMIFQQFNLIERLSVLENVLsgrlgrrstWRSLFGLFPKEEkQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 157 RAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQR 213
Cdd:cd03256 157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADR 214
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
7-217 |
1.76e-50 |
|
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: 164.60 E-value: 1.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLgkTVRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLR 86
Cdd:cd03261 1 IELRGL--TKSFG--GRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 AeQVGFVFQSFLLLPTLSALENVMLPaeLR-----GETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMT 161
Cdd:cd03261 77 R-RMGMLFQSGALFDSLTVFENVAFP--LRehtrlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 162 RPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAV 209
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
26-216 |
1.93e-50 |
|
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: 163.73 E-value: 1.93e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRaEQVGFVFQSFLLLPTLSA 105
Cdd:cd03292 17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR-RKIGVVFQDFRLLPDRNV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:cd03292 96 YENVAFALEVTGVPPREIRKRvpAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEI 175
|
170 180 190
....*....|....*....|....*....|...
gi 780224413 184 IELLFELNREhGTTLVVVTHDHELAQRCQRQLV 216
Cdd:cd03292 176 MNLLKKINKA-GTTVVVATHAKELVDTTRHRVI 207
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
7-217 |
2.47e-50 |
|
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: 164.59 E-value: 2.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldEEGRARLR 86
Cdd:COG1124 2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPV----TRRRRKAF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 AEQVGFVFQSFL--LLPTLSALENVMLPAELRGETRCEPRARELLAAVGLGER-LHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:COG1124 78 RRRVQMVFQDPYasLHPRHTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALILEP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG1124 158 ELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVM 212
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
4-217 |
2.94e-50 |
|
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: 163.76 E-value: 2.94e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLGKTVRL---GQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQS----LLQ 76
Cdd:COG4778 2 TTLLEVENLSKTFTLhlqGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 77 LDEEGRARLRAEQVGFVFQsFL-LLPTLSALENVMLPAELRGETR--CEPRARELLAAVGLGERLHHLPPR-LSGGEQQR 152
Cdd:COG4778 82 ASPREILALRRRTIGYVSQ-FLrVIPRVSALDVVAEPLLERGVDReeARARARELLARLNLPERLWDLPPAtFSGGEQQR 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 153 VAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG4778 161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAvADRVVDV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
4-217 |
3.49e-49 |
|
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: 168.54 E-value: 3.49e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPS---QGDIEILGQSLLQLDEe 80
Cdd:COG1123 2 TPLLEVRDL--SVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSE- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 graRLRAEQVGFVFQSFLL-LPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIAR 157
Cdd:COG1123 79 ---ALRGRRIGMVFQDPMTqLNPVTVGDQIAEALENLGLSRAEARARvlELLEAVGLERRLDRYPHQLSGGQRQRVAIAM 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 780224413 158 AFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHEL-AQRCQRQLVM 217
Cdd:COG1123 156 ALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVvAEIADRVVVM 216
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
16-217 |
1.21e-48 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 158.83 E-value: 1.21e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 16 VRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgraRLRAeQVGFVFQ 95
Cdd:COG4619 6 LSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPP---EWRR-QVAYVPQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 96 -SFLLLPTLSalENVMLPAELRGETRCEPRARELLAAVGLGER-LHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:COG4619 82 ePALWGGTVR--DNLPFPFQLRERKFDRERALELLERLGLPPDiLDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 780224413 174 NLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG4619 160 ALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTL 204
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
25-217 |
7.25e-48 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 156.86 E-value: 7.25e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegrARLRAEQVGFVFQ---SFLLLP 101
Cdd:cd03225 16 ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLS----LKELRRKVGLVFQnpdDQFFGP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TL-----SALENVMLPAELRGEtrcepRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:cd03225 92 TVeeevaFGLENLGLPEEEIEE-----RVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLD 166
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 177 SKTGERVIELLFELNREhGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:cd03225 167 PAGRRELLELLKKLKAE-GKTIIIVTHDlDLLLELADRVIVL 207
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
9-217 |
8.82e-48 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 156.91 E-value: 8.82e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 9 VKGLGKTVRlgqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRArlrae 88
Cdd:cd03259 3 LKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN----- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 89 qVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03259 74 -IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARvrELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03259 153 LLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVM 204
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
24-217 |
3.54e-47 |
|
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];
Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 155.95 E-value: 3.54e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqlDEEGRARLRaEQVGFVFQ---SFLLL 100
Cdd:COG1122 15 PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELR-RKVGLVFQnpdDQLFA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 101 PTLsaLENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSK 178
Cdd:COG1122 91 PTV--EEDVAFGPENLGLPREEIRERveEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPR 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 179 TGERVIELLFELNREhGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG1122 169 GRRELLELLKRLNKE-GKTVIIVTHDLDLVAElADRVIVL 207
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-217 |
7.60e-47 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 158.43 E-value: 7.60e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLR 86
Cdd:PRK11153 2 IELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:PRK11153 82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARvtELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRiCDRVAVI 214
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
24-217 |
1.56e-46 |
|
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is comprised of all BPD (Binding Protein Dependent) systems that are largely represented in archaea and eubacteria and are primarily involved in scavenging solutes from the environment. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213196 [Multi-domain] Cd Length: 178 Bit Score: 152.73 E-value: 1.56e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRaeQVGFVFQSFLLLPTL 103
Cdd:cd03229 14 TVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPLRR--RIGMVFQDFALFPHL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPaelrgetrceprarellaavglgerlhhlpprLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:cd03229 92 TVLENIALG--------------------------------LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREV 139
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 184 IELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03229 140 RALLKSLQAQLGITVVLVTHDLDEAARlADRVVVL 174
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
7-217 |
4.73e-46 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 153.30 E-value: 4.73e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRlgqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlr 86
Cdd:COG1131 1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeqVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:COG1131 75 ---IGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERidELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:COG1131 152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAII 204
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
6-210 |
1.10e-45 |
|
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: 152.45 E-value: 1.10e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQeslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARL 85
Cdd:TIGR02315 1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAeQVGFVFQSFLLLPTLSALENVM---------LPAELRGETRCEP-RARELLAAVGLGERLHHLPPRLSGGEQQRVAI 155
Cdd:TIGR02315 78 RR-RIGMIFQHYNLIERLTVLENVLhgrlgykptWRSLLGRFSEEDKeRALSALERVGLADKAYQRADQLSGGQQQRVAI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 156 ARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR 210
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKK 211
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-217 |
1.01e-44 |
|
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: 152.13 E-value: 1.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLP---SQGDIEILGQSLLQLDEEGR 82
Cdd:COG0444 1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ARLRAEQVGFVFQSFL--LLPTLSALENVMLPAEL-RGETRCEPRAR--ELLAAVGL---GERLHHLPPRLSGGEQQRVA 154
Cdd:COG0444 81 RKIRGREIQMIFQDPMtsLNPVMTVGDQIAEPLRIhGGLSKAEARERaiELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780224413 155 IARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHEL-AQRCQRQLVM 217
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVvAEIADRVAVM 224
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
7-209 |
2.38e-43 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 146.82 E-value: 2.38e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRlGQeslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQG-----DIEI-LGQSLLQldEE 80
Cdd:PRK11264 4 IEVKNLVKKFH-GQ---TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGtirvgDITIdTARSLSQ--QK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 GRARLRAEQVGFVFQSFLLLPTLSALENVML-PAELRGETRCEP--RARELLAAVGLGERLHHLPPRLSGGEQQRVAIAR 157
Cdd:PRK11264 78 GLIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEAtaRARELLAKVGLAGKETSYPRRLSGGQQQRVAIAR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 780224413 158 AFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHgTTLVVVTHDHELAQ 209
Cdd:PRK11264 158 ALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFAR 208
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
29-210 |
3.45e-43 |
|
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: 147.02 E-value: 3.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRAEQVGFVFQSFLLLPTLSALEN 108
Cdd:cd03294 43 VSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLEN 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 109 VMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIEL 186
Cdd:cd03294 123 VAFGLEVQGVPRAEreERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDE 202
|
170 180
....*....|....*....|....
gi 780224413 187 LFELNREHGTTLVVVTHDHELAQR 210
Cdd:cd03294 203 LLRLQAELQKTIVFITHDLDEALR 226
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-208 |
5.04e-43 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 146.10 E-value: 5.04e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKtvRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSL-LQLDEE 80
Cdd:COG4598 4 TAPPALEVRDLHK--SFG--DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrLKPDRD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 GR---------ARLRAeQVGFVFQSFLLLPTLSALENVML-PAELRGETR--CEPRARELLAAVGLGERLHHLPPRLSGG 148
Cdd:COG4598 80 GElvpadrrqlQRIRT-RLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKaeAIERAEALLAKVGLADKRDAYPAHLSGG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 149 EQQRVAIARAFMTRPSLLLADEPTGNLDSK-TGE--RVIELLfelnREHGTTLVVVTHDHELA 208
Cdd:COG4598 159 QQQRAAIARALAMEPEVMLFDEPTSALDPElVGEvlKVMRDL----AEEGRTMLVVTHEMGFA 217
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
16-211 |
1.15e-41 |
|
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: 141.55 E-value: 1.15e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 16 VRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTL-----LGLLAGLDLPSQGDIEILGQSLLQLDEEgRARLRAeQV 90
Cdd:cd03260 6 LNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLlrllnRLNDLIPGAPDEGEVLLDGKDIYDLDVD-VLELRR-RV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 91 GFVFQSFLLLPtLSALENVMLPAELRGE---TRCEPRARELLAAVGLGE----RLHHLppRLSGGEQQRVAIARAFMTRP 163
Cdd:cd03260 84 GMVFQKPNPFP-GSIYDNVAYGLRLHGIklkEELDERVEEALRKAALWDevkdRLHAL--GLSGGQQQRLCLARALANEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREhgTTLVVVTHDHELAQRC 211
Cdd:cd03260 161 EVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARV 206
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-210 |
1.29e-41 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 142.15 E-value: 1.29e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLgkTVRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldee 80
Cdd:COG1121 1 MMMMPAIELENL--TVSYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 GRARLRaeqVGFVFQSFLLLPT--LSALENVML------PAELRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQR 152
Cdd:COG1121 71 RRARRR---IGYVPQRAEVDWDfpITVRDVVLMgrygrrGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQR 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 153 VAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQR 210
Cdd:COG1121 148 VLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVRE 204
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
24-208 |
4.81e-41 |
|
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 140.06 E-value: 4.81e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRarlraeQVGFVFQSFLLLPTL 103
Cdd:cd03300 14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKR------PVNTVFQNYALFPHL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:cd03300 88 TVFENIAFGLRLKKLPKAEIKERvaEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRK 167
|
170 180
....*....|....*....|....*..
gi 780224413 182 RVIELLFELNREHGTTLVVVTHDHELA 208
Cdd:cd03300 168 DMQLELKRLQKELGITFVFVTHDQEEA 194
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
7-204 |
2.25e-40 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 141.75 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRarlr 86
Cdd:COG3839 4 LELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeQVGFVFQSFLLLPTLSALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:COG3839 76 --NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEidRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:COG3839 154 VFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
7-217 |
2.25e-40 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 141.44 E-value: 2.25e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKtvRLGQESLtiLEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLL-QLDeegrARL 85
Cdd:COG1118 3 IEVRNISK--RFGSFTL--LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFtNLP----PRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RaeQVGFVFQSFLLLPTLSALENVM--LPAELRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:COG1118 75 R--RVGFVFQHYALFPHMTVAENIAfgLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEP 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG1118 153 EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVM 207
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
6-217 |
5.73e-40 |
|
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: 137.87 E-value: 5.73e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLgkTVRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLdeegRARL 85
Cdd:COG1120 1 MLEAENL--SVGYGGR--PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASL----SRRE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAEQVGFVFQSFLLLPTLSALENVML---P--AELRGETRC-EPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAF 159
Cdd:COG1120 73 LARRIAYVPQEPPAPFGLTVRELVALgryPhlGLFGRPSAEdREAVEEALERTGLEHLADRPVDELSGGERQRVLIARAL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 160 MTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG1120 153 AQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARyADRLVLL 211
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
3-217 |
3.60e-39 |
|
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: 135.94 E-value: 3.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 3 STPIINVKGLGKtvRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGR 82
Cdd:COG0411 1 SDPLLEVRGLTK--RFG--GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ARLraeqvGFV--FQSFLLLPTLSALENVML-----------------PAELRGETRCEPRARELLAAVGLGERLHHLPP 143
Cdd:COG0411 77 ARL-----GIArtFQNPRLFPELTVLENVLVaaharlgrgllaallrlPRARREEREARERAEELLERVGLADRADEPAG 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 144 RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG0411 152 NLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGlADRIVVL 226
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
7-217 |
4.67e-39 |
|
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: 133.28 E-value: 4.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLR 86
Cdd:cd03228 1 IEFKNV--SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aEQVGFVFQSFLLLPTlSALENVmlpaelrgetrceprarellaavglgerlhhlpprLSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03228 76 -KNIAYVPQDPFLFSG-TIRENI-----------------------------------LSGGQRQRIAIARALLRDPPIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELnrEHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03228 119 ILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVL 167
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
22-216 |
6.06e-39 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 135.14 E-value: 6.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 22 SLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQ--SLLQLDEEGRARLRAEQVGFVFQSFLL 99
Cdd:COG4161 14 SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLLRQKVGMVFQQYNL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 100 LPTLSALENVM-LPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:COG4161 94 WPHLTVMENLIeAPCKVLGLSKEQAREKamKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAALD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 177 SKTGERVIELLFELNrEHGTTLVVVTHDHELAQRCQRQLV 216
Cdd:COG4161 174 PEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVV 212
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
26-210 |
6.55e-39 |
|
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: 135.12 E-value: 6.55e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgraRLRaEQVGFVFQSFLLLPTLSA 105
Cdd:cd03295 17 VNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPV---ELR-RKIGYVIQQIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRG--ETRCEPRARELLAAVGLGER--LHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:cd03295 93 EENIALVPKLLKwpKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRD 172
|
170 180
....*....|....*....|....*....
gi 780224413 182 RVIELLFELNREHGTTLVVVTHDHELAQR 210
Cdd:cd03295 173 QLQEEFKRLQQELGKTIVFVTHDIDEAFR 201
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-210 |
6.63e-39 |
|
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: 140.98 E-value: 6.63e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKS-----TLLGLLAGLDLPSqGDIEILGQSLL 75
Cdd:COG4172 1 MMSMPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalsILRLLPDPAAHPS-GSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 76 QLDEEGRARLRAEQVGFVFQSflllPtLSAL-----------ENVMLPAELRGEtRCEPRARELLAAVGLGE---RLHHL 141
Cdd:COG4172 80 GLSERELRRIRGNRIAMIFQE----P-MTSLnplhtigkqiaEVLRLHRGLSGA-AARARALELLERVGIPDperRLDAY 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 142 PPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD----HELAQR 210
Cdd:COG4172 154 PHQLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDlgvvRRFADR 226
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
9-217 |
5.80e-38 |
|
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: 132.18 E-value: 5.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 9 VKGLgkTVRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRae 88
Cdd:cd03219 3 VRGL--TKRFG--GLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 89 qVGFVFQSFLLLPTLSALENVMLPAELRG------------ETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIA 156
Cdd:cd03219 77 -IGRTFQIPRLFPELTVLENVMVAAQARTgsglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 780224413 157 RAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSlADRVTVL 216
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
15-204 |
8.68e-38 |
|
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: 131.12 E-value: 8.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldEEGRARlraeqVGFVF 94
Cdd:cd03235 6 TVSYGGH--PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL----EKERKR-----IGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 95 QSFLLLPT--LSALENVMLPAE-----LRGETR-CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03235 75 QRRSIDRDfpISVRDVVLMGLYghkglFRRLSKaDKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHD 204
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHD 191
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
7-210 |
1.23e-37 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 131.67 E-value: 1.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQesltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQS--LLQLDEEGRAR 84
Cdd:PRK11124 3 IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHfdFSKTPSDKAIR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LRAEQVGFVFQSFLLLPTLSALENVM-LPAELRGETRCEP--RARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMT 161
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNLIeAPCRVLGLSKDQAlaRAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 780224413 162 RPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQR 210
Cdd:PRK11124 159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARK 206
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-208 |
1.46e-37 |
|
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely related to ModC. ModC is an ABC-type transporter and the ATPase component of a molybdate transport system that also includes the periplasmic binding protein ModA and the membrane protein ModB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213266 [Multi-domain] Cd Length: 235 Bit Score: 131.30 E-value: 1.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRarlraeQVGFVFQSFLLLPTLSA 105
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR------DISYVPQNYALFPHMTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:cd03299 89 YKNIAYGLKKRKVDKKEieRKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
|
170 180
....*....|....*....|....*
gi 780224413 184 IELLFELNREHGTTLVVVTHDHELA 208
Cdd:cd03299 169 REELKKIRKEFGVTVLHVTHDFEEA 193
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
19-208 |
1.54e-37 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 131.91 E-value: 1.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 19 GQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegrarlrAEQvGFVFQSFL 98
Cdd:COG4525 16 GGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG--------ADR-GVVFQKDA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSALENVMLPAELRGETR--CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:COG4525 87 LLPWLNVLDNVAFGLRLRGVPKaeRRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALD 166
|
170 180 190
....*....|....*....|....*....|..
gi 780224413 177 SKTGERVIELLFELNREHGTTLVVVTHDHELA 208
Cdd:COG4525 167 ALTREQMQELLLDVWQRTGKGVFLITHSVEEA 198
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
5-213 |
3.85e-37 |
|
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: 129.14 E-value: 3.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLgkTVRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRAR 84
Cdd:COG4133 1 MMLEAENL--SCRRGER--LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LraeqvGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:COG4133 77 L-----AYLGHADGLKPELTVRENLRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQRCQR 213
Cdd:COG4133 152 LWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELAAARV 199
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-217 |
4.47e-37 |
|
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: 129.89 E-value: 4.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARLraeqvgFVFQSFLLLPTLSA 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGK---QITEPGPDRM------VVFQNYSLLPWLTV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAE--LRGETRCEPRA--RELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:TIGR01184 72 RENIALAVDrvLPDLSKSERRAivEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 780224413 182 RVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVM 187
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-217 |
9.75e-37 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 130.19 E-value: 9.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLGKTVRLG-----QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLD 78
Cdd:PRK10419 1 MTLLNVSGLSHHYAHGglsgkHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 79 EEGRARLRAEqVGFVFQSFL--LLPTLSALENVMLPaeLR-----GETRCEPRARELLAAVGLG-ERLHHLPPRLSGGEQ 150
Cdd:PRK10419 81 RAQRKAFRRD-IQMVFQDSIsaVNPRKTVREIIREP--LRhllslDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 151 QRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERfCQRVMVM 225
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-217 |
9.80e-37 |
|
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 129.93 E-value: 9.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLG-----QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEE 80
Cdd:TIGR02769 2 LLEVRDVTHTYRTGglfgaKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 GRARLRAEqVGFVFQSFL--LLPTLSALENVMLPAE---LRGETRCEPRARELLAAVGL-GERLHHLPPRLSGGEQQRVA 154
Cdd:TIGR02769 82 QRRAFRRD-VQLVFQDSPsaVNPRMTVRQIIGEPLRhltSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRIN 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780224413 155 IARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVM 224
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
22-217 |
1.26e-36 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 129.15 E-value: 1.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 22 SLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegrarLRAEQVGFVFQSFLLLP 101
Cdd:TIGR00968 12 SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDRKIGFVFQHYALFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKT 179
Cdd:TIGR00968 86 HLTVRDNIAFGLEIRKHPKAKIKARveELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDAKV 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 780224413 180 GERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR00968 166 RKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVV 203
|
|
| OpuBA |
COG1125 |
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ... |
24-204 |
1.32e-36 |
|
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 130.60 E-value: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgraRLRaEQVGFVFQSFLLLPTL 103
Cdd:COG1125 16 VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPV---ELR-RRIGYVIQQIGLFPHM 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRG--ETRCEPRARELLAAVGL--GERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKT 179
Cdd:COG1125 92 TVAENIATVPRLLGwdKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALDPIT 171
|
170 180
....*....|....*....|....*
gi 780224413 180 GERVIELLFELNREHGTTLVVVTHD 204
Cdd:COG1125 172 REQLQDELLRLQRELGKTIVFVTHD 196
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
20-217 |
1.35e-36 |
|
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: 129.86 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 20 QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLqlDEEGRARLRaEQVGFVFQ---- 95
Cdd:TIGR04520 12 ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTL--DEENLWEIR-KKVGMVFQnpdn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 96 -----------SFlllptlsALENVMLPaelRGETRcePRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:TIGR04520 89 qfvgatveddvAF-------GLENLGVP---REEMR--KRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVM 209
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-208 |
1.68e-36 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 131.99 E-value: 1.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEE 80
Cdd:PRK09452 9 SSLSPLVELRGISKSF----DGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 GRarlraeQVGFVFQSFLLLPTLSALENVM--LPAELRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARA 158
Cdd:PRK09452 85 NR------HVNTVFQSYALFPHMTVFENVAfgLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780224413 159 FMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELA 208
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEA 208
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
24-208 |
1.70e-36 |
|
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: 127.76 E-value: 1.70e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRarlraeQVGFVFQSFLLLPTL 103
Cdd:cd03301 14 TALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDR------DIAMVFQNYALYPHM 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRGETRCEPRARELLAA--VGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:cd03301 88 TVYDNIAFGLKLRKVPKDEIDERVREVAelLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRV 167
|
170 180
....*....|....*....|....*..
gi 780224413 182 RVIELLFELNREHGTTLVVVTHDHELA 208
Cdd:cd03301 168 QMRAELKRLQQRLGTTTIYVTHDQVEA 194
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-172 |
1.78e-36 |
|
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: 125.84 E-value: 1.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLRAEqVGFVFQSFLLLPTLSA 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDE---RKSLRKE-IGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 106 LENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPR----LSGGEQQRVAIARAFMTRPSLLLADEPT 172
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDARaeEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
4-204 |
1.82e-36 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 129.03 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIInVKGLGKtvRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRa 83
Cdd:PRK11247 11 TPLL-LNAVSK--RYGER--TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 84 rlraeqvgFVFQSFLLLPTLSALENVMLPaeLRGETRcePRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:PRK11247 85 --------LMFQDARLLPWKKVIDNVGLG--LKGQWR--DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| PhnT2 |
TIGR03265 |
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ... |
24-208 |
2.27e-36 |
|
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]
Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 131.31 E-value: 2.27e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRarlraeQVGFVFQSFLLLPTL 103
Cdd:TIGR03265 18 TALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKR------DYGIVFQSYALFPNL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:TIGR03265 92 TVADNIAYGLKNRGMGRAEVAERvaELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPLSALDARVRE 171
|
170 180
....*....|....*....|....*..
gi 780224413 182 RVIELLFELNREHGTTLVVVTHDHELA 208
Cdd:TIGR03265 172 HLRTEIRQLQRRLGVTTIMVTHDQEEA 198
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-217 |
6.19e-36 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 133.35 E-value: 6.19e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEg 81
Cdd:COG4987 329 PGGPSLELEDV--SFRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDED- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 82 raRLRAeQVGFVFQSFLLLPTlSALENVML------PAELrgetrcepraRELLAAVGLGERLHHLPP-----------R 144
Cdd:COG4987 406 --DLRR-RIAVVPQRPHLFDT-TLRENLRLarpdatDEEL----------WAALERVGLGDWLAALPDgldtwlgeggrR 471
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHgtTLVVVTHDHELAQRCQRQLVM 217
Cdd:COG4987 472 LSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVL 542
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
24-217 |
1.15e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 123.89 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlraeQVGFVFQsflllptl 103
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRR----RIGYVPQ-------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 salenvmlpaelrgetrceprarellaavglgerlhhlpprLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:cd00267 81 -----------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERL 119
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 184 IELLFELnREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd00267 120 LELLREL-AEEGRTVIIVTHDPELAELaADRVIVL 153
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
7-217 |
1.98e-35 |
|
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: 124.05 E-value: 1.98e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRlgqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlr 86
Cdd:cd03230 1 IEVRNLSKRYG----KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeqVGFVFQSFLLLPTLSALENVmlpaelrgetrceprarellaavglgerlhhlppRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03230 75 ---IGYLPEEPSLYENLTVRENL----------------------------------KLSGGMKQRLALAQALLHDPELL 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:cd03230 118 ILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAIL 168
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
7-217 |
2.49e-35 |
|
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213263 [Multi-domain] Cd Length: 239 Bit Score: 125.53 E-value: 2.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKtvRLGQesLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegrarLR 86
Cdd:cd03296 3 IEVRNVSK--RFGD--FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP------VQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 AEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEP------RARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFM 160
Cdd:cd03296 73 ERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERPPeaeiraKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 161 TRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELA-QRCQRQLVM 217
Cdd:cd03296 153 VEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVM 210
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
26-208 |
3.06e-35 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 128.27 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRArlraeqVGFVFQSFLLLPTLSA 105
Cdd:NF040840 16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRG------IAYVYQNYMLFPHKTV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELR--GETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:NF040840 90 FENIAFGLKLRkvPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDEL 169
|
170 180
....*....|....*....|....*
gi 780224413 184 IELLFELNREHGTTLVVVTHDHELA 208
Cdd:NF040840 170 IREMKRWHREFGFTAIHVTHNFEEA 194
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
25-217 |
6.50e-35 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 131.49 E-value: 6.50e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLRaEQVGFVFQSFLLLPTlS 104
Cdd:COG2274 490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR-RQIGVVLQDVFLFSG-T 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRGETrcepRARELLAAVGLGERLHHLP-----------PRLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:COG2274 565 IRENITLGDPDATDE----EIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARALLRNPRILILDEATS 640
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 780224413 174 NLDSKTGERVIELLFELNRehGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:COG2274 641 ALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVL 682
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-217 |
1.21e-34 |
|
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: 124.87 E-value: 1.21e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRaEQVGFVFQsF----LLLP 101
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLR-KKVGLVFQ-FpehqLFEE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLsaLENVM-------LPAElrgETRCepRARELLAAVGLGERLHHLPP-RLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:TIGR04521 99 TV--YKDIAfgpknlgLSEE---EAEE--RVKEALELVGLDEEYLERSPfELSGGQMRRVAIAGVLAMEPEVLILDEPTA 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 780224413 174 NLDSKTGERVIELLFELNREHGTTLVVVTHDHE-LAQRCQRQLVM 217
Cdd:TIGR04521 172 GLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEdVAEYADRVIVM 216
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
7-209 |
8.13e-34 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 122.38 E-value: 8.13e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKtvRLGQESltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSL---------LQL 77
Cdd:PRK10619 6 LNVIDLHK--RYGEHE--VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqLKV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 78 DEEGRARLRAEQVGFVFQSFLLLPTLSALENVM-LPAELRGETRCEPRAREL--LAAVGLGERLH-HLPPRLSGGEQQRV 153
Cdd:PRK10619 82 ADKNQLRLLRTRLTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVkyLAKVGIDERAQgKYPVHLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 154 AIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQ 209
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFAR 216
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-204 |
1.45e-33 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 123.30 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKT--VRLG-----QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQS 73
Cdd:COG4608 2 AMAEPLLEVRDLKKHfpVRGGlfgrtVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 74 LLQLDEEGRARLRAeQVGFVFQ----SflLLPTL---SALENVMLPAELRGETRCEPRARELLAAVGLG-ERLHHLPPRL 145
Cdd:COG4608 82 ITGLSGRELRPLRR-RMQMVFQdpyaS--LNPRMtvgDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRYPHEF 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 146 SGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:COG4608 159 SGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-217 |
2.35e-33 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 119.98 E-value: 2.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRaEQVGFVFQSFLLLPTLSA 105
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLR-RQIGMIFQDHHLLMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:PRK10908 97 YDNVAIPLIIAGASGDDIRRRvsAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGI 176
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 184 IELLFELNREhGTTLVVVTHDHEL-AQRCQRQLVM 217
Cdd:PRK10908 177 LRLFEEFNRV-GVTVLMATHDIGLiSRRSYRMLTL 210
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-217 |
3.02e-33 |
|
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: 118.31 E-value: 3.02e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegrARLRAEQVGFVFQSflllptl 103
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLS----PKELARKIAYVPQA------- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 salenvmlpaelrgetrceprarelLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:cd03214 82 -------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIEL 136
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 184 IELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03214 137 LELLRRLARERGKTVVMVLHDLNLAARyADRVILL 171
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
41-208 |
3.25e-33 |
|
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: 122.22 E-value: 3.25e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 41 LVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRArlraeqVGFVFQSFLLLPTLSALENVMLPAELRGETR 120
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRH------INMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 121 CE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTL 198
Cdd:TIGR01187 75 AEikPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154
|
170
....*....|
gi 780224413 199 VVVTHDHELA 208
Cdd:TIGR01187 155 VFVTHDQEEA 164
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
24-217 |
5.51e-33 |
|
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: 125.26 E-value: 5.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlraeQVGFVFQ-SFLLLPT 102
Cdd:COG4988 351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR----QIAWVPQnPYLFAGT 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 LsaLENVMLPAELRGETRCEprarELLAAVGLGERLHHLP-----------PRLSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:COG4988 427 I--RENLRLGRPDASDEELE----AALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLLLDEP 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 780224413 172 TGNLDSKTGERVIELLFELNREHgtTLVVVTHDHELAQRCQRQLVM 217
Cdd:COG4988 501 TAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVL 544
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
7-217 |
9.48e-33 |
|
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: 119.19 E-value: 9.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRlgqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRarlr 86
Cdd:COG4555 2 IEVENLSKKYG----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREAR---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:COG4555 74 -RQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRieELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:COG4555 153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHImQEVEALCDRVVIL 205
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
6-213 |
1.70e-32 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 118.96 E-value: 1.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQEsltiLEGIDLQVNSGETVALVGASGSGKSTLLGLLA---GLDLPSQGDIEILGQSLlqlDEEGR 82
Cdd:PRK09984 4 IIRVEKLAKTFNQHQA----LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgliTGDKSAGSHIELLGRTV---QREGR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ----ARLRAEQVGFVFQSFLLLPTLSALENVMLPAE---------LRGETRCEP-RARELLAAVGLGERLHHLPPRLSGG 148
Cdd:PRK09984 77 lardIRKSRANTGYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKqRALQALTRVGMVHFAHQRVSTLSGG 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 149 EQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQR 213
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCER 222
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
7-217 |
4.14e-32 |
|
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: 116.70 E-value: 4.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKtvRLGQesLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlr 86
Cdd:cd03265 1 IEVENLVK--KYGD--FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeqVGFVFQSFLLLPTLSALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:cd03265 75 ---IGIVFQDLSVDDELTGWENLYIHARLYGVPGAErrERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELA-QRCQRQLVM 217
Cdd:cd03265 152 VLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAII 205
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
5-217 |
4.25e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 118.19 E-value: 4.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRAR 84
Cdd:PRK13635 4 EIIRVEHI--SFRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LRaEQVGFVFQ---------------SFlllptlsALENVMLPAELRGEtrcepRARELLAAVGLGERLHHLPPRLSGGE 149
Cdd:PRK13635 79 VR-RQVGMVFQnpdnqfvgatvqddvAF-------GLENIGVPREEMVE-----RVDQALRQVGMEDFLNREPHRLSGGQ 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 150 QQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13635 146 KQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVM 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
23-217 |
1.47e-31 |
|
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: 115.22 E-value: 1.47e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 23 LTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLraeQVGFVFQSFLLLPT 102
Cdd:cd03224 13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA---GIGYVPEGRRIFPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 LSALENVMLPAELRGETRCEPRARELLAAV-GLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:cd03224 90 LTVEENLLLGAYARRRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVE 169
|
170 180 190
....*....|....*....|....*....|....*..
gi 780224413 182 RVIELLFELNREhGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03224 170 EIFEAIRELRDE-GVTILLVEQNARFALEiADRAYVL 205
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
25-208 |
1.89e-31 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 115.95 E-value: 1.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqlDEEGRARlraeqvGFVFQSFLLLPTLS 104
Cdd:PRK11248 16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV---EGPGAER------GVVFQNEGLLPWRN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRGETRCEPR--ARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGER 182
Cdd:PRK11248 87 VQDNVAFGLQLAGVEKMQRLeiAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
|
170 180
....*....|....*....|....*.
gi 780224413 183 VIELLFELNREHGTTLVVVTHDHELA 208
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEA 192
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-204 |
2.21e-31 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 120.58 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKS-TLLGLLAGLDLPS----QGDIEILGQSLLQ 76
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 77 LDEEGRARLRAEQVGFVFQSFLL-LPTLSALENVMlpAEL----RGETRCEPRAREL--LAAVGL---GERLHHLPPRLS 146
Cdd:PRK15134 81 ASEQTLRGVRGNKIAMIFQEPMVsLNPLHTLEKQL--YEVlslhRGMRREAARGEILncLDRVGIrqaAKRLTDYPHQLS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 147 GGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK15134 159 GGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-204 |
3.36e-31 |
|
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: 120.17 E-value: 3.36e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 12 LGKTVRlgqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDlPSQGDIEILGQSLLQLDEEGRARLRAE-QV 90
Cdd:COG4172 292 FRRTVG----HVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPLRRRmQV 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 91 gfVFQ----SflLLPTLSALENVM-----LPAELRGETRcEPRARELLAAVGL-GERLHHLPPRLSGGEQQRVAIARAFM 160
Cdd:COG4172 367 --VFQdpfgS--LSPRMTVGQIIAeglrvHGPGLSAAER-RARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALI 441
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 780224413 161 TRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:COG4172 442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHD 485
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-201 |
8.16e-31 |
|
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: 113.92 E-value: 8.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLgkTVRLGQesLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRA 83
Cdd:COG0410 1 MPMLEVENL--HAGYGG--IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 84 RLRaeqVGFVFQSFLLLPTLSALENVMLPAELRgetRCEPRARELLAAVG-----LGERLHHLPPRLSGGEQQRVAIARA 158
Cdd:COG0410 77 RLG---IGYVPEGRRIFPSLTVEENLLLGAYAR---RDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRA 150
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 780224413 159 FMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVV 201
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLV 192
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-210 |
1.38e-30 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 112.93 E-value: 1.38e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRArlraeqVGFVFQSFLLLPTLSALEN 108
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP------VSMLFQENNLFPHLTVAQN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 109 VML---PA-ELRGETRCepRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAF-MTRPSLLLaDEPTGNLDSKTGERV 183
Cdd:COG3840 92 IGLglrPGlKLTAEQRA--QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLvRKRPILLL-DEPFSALDPALRQEM 168
|
170 180
....*....|....*....|....*..
gi 780224413 184 IELLFELNREHGTTLVVVTHDHELAQR 210
Cdd:COG3840 169 LDLVDELCRERGLTVLMVTHDPEDAAR 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
5-217 |
2.17e-30 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 113.33 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLgkTVRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRAR 84
Cdd:PRK13548 1 AMLEARNL--SVRLGGR--TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LRA-----EQVGFVFqsflllptlSALENVMLPAELRGETRCEPRA--RELLAAVGLGERLHHLPPRLSGGEQQRVAIAR 157
Cdd:PRK13548 77 RRAvlpqhSSLSFPF---------TVEEVVAMGRAPHGLSRAEDDAlvAAALAQVDLAHLAGRDYPQLSGGEQQRVQLAR 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 780224413 158 AFM------TRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:PRK13548 148 VLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLL 214
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-203 |
2.85e-30 |
|
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: 112.87 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLgkTVRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQG-DIEILGQSLlqldeeGR 82
Cdd:COG1119 1 DPLLELRNV--TVRRGGK--TILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERR------GG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ARLRA--EQVGFVFQSFL--LLPTLSALENVM--------LPAELRGETRCepRARELLAAVGLGERLHHLPPRLSGGEQ 150
Cdd:COG1119 71 EDVWElrKRIGLVSPALQlrFPRDETVLDVVLsgffdsigLYREPTDEQRE--RARELLELLGLAHLADRPFGTLSQGEQ 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 780224413 151 QRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTH 203
Cdd:COG1119 149 RRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
29-217 |
6.71e-30 |
|
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: 110.85 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNsGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLqlDEEGRARLRAEQ--VGFVFQSFLLLPTLSAL 106
Cdd:cd03297 17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLF--DSRKKINLPPQQrkIGLVFQQYALFPHLNVR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 107 ENVM--LPAELRGETRCepRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVI 184
Cdd:cd03297 94 ENLAfgLKRKRNREDRI--SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171
|
170 180 190
....*....|....*....|....*....|....
gi 780224413 185 ELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03297 172 PELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVM 205
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
25-203 |
1.15e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.03 E-value: 1.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLRaEQVGFVFQSFLLLpTLS 104
Cdd:COG1132 355 VLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLT---LESLR-RQIGVVPQDTFLF-SGT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRGETRCEpRArelLAAVGLGERLHHLPP-----------RLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:COG1132 430 IRENIRYGRPDATDEEVE-EA---AKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIAIARALLKDPPILILDEATS 505
|
170 180 190
....*....|....*....|....*....|
gi 780224413 174 NLDSKTGERVIELLFELNRehGTTLVVVTH 203
Cdd:COG1132 506 ALDTETEALIQEALERLMK--GRTTIVIAH 533
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
2-217 |
1.53e-29 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 112.90 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPS---QGDIEILGQSLLQLD 78
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 79 EEGRARLRAEQVGFVFQSFL--LLPTLSA----LENVMLPAELRGETRCEPRAReLLAAVGLGE---RLHHLPPRLSGGE 149
Cdd:PRK09473 88 EKELNKLRAEQISMIFQDPMtsLNPYMRVgeqlMEVLMLHKGMSKAEAFEESVR-MLDAVKMPEarkRMKMYPHEFSGGM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 150 QQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:PRK09473 167 RQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVM 235
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
14-206 |
1.88e-29 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 109.49 E-value: 1.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 14 KTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLP---SQGDIEILGQSLLQLDEEGRarlraeQV 90
Cdd:COG4136 5 ENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAEQR------RI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 91 GFVFQSFLLLPTLSALENVM--LPAELRGETRCEpRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLA 168
Cdd:COG4136 79 GILFQDDLLFPHLSVGENLAfaLPPTIGRAQRRA-RVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLL 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 780224413 169 DEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHE 206
Cdd:COG4136 158 DEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
4-208 |
2.08e-29 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 113.39 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLGKTVRlGQESLtilEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRA 83
Cdd:PRK11607 17 TPLLEIRNLTKSFD-GQHAV---DDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 84 rlraeqVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMT 161
Cdd:PRK11607 93 ------INMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRvnEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAK 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 162 RPSLLLADEPTGNLDSKTGERV-IELLFELNREhGTTLVVVTHDHELA 208
Cdd:PRK11607 167 RPKLLLLDEPMGALDKKLRDRMqLEVVDILERV-GVTCVMVTHDQEEA 213
|
|
| 3a0107s01c2 |
TIGR00972 |
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ... |
26-211 |
2.91e-29 |
|
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]
Pssm-ID: 273372 [Multi-domain] Cd Length: 247 Bit Score: 110.08 E-value: 2.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTL-----LGLLAGLDLPSQGDIEILGQSLL--QLDEEgraRLRAEqVGFVFQSFL 98
Cdd:TIGR00972 17 LKNINLDIPKNQVTALIGPSGCGKSTLlrslnRMNDLVPGVRIEGKVLFDGQDIYdkKIDVV---ELRRR-VGMVFQKPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPtLSALENVMLPAELRG---ETRCEPRARELLAAVGLGE----RLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:TIGR00972 93 PFP-MSIYDNIAYGPRLHGikdKKELDEIVEESLKKAALWDevkdRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEP 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 172 TGNLDSKTGERVIELLFELNREHgtTLVVVTHDHELAQRC 211
Cdd:TIGR00972 172 TSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARI 209
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-217 |
7.30e-29 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 109.41 E-value: 7.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQ-ESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRAR 84
Cdd:COG1101 1 MLELKNLSKTFNPGTvNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LraeqVGFVFQSFLL--LPTLSALENVMLpAELRGETR---------CEPRARELLAAVGLG--ERLHHLPPRLSGGEQQ 151
Cdd:COG1101 81 Y----IGRVFQDPMMgtAPSMTIEENLAL-AYRRGKRRglrrgltkkRRELFRELLATLGLGleNRLDTKVGLLSGGQRQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 152 RVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:COG1101 156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIM 221
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-217 |
7.90e-29 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 111.33 E-value: 7.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldeeGRARLRAEQVGFVFQSFLLLPTLS 104
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDV------SRLHARDRKVGFVFQHYALFRHMT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENV-----MLPAELRGETRC-EPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSK 178
Cdd:PRK10851 91 VFDNIafgltVLPRRERPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDAQ 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 179 TGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:PRK10851 171 VRKELRRWLRQLHEELKFTSVFVTHDQEEAMEvADRVVVM 210
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
7-217 |
1.03e-28 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 106.53 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlr 86
Cdd:cd03246 1 LEVENV--SFRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGD-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeQVGFVFQSFLLLPTlSALENVmlpaelrgetrceprarellaavglgerlhhlpprLSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03246 77 --HVGYLPQDDELFSG-SIAENI-----------------------------------LSGGQRQRLGLARALYGNPRIL 118
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 780224413 167 LADEPTGNLDSKtGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03246 119 VLDEPNSHLDVE-GERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
26-217 |
1.11e-28 |
|
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: 113.15 E-value: 1.11e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlraeQVGFVFQSFLLLPTlSA 105
Cdd:TIGR02857 338 LRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD----QIAWVPQHPFLFAG-TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVML------PAELrgetrcepraRELLAAVGLGERLHHLPP-----------RLSGGEQQRVAIARAFMTRPSLLLA 168
Cdd:TIGR02857 413 AENIRLarpdasDAEI----------REALERAGLDEFVAALPQgldtpigeggaGLSGGQAQRLALARAFLRDAPLLLL 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 780224413 169 DEPTGNLDSKTGERVIELLFELNRehGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR02857 483 DEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
3-204 |
2.55e-28 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 109.28 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 3 STPIINVKGLGK--TVRLG----QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQ 76
Cdd:PRK11308 2 QQPLLQAIDLKKhyPVKRGlfkpERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 77 LDEEGRARLRaEQVGFVFQSflllPTLS---------ALE-----NVMLPAELRGEtrcepRARELLAAVGL-GERLHHL 141
Cdd:PRK11308 82 ADPEAQKLLR-QKIQIVFQN----PYGSlnprkkvgqILEeplliNTSLSAAERRE-----KALAMMAKVGLrPEHYDRY 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 142 PPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK11308 152 PHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
7-217 |
3.50e-28 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 107.51 E-value: 3.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLgkTVRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLR 86
Cdd:COG4559 2 LEAENL--SVRLGGR--TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 A-----EQVGFVFqsflllptlSALENVMLPAE--LRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAF 159
Cdd:COG4559 78 AvlpqhSSLAFPF---------TVEEVVALGRAphGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 160 -------MTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVtHDHEL-AQRCQRQLVM 217
Cdd:COG4559 149 aqlwepvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVL-HDLNLaAQYADRILLL 213
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
25-203 |
4.69e-28 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 106.54 E-value: 4.69e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLRaEQVGFVFQSFLLLPTlS 104
Cdd:cd03254 18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDIS---RKSLR-SMIGVVLQDTFLFSG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRGETRCEprarELLAAVGLGERLHHLP-----------PRLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:cd03254 93 IMENIRLGRPNATDEEVI----EAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDEATS 168
|
170 180 190
....*....|....*....|....*....|
gi 780224413 174 NLDSKTGERVIELLFELNreHGTTLVVVTH 203
Cdd:cd03254 169 NIDTETEKLIQEALEKLM--KGRTSIIIAH 196
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-217 |
8.83e-28 |
|
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: 108.26 E-value: 8.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLqlDEEGRARLRAEQ--VGFVFQSFLLLPTLSAL 106
Cdd:COG4148 18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQ--DSARGIFLPPHRrrIGYVFQEARLFPHLSVR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 107 ENvmlpaeLR-GETRCEPRAR-----ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTG 180
Cdd:COG4148 96 GN------LLyGRKRAPRAERrisfdEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
|
170 180 190
....*....|....*....|....*....|....*...
gi 780224413 181 ERVIELLFELNREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSlDEVARLADHVVLL 207
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
2-217 |
3.16e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 105.46 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGqslLQLDEEG 81
Cdd:PRK13632 3 NKSVMIKVENV--SFSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKEN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 82 RARLRaEQVGFVFQS----FLLLpTLSA-----LENVMLPaelRGETRcePRARELLAAVGLGERLHHLPPRLSGGEQQR 152
Cdd:PRK13632 78 LKEIR-KKIGIIFQNpdnqFIGA-TVEDdiafgLENKKVP---PKKMK--DIIDDLAKKVGMEDYLDKEPQNLSGGQKQR 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 153 VAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13632 151 VAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVF 215
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-213 |
3.16e-27 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 108.57 E-value: 3.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 3 STPIINVKGLGKT---VRLgqesltiLEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqlde 79
Cdd:COG1129 1 AEPLLEMRGISKSfggVKA-------LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPV----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 80 EGRARLRAEQ--VGFVFQSFLLLPTLSALENVMLPAELRG-----ETRCEPRARELLAAVGLgerlhHLPPR-----LSG 147
Cdd:COG1129 69 RFRSPRDAQAagIAIIHQELNLVPNLSVAENIFLGREPRRgglidWRAMRRRARELLARLGL-----DIDPDtpvgdLSV 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 780224413 148 GEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHD-HELAQRCQR 213
Cdd:COG1129 144 AQQQLVEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRlDEVFEIADR 209
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-208 |
6.09e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 104.77 E-value: 6.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlQLDEEGRARLRaEQVGFVFQS---FLLLPT 102
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVR-KTVGIVFQNpddQLFAPT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 LsaLENVML-PAELR-GETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTG 180
Cdd:PRK13639 96 V--EEDVAFgPLNLGlSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGA 173
|
170 180
....*....|....*....|....*...
gi 780224413 181 ERVIELLFELNREhGTTLVVVTHDHELA 208
Cdd:PRK13639 174 SQIMKLLYDLNKE-GITIIISTHDVDLV 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
16-217 |
8.26e-27 |
|
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: 105.96 E-value: 8.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 16 VRLGQESLTIlegiDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLqlDEEGRARLRAEQ--VGFV 93
Cdd:TIGR02142 7 KRLGDFSLDA----DFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFLPPEKrrIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 94 FQSFLLLPTLSALENVmlpaeLRGETRCEPRAR-----ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLA 168
Cdd:TIGR02142 81 FQEARLFPHLSVRGNL-----RYGMKRARPSERrisfeRVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLM 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780224413 169 DEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:TIGR02142 156 DEPLAALDDPRKYEILPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVL 205
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
25-204 |
8.94e-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: 107.45 E-value: 8.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLraeqVGFVFQSFLLLPTlS 104
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRR----VSVCAQDAHLFDT-T 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAElrgeTRCEPRARELLAAVGLGERLHHLPP-----------RLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:TIGR02868 425 VRENLRLARP----DATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPTE 500
|
170 180 190
....*....|....*....|....*....|.
gi 780224413 174 NLDSKTGERVIELLFELNRehGTTLVVVTHD 204
Cdd:TIGR02868 501 HLDAETADELLEDLLAALS--GRTVVLITHH 529
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
6-217 |
1.37e-26 |
|
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: 102.45 E-value: 1.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARL 85
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 raeqvGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:cd03266 81 -----GFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARleELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:cd03266 156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHImQEVERLCDRVVVL 209
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
7-206 |
2.28e-26 |
|
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: 101.50 E-value: 2.28e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQesltILEGIDLQVNSGETvALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLr 86
Cdd:cd03264 1 LQLENLTKRYGKKR----ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRI- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeqvGFVFQSFLLLPTLSALENVMLPAELRG--ETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPS 164
Cdd:cd03264 75 ----GYLPQEFGVYPNFTVREFLDYIAWLKGipSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 165 LLLADEPTGNLDSKTGERVIELLFELNREHgtTLVVVTHDHE 206
Cdd:cd03264 151 ILIVDEPTAGLDPEERIRFRNLLSELGEDR--IVILSTHIVE 190
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
21-217 |
3.01e-26 |
|
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: 101.18 E-value: 3.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 21 ESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldeegRARLRAEQVGFVFQ-SFLL 99
Cdd:cd03226 11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI-------KAKERRKSIGYVMQdVDYQ 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 100 LPTLSALENVMLPAELRGETrcEPRARELLAAVGLgERLHHLPPR-LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSK 178
Cdd:cd03226 84 LFTDSVREELLLGLKELDAG--NEQAETVLKDLDL-YALKERHPLsLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160
|
170 180 190
....*....|....*....|....*....|....*....
gi 780224413 179 TGERVIELLFELNREhGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03226 161 NMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLL 198
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
2-203 |
4.13e-26 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 102.04 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLgkTVRLGQEslTILEGIDLQVNSGETVALVGASGSGKST----------LLgllagldlPSQ---GDIE 68
Cdd:COG1117 7 TLEPKIEVRNL--NVYYGDK--QALKDINLDIPENKVTALIGPSGCGKSTllrclnrmndLI--------PGArveGEIL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 69 ILGQSLLQLDEEgRARLRAeQVGFVFQSflllPT---LSALENVMLPAELRGETR---CEPRARELLAAVGLGE----RL 138
Cdd:COG1117 75 LDGEDIYDPDVD-VVELRR-RVGMVFQK----PNpfpKSIYDNVAYGLRLHGIKSkseLDEIVEESLRKAALWDevkdRL 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 139 HHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHgtTLVVVTH 203
Cdd:COG1117 149 KKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTH 211
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-216 |
4.18e-26 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 101.03 E-value: 4.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 30 DLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRArlraeqVGFVFQSFLLLPTLSALENV 109
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP------VSMLFQENNLFAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 110 MLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELL 187
Cdd:cd03298 92 GLGLSPGLKLTAEDRQAieVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
|
170 180
....*....|....*....|....*....
gi 780224413 188 FELNREHGTTLVVVTHDHELAQRCQRQLV 216
Cdd:cd03298 172 LDLHAETKMTVLMVTHQPEDAKRLAQRVV 200
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
20-217 |
6.41e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 102.09 E-value: 6.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 20 QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGqsLLQLDEEGRARLRaEQVGFVFQS--F 97
Cdd:PRK13633 20 STEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENLWDIR-NKAGMVFQNpdN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 98 LLLPTLSAlENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNL 175
Cdd:PRK13633 97 QIVATIVE-EDVAFGPENLGIPPEEIRERvdESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAML 175
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 176 DSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13633 176 DPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVM 217
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
14-210 |
1.20e-25 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 100.76 E-value: 1.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 14 KTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAG-----LDLPSQGDIEILGQSLLQLD-EEGRARlra 87
Cdd:PRK14247 7 RDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRlielyPEARVSGEVYLDGQDIFKMDvIELRRR--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 88 eqVGFVFQSFLLLPTLSALENVMLPAEL----RGETRCEPRARELLAAVGLGE----RLHHLPPRLSGGEQQRVAIARAF 159
Cdd:PRK14247 84 --VQMVFQIPNPIPNLSIFENVALGLKLnrlvKSKKELQERVRWALEKAQLWDevkdRLDAPAGKLSGGQQQRLCIARAL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 780224413 160 MTRPSLLLADEPTGNLDSKTGERVIELLFELNREhgTTLVVVTHDHELAQR 210
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAAR 210
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
24-204 |
1.89e-25 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 102.11 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQ-----SLLQLDeegrarlraeqVGFVFQSFL 98
Cdd:PRK11432 20 TVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEdvthrSIQQRD-----------ICMVFQSYA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSALENVMLPAELRGETRCEPRAR--ELLAAV---GLGERLhhlPPRLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:PRK11432 89 LFPHMSLGENVGYGLKMLGVPKEERKQRvkEALELVdlaGFEDRY---VDQISGGQQQRVALARALILKPKVLLFDEPLS 165
|
170 180 190
....*....|....*....|....*....|.
gi 780224413 174 NLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK11432 166 NLDANLRRSMREKIRELQQQFNITSLYVTHD 196
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
10-210 |
2.11e-25 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 102.80 E-value: 2.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 10 KGLGKTVRLGQESLTI-LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRAE 88
Cdd:PRK10070 27 QGLSKEQILEKTGLSLgVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 89 QVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAREL--LAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:PRK10070 107 KIAMVFQSFALMPHMTVLDNTAFGMELAGINAEERREKALdaLRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDIL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR 210
Cdd:PRK10070 187 LMDEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMR 230
|
|
| SapF |
COG4167 |
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms]; |
4-204 |
6.31e-25 |
|
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 99.14 E-value: 6.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLGKTVR-----LGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqld 78
Cdd:COG4167 2 SALLEVRNLSKTFKyrtglFRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKL---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 79 EEGRARLRAEQVGFVFQ--SFLLLPTLsaleNV--MLPAELRGETRCEPRAREL-----LAAVGL-GERLHHLPPRLSGG 148
Cdd:COG4167 78 EYGDYKYRCKHIRMIFQdpNTSLNPRL----NIgqILEEPLRLNTDLTAEEREErifatLRLVGLlPEHANFYPHMLSSG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 149 EQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:COG4167 154 QKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
14-203 |
7.51e-25 |
|
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: 97.24 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 14 KTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLA--GLDLPSQGDIEILGQSLlqldeeGRARLRAeQVG 91
Cdd:cd03213 13 VKSSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPL------DKRSFRK-IIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 92 FVFQSFLLLPTLSALENVMLPAELRGetrceprarellaavglgerlhhlpprLSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKLRG---------------------------LSGGERKRVSIALELVSNPSLLFLDEP 138
|
170 180 190
....*....|....*....|....*....|..
gi 780224413 172 TGNLDSKTGERVIELLFELnREHGTTLVVVTH 203
Cdd:cd03213 139 TSGLDSSSALQVMSLLRRL-ADTGRTIICSIH 169
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
6-217 |
9.42e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 98.65 E-value: 9.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLtilEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARL 85
Cdd:PRK13647 4 IIEVEDLHFRYKDGTKAL---KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGR---EVNAENEKWV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RAeQVGFVFQSflllP-----TLSALENVML-PAELR-GETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARA 158
Cdd:PRK13647 78 RS-KVGLVFQD----PddqvfSSTVWDDVAFgPVNMGlDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGV 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 159 FMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13647 153 LAMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIV 210
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-217 |
9.49e-25 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 98.46 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKT--VRLGqesltiLEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQS----- 73
Cdd:PRK11701 1 MMDQPLLSVRGLTKLygPRKG------CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDgqlrd 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 74 LLQLDEEGRARLRAEQVGFVFQSFL--LLPTLSALENV----M-LPAELRGETRCEprARELLAAVGLG-ERLHHLPPRL 145
Cdd:PRK11701 75 LYALSEAERRRLLRTEWGFVHQHPRdgLRMQVSAGGNIgerlMaVGARHYGDIRAT--AGDWLERVEIDaARIDDLPTTF 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 146 SGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQ-RCQRQLVM 217
Cdd:PRK11701 153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARlLAHRLLVM 225
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
21-217 |
1.19e-24 |
|
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: 97.79 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 21 ESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllqLDEEGRARLRAeQVGFVF-QSFLL 99
Cdd:cd03267 32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLR-RIGVVFgQKTQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 100 LPTLSALENVMLPAELRG--ETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDS 177
Cdd:cd03267 107 WWDLPVIDSFYLLAAIYDlpPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDV 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 780224413 178 KTGERVIELLFELNREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:cd03267 187 VAQENIRNFLKEYNRERGTTVLLTSHYmKDIEALARRVLVI 227
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-210 |
1.21e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 97.99 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQ-----GDIEILGQSLLQLDEEGrARLRaEQVGFVFQSFLL 99
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNEearveGEVRLFGRNIYSPDVDP-IEVR-REVGMVFQYPNP 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 100 LPTLSALENVMLPAEL----RGETRCEPRARELLAAVGLGE----RLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:PRK14267 97 FPHLTIYDNVAIGVKLnglvKSKKELDERVEWALKKAALWDevkdRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 780224413 172 TGNLDSKTGERVIELLFELNREHgtTLVVVTHDHELAQR 210
Cdd:PRK14267 177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAAR 213
|
|
| nickel_nikD |
TIGR02770 |
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ... |
28-216 |
1.46e-24 |
|
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a multisubunit nickel import ABC transporter complex. Nickel, once imported, may be used in urease and in certain classes of hydrogenase and superoxide dismutase. NikD and NikE are homologous. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 131817 [Multi-domain] Cd Length: 230 Bit Score: 97.44 E-value: 1.46e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 28 GIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLP----SQGDIEILGQSLLQLdeegraRLRAEQVGFVFQSFL--LLP 101
Cdd:TIGR02770 4 DLNLSLKRGEVLALVGESGSGKSLTCLAILGLLPPgltqTSGEILLDGRPLLPL------SIRGRHIATIMQNPRtaFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLSALENVMLPAELRGETRCEPRAR--ELLAAVGL--GERLHHLPP-RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:TIGR02770 78 LFTMGNHAIETLRSLGKLSKQARALilEALEAVGLpdPEEVLKKYPfQLSGGMLQRVMIALALLLEPPFLIADEPTTDLD 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 177 SKTGERVIELLFELNREHGTTLVVVTHD--------HELAQRCQRQLV 216
Cdd:TIGR02770 158 VVNQARVLKLLRELRQLFGTGILLITHDlgvvariaDEVAVMDDGRIV 205
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
22-217 |
1.86e-24 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 99.01 E-value: 1.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 22 SLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRAEqVGFVFQSflllp 101
Cdd:PRK15079 33 TLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSD-IQMIFQD----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLSALENVMLPAELRGE---------TRCE--PRARELLAAVGLGERL-HHLPPRLSGGEQQRVAIARAFMTRPSLLLAD 169
Cdd:PRK15079 107 PLASLNPRMTIGEIIAEplrtyhpklSRQEvkDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARALILEPKLIICD 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 780224413 170 EPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:PRK15079 187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVM 235
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
29-210 |
3.63e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 97.40 E-value: 3.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIlGQSLLQ--LDEEGRARLRaEQVGFVFQsfllLPTLSAL 106
Cdd:PRK13634 26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTI-GERVITagKKNKKLKPLR-KKVGIVFQ----FPEHQLF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 107 ENVMLPAELRG-------ETRCEPRARELLAAVGLGER-LHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSK 178
Cdd:PRK13634 100 EETVEKDICFGpmnfgvsEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190
....*....|....*....|....*....|..
gi 780224413 179 TGERVIELLFELNREHGTTLVVVTHDHELAQR 210
Cdd:PRK13634 180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-217 |
3.65e-24 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 98.28 E-value: 3.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKS-TLLGLLAGLDLPSQGDIEIL---GQSLLQLDEEGRARLRAEQVGFVFQSFL--LLPT 102
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPGRVMAEKLefnGQDLQRISEKERRNLVGAEVAMIFQDPMtsLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 LSALENVMLPAEL-RGETRCEPRAR--ELLAAVGL---GERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PRK11022 106 YTVGFQIMEAIKVhQGGNKKTRRQRaiDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALD 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 177 SKTGERVIELLFELNREHGTTLVVVTHDHEL-AQRCQRQLVM 217
Cdd:PRK11022 186 VTIQAQIIELLLELQQKENMALVLITHDLALvAEAAHKIIVM 227
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-179 |
3.79e-24 |
|
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: 96.07 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLraeQVGFVFQSFLLLPTL 103
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL---GIGYLPQEASIFRKL 90
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 104 SALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKT 179
Cdd:cd03218 91 TVEENILAVLEIRGLSKKEREEKleELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIA 168
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-217 |
4.35e-24 |
|
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: 95.65 E-value: 4.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 9 VKGLGKTvrLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLqldeEGRARLRAE 88
Cdd:cd03263 3 IRNLTKT--YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIR----TDRKAARQS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 89 qVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03263 77 -LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEveLLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELNRehGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03263 156 LLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEAlCDRIAIM 205
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
1-204 |
4.81e-24 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.56 E-value: 4.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINV-KGLGKTVrlgqesltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDE 79
Cdd:PRK11000 1 MASVTLRNVtKAYGDVV--------ISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 80 EGRArlraeqVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRARELLAA--VGLGERLHHLPPRLSGGEQQRVAIAR 157
Cdd:PRK11000 73 AERG------VGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAevLQLAHLLDRKPKALSGGQRQRVAIGR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780224413 158 AFMTRPSLLLADEPTGNLDSktGERViELLFELNREH---GTTLVVVTHD 204
Cdd:PRK11000 147 TLVAEPSVFLLDEPLSNLDA--ALRV-QMRIEISRLHkrlGRTMIYVTHD 193
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
5-217 |
5.00e-24 |
|
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P lyase systems for utilization of phosphonates. These systems resemble phosphonatase-based systems in having a three component ABC transporter, where TIGR01097 is the permease, TIGR01098 is the phosphonates binding protein, and TIGR02315 is the ATP-binding cassette (ABC) protein. They differ, however, in having, typically, ten or more additional genes, many of which are believed to form a membrane-associated complex. This protein (PhnK) and the adjacent-encoded PhnL resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this complex rather than part of a transporter per se. [Central intermediary metabolism, Phosphorus compounds]
Pssm-ID: 188208 [Multi-domain] Cd Length: 253 Bit Score: 96.44 E-value: 5.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLGKTVRLGQEsltiLEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQS-----LLQLDE 79
Cdd:TIGR02323 2 PLLQVSGLSKSYGGGKG----CRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 80 EGRARLRAEQVGFVFQSFL--LLPTLSALENV---MLPAELRGETRCEPRARELLAAVGLGE-RLHHLPPRLSGGEQQRV 153
Cdd:TIGR02323 78 AERRRLMRTEWGFVHQNPRdgLRMRVSAGANIgerLMAIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRL 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 154 AIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQ-RCQRQLVM 217
Cdd:TIGR02323 158 QIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARlLAQRLLVM 222
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
7-213 |
9.88e-24 |
|
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: 94.59 E-value: 9.88e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQesltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgrarlr 86
Cdd:cd03268 1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 AEQVGFVFQSFLLLPTLSALENVMLPAELRGetRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03268 71 LRRIGALIEAPGFYPNLTARENLRLLARLLG--IRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLL 148
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHD-HELAQRCQR 213
Cdd:cd03268 149 ILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLlSEIQKVADR 195
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
2-207 |
1.18e-23 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 95.44 E-value: 1.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLgkTVRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEG 81
Cdd:PRK11300 1 MSQPLLSVSGL--MMRFG--GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 82 RARLraeqvGFV--FQSFLLLPTLSALENVML-----------------PAELRGETRCEPRARELLAAVGLGERLHHLP 142
Cdd:PRK11300 77 IARM-----GVVrtFQHVRLFREMTVIENLLVaqhqqlktglfsgllktPAFRRAESEALDRAATWLERVGLLEHANRQA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 143 PRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHEL 207
Cdd:PRK11300 152 GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKL 216
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
25-203 |
1.80e-23 |
|
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.
Pssm-ID: 213216 [Multi-domain] Cd Length: 238 Bit Score: 94.53 E-value: 1.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegrARLRAEQVGFVFQSFLLLPTlS 104
Cdd:cd03249 18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLN----LRWLRSQIGLVSQEPVLFDG-T 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRGETRCEPRARELLAA---VGLGERLH-HLPPR---LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDS 177
Cdd:cd03249 93 IAENIRYGKPDATDEEVEEAAKKANIHdfiMSLPDGYDtLVGERgsqLSGGQKQRIAIARALLRNPKILLLDEATSALDA 172
|
170 180
....*....|....*....|....*.
gi 780224413 178 KTGERVIELLFELNRehGTTLVVVTH 203
Cdd:cd03249 173 ESEKLVQEALDRAMK--GRTTIVIAH 196
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
24-217 |
1.94e-23 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 98.34 E-value: 1.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTllgllagldlpsqgdieiLGQSLLQL--DEEGR-ARLRAEQVGFVFQ-SFLL 99
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKST------------------LLRAIAGLwpYGSGRiARPAGARVLFLPQrPYLP 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 100 LPTLsaLENVMLPAELRGETrcEPRARELLAAVGLGerlhHLPPR----------LSGGEQQRVAIARAFMTRPSLLLAD 169
Cdd:COG4178 439 LGTL--REALLYPATAEAFS--DAELREALEAVGLG----HLAERldeeadwdqvLSLGEQQRLAFARLLLHKPDWLFLD 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 170 EPTGNLDSKTGERVIELLfeLNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:COG4178 511 EATSALDEENEAALYQLL--REELPGTTVISVGHRSTLAAFHDRVLEL 556
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-217 |
1.99e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 95.67 E-value: 1.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSL-LQLDEEGRARLRaEQVGFVFQsfllLPTLS 104
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItPETGNKNLKKLR-KKVSLVFQ----FPEAQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRG-------ETRCEPRARELLAAVGLGERL-HHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PRK13641 98 LFENTVLKDVEFGpknfgfsEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 177 SKTGERVIELLFELNREhGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKA-GHTVILVTHNmDDVAEYADDVLVL 218
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-204 |
2.02e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 97.83 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIlgqsllqldeegRARLRaeqVGFVFQSFLLLPTL 103
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI------------PKGLR---IGYLPQEPPLDDDL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVM--------LPAELRG------------------ETRC--------EPRARELLAAVGLGERLHHLPPR-LSGG 148
Cdd:COG0488 77 TVLDTVLdgdaelraLEAELEEleaklaepdedlerlaelQEEFealggweaEARAEEILSGLGFPEEDLDRPVSeLSGG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 780224413 149 EQQRVAIARAFMTRPSLLLADEPTGNLDSKTgervIELLFE-LNREHGtTLVVVTHD 204
Cdd:COG0488 157 WRRRVALARALLSEPDLLLLDEPTNHLDLES----IEWLEEfLKNYPG-TVLVVSHD 208
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
15-200 |
3.05e-23 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 93.83 E-value: 3.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSL--LQLDEegrarLRaEQVGF 92
Cdd:cd03251 7 TFRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVrdYTLAS-----LR-RQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 93 VFQ-SFLLLPTLSalENVMLPAelRGETRCEprARELLAAVGLGERLHHLPP-----------RLSGGEQQRVAIARAFM 160
Cdd:cd03251 81 VSQdVFLFNDTVA--ENIAYGR--PGATREE--VEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 161 TRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVV 200
Cdd:cd03251 155 KDPPILILDEATSALDTESERLVQAALERL-MKNRTTFVI 193
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
6-217 |
4.72e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.41 E-value: 4.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQESLTiLEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARL 85
Cdd:PRK13650 4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 RaEQVGFVFQS---FLLLPTLS-----ALENVMLPAELRGEtrcepRARELLAAVGLGERLHHLPPRLSGGEQQRVAIAR 157
Cdd:PRK13650 80 R-HKIGMVFQNpdnQFVGATVEddvafGLENKGIPHEEMKE-----RVNEALELVGMQDFKEREPARLSGGQKQRVAIAG 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 158 AFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13650 154 AVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVM 213
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
30-217 |
8.34e-23 |
|
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: 92.23 E-value: 8.34e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 30 DLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRArlraeqVGFVFQSFLLLPTLSALENV 109
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP------VSMLFQENNLFAHLTVRQNI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 110 MLPAE--LRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELL 187
Cdd:TIGR01277 92 GLGLHpgLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
|
170 180 190
....*....|....*....|....*....|
gi 780224413 188 FELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR01277 172 KQLCSERQRTLLMVTHHLSDARAIASQIAV 201
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
24-217 |
8.37e-23 |
|
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: 92.60 E-value: 8.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQ--SLLQLdeegrarlraeQVGFvfqsfllLP 101
Cdd:cd03220 36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvsSLLGL-----------GGGF-------NP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLhHLPPR-LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSK 178
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKEIDEKidEIIEFSELGDFI-DLPVKtYSSGMKARLAFAIATALEPDILLIDEVLAVGDAA 176
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 179 TGERVIELLFELnREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03220 177 FQEKCQRRLREL-LKQGKTVILVSHDPSSIKRlCDRALVL 215
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
5-217 |
9.37e-23 |
|
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in methanogenesis, methyl coenzyme M reductase, contains alpha, beta, and gamma chains. In older literature, the complex of alpha, beta, and gamma chains was termed component C, while this single chain protein was termed methyl coenzyme M reductase system component A2. [Energy metabolism, Methanogenesis]
Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 96.02 E-value: 9.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLGKT-VRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEI-LGQSLLQLDEEG- 81
Cdd:TIGR03269 278 PIIKVRNVSKRyISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrVGDEWVDMTKPGp 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 82 RARLRAEQ-VGFVFQSFLLLPTLSALENVM------LPAELrgetrCEPRARELLAAVGLGER-----LHHLPPRLSGGE 149
Cdd:TIGR03269 358 DGRGRAKRyIGILHQEYDLYPHRTVLDNLTeaigleLPDEL-----ARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGE 432
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 150 QQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDvCDRAALM 501
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
7-204 |
1.11e-22 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.00 E-value: 1.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVRLGQES-LTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIL------------GQS 73
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIfkdeknkkktkeKEK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 74 LLQLDEEGRARLRA--------EQVGFVFQsF----LLLPTLsaLENVMLPAELRGETRCEP--RARELLAAVGLGER-L 138
Cdd:PRK13651 83 VLEKLVIQKTRFKKikkikeirRRVGVVFQ-FaeyqLFEQTI--EKDIIFGPVSMGVSKEEAkkRAAKYIELVGLDESyL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 139 HHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHD 204
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHD 224
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
26-217 |
2.36e-22 |
|
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: 91.11 E-value: 2.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLRAeQVGFVFQ-SFLLLPTLS 104
Cdd:cd03245 20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLD---PADLRR-NIGYVPQdVTLFYGTLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 alENVMLPAELRGEtrcepraRELLAAV---GLGE--RLHhlpPR------------LSGGEQQRVAIARAFMTRPSLLL 167
Cdd:cd03245 96 --DNITLGAPLADD-------ERILRAAelaGVTDfvNKH---PNgldlqigergrgLSGGQRQAVALARALLNDPPILL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780224413 168 ADEPTGNLDSKTGERVIELLFELNRehGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03245 164 LDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLDLVDRIIVM 211
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
25-210 |
2.50e-22 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 93.75 E-value: 2.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRarlraeQVGFVFQSFLLLPTLS 104
Cdd:PRK11650 19 VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADR------DIAMVFQNYALYPHMS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRGETRCEPRARELLAA--VGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTgeR 182
Cdd:PRK11650 93 VRENMAYGLKIRGMPKAEIEERVAEAAriLELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKL--R 170
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 183 V---IELLfELNREHGTTLVVVTHDH----ELAQR 210
Cdd:PRK11650 171 VqmrLEIQ-RLHRRLKTTSLYVTHDQveamTLADR 204
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
26-203 |
3.05e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 92.11 E-value: 3.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRAEQVGFVFQ---SFLLLPT 102
Cdd:PRK13649 23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpeSQLFEET 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 LsaLENVMLPAELRG--ETRCEPRARELLAAVGLGERLHHLPP-RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKt 179
Cdd:PRK13649 103 V--LKDVAFGPQNFGvsQEEAEALAREKLALVGISESLFEKNPfELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK- 179
|
170 180
....*....|....*....|....
gi 780224413 180 GERVIELLFELNREHGTTLVVVTH 203
Cdd:PRK13649 180 GRKELMTLFKKLHQSGMTIVLVTH 203
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
24-203 |
3.11e-22 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 94.73 E-value: 3.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLdlpSQGDIEILGQSLLQldeeGRARLRAEQ---VGFVFQSFLLL 100
Cdd:TIGR00955 39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFR---SPKGVKGSGSVLLN----GMPIDAKEMraiSAYVQQDDLFI 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 101 PTLSALENVMLPAELR---GETRCEPRAR--ELLAAVGLGERLHHL---PPR---LSGGEQQRVAIARAFMTRPSLLLAD 169
Cdd:TIGR00955 112 PTLTVREHLMFQAHLRmprRVTKKEKRERvdEVLQALGLRKCANTRigvPGRvkgLSGGERKRLAFASELLTDPPLLFCD 191
|
170 180 190
....*....|....*....|....*....|....
gi 780224413 170 EPTGNLDSKTGERVIELLFELNrEHGTTLVVVTH 203
Cdd:TIGR00955 192 EPTSGLDSFMAYSVVQVLKGLA-QKGKTIICTIH 224
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
19-203 |
4.16e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 89.29 E-value: 4.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 19 GQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgrarlRAEQVGFVFQSFL 98
Cdd:cd03247 11 PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----LSSLISVLNQRPY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTlSALENvmlpaelrgetrceprarellaavgLGErlhhlppRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSK 178
Cdd:cd03247 86 LFDT-TLRNN-------------------------LGR-------RFSGGERQRLALARILLQDAPIVLLDEPTVGLDPI 132
|
170 180
....*....|....*....|....*
gi 780224413 179 TGERVIELLFELNREHgtTLVVVTH 203
Cdd:cd03247 133 TERQLLSLIFEVLKDK--TLIWITH 155
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
1-204 |
5.30e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 91.36 E-value: 5.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLgkTVRLGQESltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDee 80
Cdd:PRK11831 2 QSVANLVDMRGV--SFTRGNRC--IFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMS-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 gRARLRA--EQVGFVFQSFLLLPTLSALENVMLPaeLRGETRC-EPRAREL----LAAVGLGERLHHLPPRLSGGEQQRV 153
Cdd:PRK11831 76 -RSRLYTvrKRMSMLFQSGALFTDMNVFDNVAYP--LREHTQLpAPLLHSTvmmkLEAVGLRGAAKLMPSELSGGMARRA 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 780224413 154 AIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK11831 153 ALARAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHD 203
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
24-217 |
5.49e-22 |
|
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: 90.03 E-value: 5.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARLraeqvGFVFQSFLLLPTL 103
Cdd:cd03269 14 TALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAARNRI-----GYLPEERGLYPKM 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:cd03269 86 KVIDQLVYLAQLKGLKKEEarRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVE 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 780224413 182 RVIELLFELnREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:cd03269 166 LLKDVIREL-ARAGKTVILSTHQMELVEElCDRVLLL 201
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
7-203 |
6.59e-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: 93.71 E-value: 6.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLL--AGLDLPSQGDI----------------E 68
Cdd:TIGR03269 1 IEVKNLTKKF----DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLrgMDQYEPTSGRIiyhvalcekcgyverpS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 69 ILGQS--------------LLQLDEEGRARLRaEQVGFVFQ-SFLLLPTLSALENVM--LP-AELRGETRCEpRARELLA 130
Cdd:TIGR03269 77 KVGEPcpvcggtlepeevdFWNLSDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLeaLEeIGYEGKEAVG-RAVDLIE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 131 AVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTH 203
Cdd:TIGR03269 155 MVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
25-203 |
1.03e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 89.98 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGrarLRaEQVGFVFQSFLLLPT-- 102
Cdd:cd03253 16 VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDS---LR-RAIGVVPQDTVLFNDti 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 --------LSA----LENVMLPAELRGETRCEPRARELLaavgLGER-LhhlppRLSGGEQQRVAIARAFMTRPSLLLAD 169
Cdd:cd03253 92 gynirygrPDAtdeeVIEAAKAAQIHDKIMRFPDGYDTI----VGERgL-----KLSGGEKQRVAIARAILKNPPILLLD 162
|
170 180 190
....*....|....*....|....*....|....
gi 780224413 170 EPTGNLDSKTGERVIELLFELNRehGTTLVVVTH 203
Cdd:cd03253 163 EATSALDTHTEREIQAALRDVSK--GRTTIVIAH 194
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
19-217 |
1.15e-21 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 88.44 E-value: 1.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 19 GQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIeilgqsllqldeegrARLRAEQVGFVFQSFL 98
Cdd:NF040873 1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------------RRAGGARVAYVPQRSE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTL--SALENVML----PAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADE 170
Cdd:NF040873 66 VPDSLplTVRDLVAMgrwaRRGLWRRLTRDDRAAvdDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 780224413 171 PTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-217 |
1.19e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 90.88 E-value: 1.19e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLqlDEEGRARLRAEQVGFVFQsfllLPTLSA 105
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDIT--DKKVKLSDIRKKVGLVFQ----YPEYQL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVML------PAEL-RGETRCEPRARELLAAVGLG-ERLHHLPP-RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PRK13637 97 FEETIEkdiafgPINLgLSEEEIENRVKRAMNIVGLDyEDYKDKSPfELSGGQKRRVAIAGVVAMEPKILILDEPTAGLD 176
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 177 SKTGERVIELLFELNREHGTTLVVVTHDHE-LAQRCQRQLVM 217
Cdd:PRK13637 177 PKGRDEILNKIKELHKEYNMTIILVSHSMEdVAKLADRIIVM 218
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-204 |
1.49e-21 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.00 E-value: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEE 80
Cdd:PRK10247 2 QENSPLLQLQNVGYLA----GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 graRLRaEQVGFVFQSflllPTL---SALENVMLPAELRGETRCEPRARELLAAVGLGERLHHLP-PRLSGGEQQRVAIA 156
Cdd:PRK10247 78 ---IYR-QQVSYCAQT----PTLfgdTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNiAELSGGEKQRISLI 149
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 157 RAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK10247 150 RNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
24-217 |
2.04e-21 |
|
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: 88.74 E-value: 2.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLraeQVGFVFQSFLLLPTL 103
Cdd:TIGR03410 14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARA---GIAYVPQGREIFPRL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRG--ETRCEPRARELLAAvgLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPT-GNLDS--K 178
Cdd:TIGR03410 91 TVEENLLTGLAALPrrSRKIPDEIYELFPV--LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTeGIQPSiiK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 179 TGERVIEllfELNREHGTTLVVVTHDHELAQRC-QRQLVM 217
Cdd:TIGR03410 169 DIGRVIR---RLRAEGGMAILLVEQYLDFARELaDRYYVM 205
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
25-211 |
2.60e-21 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 88.99 E-value: 2.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPsqGDIEILGQSLLQLDEEGRARLRAEQVGFVFQ----SFLLL 100
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPA--GVRQTAGRVLLDGKPVAPCALRGRKIATIMQnprsAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 101 PTLSALENVMLPAelRGETRCEPRARELLAAVGLGER---LHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDS 177
Cdd:PRK10418 96 HTMHTHARETCLA--LGKPADDATLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDV 173
|
170 180 190
....*....|....*....|....*....|....
gi 780224413 178 KTGERVIELLFELNREHGTTLVVVTHDHELAQRC 211
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDMGVVARL 207
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
20-203 |
2.65e-21 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 92.20 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 20 QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEegrARLRAeQVGFVFQS-FL 98
Cdd:PRK11160 350 DQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSE---AALRQ-AISVVSQRvHL 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSalENVMLPAElrgeTRCEPRARELLAAVGLGERLHHLPP----------RLSGGEQQRVAIARAFMTRPSLLLA 168
Cdd:PRK11160 426 FSATLR--DNLLLAAP----NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARALLHDAPLLLL 499
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 169 DEPTGNLDSKTGERVIELLFELNRehGTTLVVVTH 203
Cdd:PRK11160 500 DEPTEGLDAETERQILELLAEHAQ--NKTVLMITH 532
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
24-217 |
3.06e-21 |
|
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: 86.71 E-value: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldeEGRARLRAEQ--VGFVFQsflllp 101
Cdd:cd03216 14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEV-----SFASPRDARRagIAMVYQ------ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 tlsalenvmlpaelrgetrceprarellaavglgerlhhlpprLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:cd03216 83 -------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTPAEVE 119
|
170 180 190
....*....|....*....|....*....|....*..
gi 780224413 182 RVIELLFELnREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:cd03216 120 RLFKVIRRL-RAQGVAVIFISHRlDEVFEIADRVTVL 155
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
24-176 |
3.71e-21 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 88.49 E-value: 3.71e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLraeQVGFVFQSFLLLPTL 103
Cdd:TIGR04406 15 KVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPMHERARL---GIGYLPQEASIFRKL 91
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 104 SALENVMLPAELRGE---TRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:TIGR04406 92 TVEENIMAVLEIRKDldrAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDEPFAGVD 167
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
2-204 |
4.47e-21 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 91.31 E-value: 4.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKTVRLGQESL-------TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDlPSQGDIEILGQSL 74
Cdd:PRK15134 271 PASPLLDVEQLQVAFPIRKGILkrtvdhnVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPL 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 75 LQLDEEGRARLRaEQVGFVFQ--SFLLLPTLSALE------NVMLPaELRGETRcEPRARELLAAVGLG-ERLHHLPPRL 145
Cdd:PRK15134 350 HNLNRRQLLPVR-HRIQVVFQdpNSSLNPRLNVLQiieeglRVHQP-TLSAAQR-EQQVIAVMEEVGLDpETRHRYPAEF 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 146 SGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK15134 427 SGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
25-217 |
1.37e-20 |
|
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: 89.81 E-value: 1.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLraeqVGFVFQSFLLLP-TL 103
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELFDgTI 422
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SalENV-MLPaelrgetrcEPRARELLAA---VGLGERLHHLP-----------PRLSGGEQQRVAIARAFMTRPSLLLA 168
Cdd:COG4618 423 A--ENIaRFG---------DADPEKVVAAaklAGVHEMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPRLVVL 491
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780224413 169 DEPTGNLDSkTGER-VIELLFELnREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:COG4618 492 DEPNSNLDD-EGEAaLAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVL 539
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-210 |
1.90e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 89.35 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIlGQSLlqldeegrar 84
Cdd:COG0488 314 KVLELEGLSKSY----GDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------- 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 lraeQVGFVFQSFLLL-PTLSALENVmlpAELRGETRcEPRARELLAAVGL-GERLHHLPPRLSGGEQQRVAIARAFMTR 162
Cdd:COG0488 379 ----KIGYFDQHQEELdPDKTVLDEL---RDGAPGGT-EQEVRGYLGRFLFsGDDAFKPVGVLSGGEKARLALAKLLLSP 450
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780224413 163 PSLLLADEPTGNLDSKTGERVIELL--FElnrehGtTLVVVTHDHELAQR 210
Cdd:COG0488 451 PNVLLLDEPTNHLDIETLEALEEALddFP-----G-TVLLVSHDRYFLDR 494
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-204 |
2.28e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 87.11 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKglgkTVRL---GQESLTiLEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGdiEILGQSLLqL 77
Cdd:PRK13648 2 EDKNSIIVFK----NVSFqyqSDASFT-LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSG--EIFYNNQA-I 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 78 DEEGRARLRaEQVGFVFQ--------SFLLLPTLSALENVMLPAElrgetRCEPRARELLAAVGLGERLHHLPPRLSGGE 149
Cdd:PRK13648 74 TDDNFEKLR-KHIGIVFQnpdnqfvgSIVKYDVAFGLENHAVPYD-----EMHRRVSEALKQVDMLERADYEPNALSGGQ 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 150 QQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK13648 148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHD 202
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
26-217 |
2.65e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.21 E-value: 2.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlQLDEEGRARLRaEQVGFVFQS-FLLLPTLS 104
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLR-ESVGMVFQDpDNQLFSAS 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALE-------NVMLPaelrgETRCEPRARELLAAVGLgERLHHLPPR-LSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PRK13636 100 VYQdvsfgavNLKLP-----EDEVRKRVDNALKRTGI-EHLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLD 173
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 177 SKTGERVIELLFELNREHGTTLVVVTHDHEL-AQRCQRQLVM 217
Cdd:PRK13636 174 PMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVM 215
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
15-217 |
3.55e-20 |
|
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: 85.62 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLRAeQVGFVF 94
Cdd:cd03252 7 RFRYKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALAD---PAWLRR-QVGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 95 QSFLLLpTLSALENVMLPAELRGETRCEPRARelLAavGLGERLHHLP-----------PRLSGGEQQRVAIARAFMTRP 163
Cdd:cd03252 83 QENVLF-NRSIRDNIALADPGMSMERVIEAAK--LA--GAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNP 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNRehGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03252 158 RILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVM 209
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
4-217 |
3.71e-20 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 85.90 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 4 TPIINVKGLGKTVRLGQESL------------------TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQG 65
Cdd:COG1134 2 SSMIEVENVSKSYRLYHEPSrslkelllrrrrtrreefWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 66 DIEILGQ--SLLQLdeegrarlraeQVGFVfqsflllPTLSALENVMLPAELRGETRCEPRARelLAAV----GLGERLh 139
Cdd:COG1134 82 RVEVNGRvsALLEL-----------GAGFH-------PELTGRENIYLNGRLLGLSRKEIDEK--FDEIvefaELGDFI- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 140 HLPPR-LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:COG1134 141 DQPVKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRlCDRAIWL 219
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
15-217 |
3.72e-20 |
|
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 88.62 E-value: 3.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLRAeQVGFVF 94
Cdd:TIGR02203 337 TFRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYT---LASLRR-QVALVS 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 95 QSFLLLPTLSAlENVmlpAELRGETRCEPRARELLAAVGLGERLHHLP-----------PRLSGGEQQRVAIARAFMTRP 163
Cdd:TIGR02203 413 QDVVLFNDTIA-NNI---AYGRTEQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIARALLKDA 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 164 SLLLADEPTGNLDSKTgERVIELLFELNREHGTTLVVVthdHELA--QRCQRQLVM 217
Cdd:TIGR02203 489 PILILDEATSALDNES-ERLVQAALERLMQGRTTLVIA---HRLStiEKADRIVVM 540
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
5-171 |
4.19e-20 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 85.47 E-value: 4.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLGKTVRlgqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRAR 84
Cdd:COG1137 2 MTLEAENLVKSYG----KRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRAR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LraeQVGF------VFQSflllptLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIA 156
Cdd:COG1137 78 L---GIGYlpqeasIFRK------LTVEDNILAVLELRKLSKKEREERleELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
|
170
....*....|....*
gi 780224413 157 RAFMTRPSLLLADEP 171
Cdd:COG1137 149 RALATNPKFILLDEP 163
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-210 |
4.49e-20 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 85.87 E-value: 4.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEI------LGQSLLQLDEegrARLRAEqVGFVFQSFL 98
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyFGKDIFQIDA---IKLRKE-VGMVFQQPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSALENVMLPAELRG---ETRCEPRARELLAAVGLG----ERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:PRK14246 101 PFPHLSIYDNIAYPLKSHGikeKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 780224413 172 TGNLDSKTGERVIELLFELNREhgTTLVVVTHDHELAQR 210
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVAR 217
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
25-217 |
5.32e-20 |
|
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: 88.26 E-value: 5.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRARLRA-----EQVGFVFqsfll 99
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDID---RHTLRQfinylPQEPYIF----- 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 100 lpTLSALENVMLPAElRGETRcepraRELLAAV--------------GLGERLHHLPPRLSGGEQQRVAIARAFMTRPSL 165
Cdd:TIGR01193 561 --SGSILENLLLGAK-ENVSQ-----DEIWAACeiaeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTDSKV 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 780224413 166 LLADEPTGNLDSKTGERVIELLFELNREhgtTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR01193 633 LILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVL 681
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
7-211 |
5.88e-20 |
|
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: 82.88 E-value: 5.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTllgllagldlpsqgdieilgqsLLQLdeegrarlr 86
Cdd:cd03221 1 IELENLSKTY----GGKLLLKDISLTINPGDRIGLVGRNGAGKST----------------------LLKL--------- 45
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeqvgfvfqsflllptlsaLENVMLPAElrGETRceprarellaaVGLGERLHHLPpRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03221 46 -------------------IAGELEPDE--GIVT-----------WGSTVKIGYFE-QLSGGEKMRLALAKLLLENPNLL 92
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 780224413 167 LADEPTGNLDSKTGERVIELLfelnREHGTTLVVVTHDHELAQRC 211
Cdd:cd03221 93 LLDEPTNHLDLESIEALEEAL----KEYPGTVILVSHDRYFLDQV 133
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
26-217 |
9.32e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 85.42 E-value: 9.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGqsllqLDEEGRARLRA--EQVGFVFQS----FLL 99
Cdd:PRK13644 18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG-----IDTGDFSKLQGirKLVGIVFQNpetqFVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 100 LPTLSAL----ENVMLPAelrgeTRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNL 175
Cdd:PRK13644 93 RTVEEDLafgpENLCLPP-----IEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 176 DSKTGERVIELLFELNREhGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEK-GKTIVYITHNLEELHDADRIIVM 208
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
5-204 |
1.30e-19 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 84.70 E-value: 1.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLGktvrLGQESLTILEGIDLQVNSGETVALVGASGSGKST-----LLGLLAGLDLPSQGDIEILGQSLLqlde 79
Cdd:PRK14258 6 PAIKVNNLS----FYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkclNRMNELESEVRVEGRVEFFNQNIY---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 80 EGRA---RLRaEQVGFVFQSFLLLPtLSALENVML---------PAELRGETRCEPRARELLAAVGlgERLHHLPPRLSG 147
Cdd:PRK14258 78 ERRVnlnRLR-RQVSMVHPKPNLFP-MSVYDNVAYgvkivgwrpKLEIDDIVESALKDADLWDEIK--HKIHKSALDLSG 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 780224413 148 GEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK14258 154 GQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
26-217 |
1.53e-19 |
|
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: 82.87 E-value: 1.53e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRaeqVGFV---FQSFLLLPT 102
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAG---IAYVpedRKREGLVLD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 LSALENVMLPAelrgetrceprarellaavglgerlhhlppRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGER 182
Cdd:cd03215 93 LSVAENIALSS------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 183 VIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03215 143 IYRLIRELADAGKAVLLISSELDELLGLCDRILVM 177
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
1-204 |
2.11e-19 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 84.55 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKTVRLGQeslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldee 80
Cdd:PRK15056 1 MMQQAGIVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPT------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 gRARLRAEQVGFVFQSFLL---LPTLsaLENVMLPAEL-------RGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQ 150
Cdd:PRK15056 72 -RQALQKNLVAYVPQSEEVdwsFPVL--VEDVVMMGRYghmgwlrRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQK 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 780224413 151 QRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHD 204
Cdd:PRK15056 149 KRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHN 201
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-217 |
2.76e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 85.99 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEG 81
Cdd:PRK09700 1 MATPYISMAGIGKSF----GPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 82 RARLraeQVGFVFQSFLLLPTLSALENVM---LP------------AELRgetrcePRARELLAAVGLGERLHHLPPRLS 146
Cdd:PRK09700 77 AAQL---GIGIIYQELSVIDELTVLENLYigrHLtkkvcgvniidwREMR------VRAAMMLLRVGLKVDLDEKVANLS 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 780224413 147 GGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:PRK09700 148 ISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKlAEIRRICDRYTVM 218
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
25-217 |
3.20e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 84.08 E-value: 3.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGD---IEILGqslLQLDEEGRARLRaEQVGFVFQS---FL 98
Cdd:PRK13640 22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDG---ITLTAKTVWDIR-EKVGIVFQNpdnQF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSalENVMLPAELRGETRCEPR--ARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PRK13640 98 VGATVG--DDVAFGLENRAVPRPEMIkiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 780224413 177 SKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13640 176 PAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVL 216
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-217 |
3.47e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 84.00 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKtvRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARl 85
Cdd:COG4152 1 MLELKGLTK--RFG--DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGE---PLDPEDRRR- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 raeqVGFvfqsfL-----LLPTLSALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARA 158
Cdd:COG4152 73 ----IGY-----LpeergLYPKMKVGEQLVYLARLKGLSKAEakRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 159 FMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQR-CQRqLVM 217
Cdd:COG4152 144 LLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEElCDR-IVI 201
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
29-217 |
3.49e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.05 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDlPSQGDIEILGQSLLQLDEegrARLRaEQVGFVFQSFLLL-PTLsaLE 107
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDP---ESWR-KHLSWVGQNPQLPhGTL--RD 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 108 NVMLPAELRGETRceprARELLAAVGLGERLHHLPP-----------RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PRK11174 442 NVLLGNPDASDEQ----LQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLD 517
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 780224413 177 SKTGERVIELLFELNRehGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK11174 518 AHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVM 556
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
23-203 |
4.17e-19 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 82.02 E-value: 4.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 23 LTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgrarlRAEQVGFVFQSFLLLPT 102
Cdd:TIGR01189 13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-----PHENILYLGHLPGLKPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 LSALENVMLPAELRGETRCEPraRELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDsKTGER 182
Cdd:TIGR01189 88 LSALENLHFWAAIHGGAQRTI--EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-KAGVA 164
|
170 180
....*....|....*....|.
gi 780224413 183 VIELLFELNREHGTTLVVVTH 203
Cdd:TIGR01189 165 LLAGLLRAHLARGGIVLLTTH 185
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-210 |
5.17e-19 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 82.90 E-value: 5.17e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 3 STPIINVKGLgkTVRLGQESltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGL--DLPS---QGDIEILGQSLLQL 77
Cdd:PRK14239 2 TEPILQVSDL--SVYYNKKK--ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNIYSP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 78 DEEgRARLRAEqVGFVFQSFLLLPtLSALENVMLPAELRG----ETRCEPRARELLAAVGLGE---RLHHLPPRLSGGEQ 150
Cdd:PRK14239 78 RTD-TVDLRKE-IGMVFQQPNPFP-MSIYENVVYGLRLKGikdkQVLDEAVEKSLKGASIWDEvkdRLHDSALGLSGGQQ 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 151 QRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHgtTLVVVTHDHELAQR 210
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASR 212
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
20-217 |
5.43e-19 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 84.19 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 20 QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQ---------GDIEilgqsLLQLDEEGRARLRAEQV 90
Cdd:COG4170 17 QGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWhvtadrfrwNGID-----LLKLSPRERRKIIGREI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 91 GFVFQ--SFLLLPTLSA---LENVMLPAELRG------ETRCEpRARELLAAVGLGERLHHL---PPRLSGGEQQRVAIA 156
Cdd:COG4170 92 AMIFQepSSCLDPSAKIgdqLIEAIPSWTFKGkwwqrfKWRKK-RAIELLHRVGIKDHKDIMnsyPHELTEGECQKVMIA 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 780224413 157 RAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHE-LAQRCQRQLVM 217
Cdd:COG4170 171 MAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLEsISQWADTITVL 232
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-200 |
8.46e-19 |
|
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: 84.87 E-value: 8.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEegrARLRAeQVGFVFQsflllptl 103
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQ---ASLRA-AIGIVPQ-------- 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 salENVMLPAELR--------GETRCEPRARELLAAVG-------------LGER-LhhlppRLSGGEQQRVAIARAFMT 161
Cdd:COG5265 440 ---DTVLFNDTIAyniaygrpDASEEEVEAAARAAQIHdfieslpdgydtrVGERgL-----KLSGGEKQRVAIARTLLK 511
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 162 RPSLLLADEPTGNLDSKTgERVI-ELLFELNREHgTTLVV 200
Cdd:COG5265 512 NPPILIFDEATSALDSRT-ERAIqAALREVARGR-TTLVI 549
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-203 |
8.55e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 84.69 E-value: 8.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKtvRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSlLQLDEEG 81
Cdd:COG3845 1 MMPPALELRGITK--RFG--GVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKP-VRIRSPR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 82 RArlRAEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPR-ARELLAAvgLGERLH-HLPP-----RLSGGEQQRVA 154
Cdd:COG3845 76 DA--IALGIGMVHQHFMLVPNLTVAENIVLGLEPTKGGRLDRKaARARIRE--LSERYGlDVDPdakveDLSVGEQQRVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 780224413 155 IARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTH 203
Cdd:COG3845 152 ILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITH 199
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
25-201 |
1.18e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 81.55 E-value: 1.18e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDlpsQGDIEILGQSLLqldeEGRARLRAE---QVGFVFQSFLLLP 101
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGQILF----NGQPRKPDQfqkCVAYVRQDDILLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLSALENVMLPAELRGETRCEPRARELLAAVGLGERLHHLPPR------LSGGEQQRVAIARAFMTRPSLLLADEPTGNL 175
Cdd:cd03234 95 GLTVRETLTYTAILRLPRKSSDAIRKKRVEDVLLRDLALTRIGgnlvkgISGGERRRVSIAVQLLWDPKVLILDEPTSGL 174
|
170 180
....*....|....*....|....*.
gi 780224413 176 DSKTGERVIELLFELNREHGTTLVVV 201
Cdd:cd03234 175 DSFTALNLVSTLSQLARRNRIVILTI 200
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-203 |
1.29e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 82.47 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRAEQVGFVFQsfllLPTLSALEN 108
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQ----FPESQLFEE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 109 VMLPAELRG-------ETRCEPRARELLAAVGLGERLHHLPP-RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTG 180
Cdd:PRK13643 101 TVLKDVAFGpqnfgipKEKAEKIAAEKLEMVGLADEFWEKSPfELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
|
170 180
....*....|....*....|...
gi 780224413 181 ERVIElLFELNREHGTTLVVVTH 203
Cdd:PRK13643 181 IEMMQ-LFESIHQSGQTVVLVTH 202
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
16-207 |
1.43e-18 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 81.16 E-value: 1.43e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 16 VRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTllgllagldlpsqgdieiLGQSLLqldeeGRARLRAEQVGFVFQ 95
Cdd:COG2401 36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKST------------------LLRLLA-----GALKGTPVAGCVDVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 96 SFLLLPTLSALENVMLPAELrgetrcePRARELLAAVGLGERLHHL--PPRLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:COG2401 93 DNQFGREASLIDAIGRKGDF-------KDAVELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|....
gi 780224413 174 NLDSKTGERVIELLFELNREHGTTLVVVTHDHEL 207
Cdd:COG2401 166 HLDRQTAKRVARNLQKLARRAGITLVVATHHYDV 199
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-217 |
1.49e-18 |
|
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: 83.94 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlraeQVGFVFQSFLLLPTL 103
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGK----HIGYLPQDVELFPGT 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SAlENVMlpaelRGETRCEPRA-RELLAAVGLGERLHHLP--------PR---LSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:TIGR01842 408 VA-ENIA-----RFGENADPEKiIEAAKLAGVHELILRLPdgydtvigPGgatLSGGQRQRIALARALYGDPKLVVLDEP 481
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 780224413 172 TGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR01842 482 NSNLDEEGEQALANAIKAL-KARGITVVVITHRPSLLGCVDKILVL 526
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
27-208 |
2.13e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 80.23 E-value: 2.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 27 EGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgrarlraeqvgfvFQSFLLL------ 100
Cdd:PRK13538 18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDE-------------YHQDLLYlghqpg 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 101 --PTLSALENVMLPAELRGETRcEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDsK 178
Cdd:PRK13538 85 ikTELTALENLRFYQRLHGPGD-DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID-K 162
|
170 180 190
....*....|....*....|....*....|
gi 780224413 179 TGERVIELLFELNREHGTTLVVVTHdHELA 208
Cdd:PRK13538 163 QGVARLEALLAQHAEQGGMVILTTH-QDLP 191
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
26-203 |
2.51e-18 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 83.47 E-value: 2.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLdeeGRARLRaEQVGFVFQSFLLLpTLSA 105
Cdd:PRK13657 351 VEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTV---TRASLR-RNIAVVFQDAGLF-NRSI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVML------PAELRgetrcepRARELLAAVGL------------GERlhhlPPRLSGGEQQRVAIARAFMTRPSLLL 167
Cdd:PRK13657 426 EDNIRVgrpdatDEEMR-------AAAERAQAHDFierkpdgydtvvGER----GRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190
....*....|....*....|....*....|....*.
gi 780224413 168 ADEPTGNLDSKTGERVIELLFELNreHGTTLVVVTH 203
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALDELM--KGRTTFIIAH 528
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
6-216 |
2.96e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 82.06 E-value: 2.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKT--VRLGQESL-------------TI--LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIE 68
Cdd:COG4586 1 IIEVENLSKTyrVYEKEPGLkgalkglfrreyrEVeaVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 69 ILGqsllqLD--EEGRARLRaeQVGFVF----QsflLLPTLSALENVMLPAELRG--ETRCEPRARELLAAVGLGERLHH 140
Cdd:COG4586 81 VLG-----YVpfKRRKEFAR--RIGVVFgqrsQ---LWWDLPAIDSFRLLKAIYRipDAEYKKRLDELVELLDLGELLDT 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 141 lPPR-LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD-HELAQRCQRQLV 216
Cdd:COG4586 151 -PVRqLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDmDDIEALCDRVIV 227
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-210 |
2.99e-18 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 80.40 E-value: 2.99e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 30 DLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRArlraeqVGFVFQSFLLLPTLSALENV 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP------VSMLFQENNLFSHLTVAQNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 110 ML---PA-ELRGETRCepRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIE 185
Cdd:PRK10771 93 GLglnPGlKLNAAQRE--KLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170
|
170 180
....*....|....*....|....*
gi 780224413 186 LLFELNREHGTTLVVVTHDHELAQR 210
Cdd:PRK10771 171 LVSQVCQERQLTLLMVSHSLEDAAR 195
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
6-202 |
5.65e-18 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 80.22 E-value: 5.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVR-----LGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldEE 80
Cdd:PRK15112 4 LLEVRNLSKTFRyrtgwFRRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL----HF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 GRARLRAEQVGFVFQ--SFLLLPTLSALENVMLPaeLRGETRCEPRARE-----LLAAVGL-GERLHHLPPRLSGGEQQR 152
Cdd:PRK15112 80 GDYSYRSQRIRMIFQdpSTSLNPRQRISQILDFP--LRLNTDLEPEQREkqiieTLRQVGLlPDHASYYPHMLAPGQKQR 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 780224413 153 VAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVT 202
Cdd:PRK15112 158 LGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVT 207
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
25-208 |
7.10e-18 |
|
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: 78.72 E-value: 7.10e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLL--AGLDLPSQGDIEILGQSLLQLDEEGRARLraeQVGFVFQSflllpt 102
Cdd:cd03217 15 ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEERARL---GIFLAFQY------ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 lsalenvmlPAELRGETrceprARELLAAVGLGerlhhlpprLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGER 182
Cdd:cd03217 86 ---------PPEIPGVK-----NADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
|
170 180
....*....|....*....|....*.
gi 780224413 183 VIELLFELnREHGTTLVVVTHDHELA 208
Cdd:cd03217 143 VAEVINKL-REEGKSVLIITHYQRLL 167
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-217 |
8.54e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 80.14 E-value: 8.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARLRaEQVGFVFQS----FLllp 101
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNLR-RKIGMVFQNpdnqFV--- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLSALENVMLPAELRGETRCE--PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKT 179
Cdd:PRK13642 96 GATVEDDVAFGMENQGIPREEmiKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 780224413 180 GERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVM 213
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-217 |
1.11e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 80.23 E-value: 1.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 3 STPIINVKGLGKtvRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldeEGR 82
Cdd:PRK13537 4 SVAPIDFRNVEK--RYGDK--LVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPV-----PSR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ARLRAEQVGFVFQSFLLLPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFM 160
Cdd:PRK13537 75 ARHARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALvpPLLEFAKLENKADAKVGELSGGMKRRLTLARALV 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 161 TRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:PRK13537 155 NDPDVLVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERlCDRLCVI 211
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
17-203 |
1.24e-17 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 80.69 E-value: 1.24e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 17 RLGQESLTIlegiDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIeILGQSLLqLDEEGRARLRAEQ--VGFVF 94
Cdd:PRK11144 9 QLGDLCLTV----NLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRI-VLNGRVL-FDAEKGICLPPEKrrIGYVF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 95 QSFLLLPTLSALENvmlpaeLRGETRCEPRAR-----ELLaavGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLAD 169
Cdd:PRK11144 83 QDARLFPHYKVRGN------LRYGMAKSMVAQfdkivALL---GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMD 153
|
170 180 190
....*....|....*....|....*....|....
gi 780224413 170 EPTGNLDSKTGERVIELLFELNREHGTTLVVVTH 203
Cdd:PRK11144 154 EPLASLDLPRKRELLPYLERLAREINIPILYVSH 187
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-217 |
1.54e-17 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 80.87 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEe 80
Cdd:PRK15439 6 TTAPPLLCARSISKQY----SGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 grarLRAEQVG--FVFQSFLLLPTLSALENVM--LPAELRGETRCEprarELLAAVGLGERLHHLPPRLSGGEQQRVAIA 156
Cdd:PRK15439 81 ----AKAHQLGiyLVPQEPLLFPNLSVKENILfgLPKRQASMQKMK----QLLAALGCQLDLDSSAGSLEVADRQIVEIL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 780224413 157 RAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:PRK15439 153 RGLMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKlPEIRQLADRISVM 213
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
5-210 |
1.69e-17 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 80.66 E-value: 1.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLgkTVRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegrAR 84
Cdd:PRK09536 2 PMIDVSDL--SVEFG--DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALS----AR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LRAEQVGFVFQSFLLLPTLSALENVML---PAELR--GETRCEPRA-RELLAAVGLGERLHHLPPRLSGGEQQRVAIARA 158
Cdd:PRK09536 74 AASRRVASVPQDTSLSFEFDVRQVVEMgrtPHRSRfdTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARA 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 780224413 159 FMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQR 210
Cdd:PRK09536 154 LAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAAR 204
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
25-217 |
2.23e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.92 E-value: 2.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlraeQVGFVFQSFLLLpTLS 104
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHR----QVALVGQEPVLF-SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVmlpaeLRGETRCEprARELLAAV--------------GLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADE 170
Cdd:TIGR00958 571 VRENI-----AYGLTDTP--DEEIMAAAkaanahdfimefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDE 643
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 780224413 171 PTGNLDSktgeRVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR00958 644 ATSALDA----ECEQLLQESRSRASRTVLLIAHRLSTVERADQILVL 686
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
24-216 |
3.01e-17 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 78.29 E-value: 3.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlraeQVGFVFQSfllLPTL 103
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR----KVAYLPQQ---LPAA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELR-------GETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGN 174
Cdd:PRK10575 98 EGMTVRELVAIGRypwhgalGRFGAADREKveEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 175 LDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLV 216
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLV 219
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-217 |
5.01e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 77.90 E-value: 5.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRAEQVGFVFQsfllLPTLSA 105
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIRPVRKRIGMVFQ----FPESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LE------------NVMLPAElrgetRCEPRARELLAAVGLGERLHHLPP-RLSGGEQQRVAIARAFMTRPSLLLADEPT 172
Cdd:PRK13646 99 FEdtvereiifgpkNFKMNLD-----EVKNYAHRLLMDLGFSRDVMSQSPfQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 780224413 173 GNLDSKTGERVIELLFELNREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVM 219
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
26-217 |
7.31e-17 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 79.13 E-value: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRAEqVGFVFQSFL--LLPTL 103
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRD-IQFIFQDPYasLDPRQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRGETRCEPRAR---ELLAAVGL-GERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKT 179
Cdd:PRK10261 419 TVGDSIMEPLRVHGLLPGKAAAArvaWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSI 498
|
170 180 190
....*....|....*....|....*....|....*....
gi 780224413 180 GERVIELLFELNREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:PRK10261 499 RGQIINLLLDLQRDFGIAYLFISHDMAVVERiSHRVAVM 537
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-217 |
8.02e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.07 E-value: 8.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGqsllqldEEGRARLRAEQVGFVFQSFLLLPTL 103
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDG-------GDIDDPDVAEACHYLGHRNAMKPAL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRGETrcEPRARELLAAVGLGeRLHHLPPR-LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGER 182
Cdd:PRK13539 89 TVAENLEFWAAFLGGE--ELDIAAALEAVGLA-PLAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVAL 165
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 183 VIELLFElNREHGTTLVVVTHdHELAQRCQRQLVM 217
Cdd:PRK13539 166 FAELIRA-HLAQGGIVIAATH-IPLGLPGARELDL 198
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
25-203 |
1.13e-16 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 78.61 E-value: 1.13e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLdeeGRARLRaEQVGFVFQSFLLLPTlS 104
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSL---SHSVLR-QGVAMVQQDPVVLAD-T 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRgetrcEPRARELLAAVGLGERLHHLPP-----------RLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:PRK10790 431 FLANVTLGRDIS-----EEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190
....*....|....*....|....*....|
gi 780224413 174 NLDSKTgERVIELLFELNREHgTTLVVVTH 203
Cdd:PRK10790 506 NIDSGT-EQAIQQALAAVREH-TTLVVIAH 533
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
24-217 |
1.15e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 76.47 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlraEQVGFVFQSFLLLPTL 103
Cdd:PRK10895 17 RVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARAR---RGIGYLPQEASIFRRL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLPAELRGETRCEP---RARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTG 180
Cdd:PRK10895 94 SVYDNLMAVLQIRDDLSAEQredRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 780224413 181 ---ERVIELLfelnREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:PRK10895 174 idiKRIIEHL----RDSGLGVLITDHNvRETLAVCERAYIV 210
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
26-203 |
2.14e-16 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 77.66 E-value: 2.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTlLGLLAGLDLPS---QGDIEILGQSLlqldeegRAR-LR-AEQVGFV--FQSFL 98
Cdd:PRK13549 21 LDNVSLKVRAGEIVSLCGENGAGKST-LMKVLSGVYPHgtyEGEIIFEGEEL-------QASnIRdTERAGIAiiHQELA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSALENVMLPAELRGETRCE-----PRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:PRK13549 93 LVKELSVLENIFLGNEITPGGIMDydamyLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190
....*....|....*....|....*....|
gi 780224413 174 NLDSKTGERVIELLFELnREHGTTLVVVTH 203
Cdd:PRK13549 173 SLTESETAVLLDIIRDL-KAHGIACIYISH 201
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
13-212 |
3.23e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 3.23e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 13 GKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlraeQVGF 92
Cdd:PRK10253 10 GEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR----RIGL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 93 VFQSFLLLPTLSALENVM------LPAELRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:PRK10253 86 LAQNATTPGDITVQELVArgryphQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIM 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDheLAQRCQ 212
Cdd:PRK10253 166 LLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHD--LNQACR 209
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
18-210 |
5.89e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 75.13 E-value: 5.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 18 LGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQG-----DIEILGQSLLQLDEEGRARLRaeqVGF 92
Cdd:PRK14271 29 LGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVLEFRRR---VGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 93 VFQSFLLLPtLSALENVMLPAEL-----RGETRCEPRARelLAAVGL----GERLHHLPPRLSGGEQQRVAIARAFMTRP 163
Cdd:PRK14271 106 LFQRPNPFP-MSIMDNVLAGVRAhklvpRKEFRGVAQAR--LTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNP 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNREhgTTLVVVTHDHELAQR 210
Cdd:PRK14271 183 EVLLLDEPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAAR 227
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
23-217 |
7.66e-16 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 73.30 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 23 LTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgrarlRAEQVGFVFQSFLLLPT 102
Cdd:cd03231 13 RALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-----IARGLLYLGHAPGIKTT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 LSALENVMLPAELRGETRCEprarELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDsKTGER 182
Cdd:cd03231 88 LSVLENLRFWHADHSDEQVE----EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD-KAGVA 162
|
170 180 190
....*....|....*....|....*....|....*.
gi 780224413 183 VIELLFELNREHGTTLVVVTH-DHELAQRCQRQLVM 217
Cdd:cd03231 163 RFAEAMAGHCARGGMVVLTTHqDLGLSEAGARELDL 198
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-176 |
1.56e-15 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 73.34 E-value: 1.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTlLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRA------EQVGF--VFQsF 97
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKST-LLARMAGLLPGQGEILLNGRPLSDWSAAELARHRAylsqqqSPPFAmpVFQ-Y 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 98 LllpTLSalenvmLPAELRGETrCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMT-------RPSLLLADE 170
Cdd:COG4138 90 L---ALH------QPAGASSEA-VEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDE 159
|
....*.
gi 780224413 171 PTGNLD 176
Cdd:COG4138 160 PMNSLD 165
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-217 |
1.60e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.89 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIeILGQ-----SLLQLDEEGRARlraEQVGFVFQ--SFL 98
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQT-IVGDyaipaNLKKIKEVKRLR---KEIGLVFQfpEYQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSALENVMLPAELrGETRCE--PRARELLAAVGLGERLHHLPP-RLSGGEQQRVAIARAFMTRPSLLLADEPTGNL 175
Cdd:PRK13645 103 LFQETIEKDIAFGPVNL-GENKQEayKKVPELLKLVQLPEDYVKRSPfELSGGQKRRVALAGIIAMDGNTLVLDEPTGGL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 176 DSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13645 182 DPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIV 223
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
5-213 |
2.13e-15 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 2.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLgkTVRLGqeSLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRAR 84
Cdd:NF033858 265 PAIEARGL--TMRFG--DFTAVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRR 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 lraeqVGFVFQSFLLLPTLSALENVMLPAELRG--ETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTR 162
Cdd:NF033858 341 -----VGYMSQAFSLYGELTVRQNLELHARLFHlpAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 780224413 163 PSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQR 213
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEAERCDR 466
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
26-203 |
2.27e-15 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 74.83 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLagldlpS--------QGDIEILGqsllqldEEGRAR-LRA-EQVGFVF- 94
Cdd:NF040905 17 LDDVNLSVREGEIHALCGENGAGKSTLMKVL------SgvyphgsyEGEILFDG-------EVCRFKdIRDsEALGIVIi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 95 -QSFLLLPTLSALENVMLPAEL--RG-----ETRcePRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:NF040905 84 hQELALIPYLSIAENIFLGNERakRGvidwnETN--RRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLL 161
|
170 180 190
....*....|....*....|....*....|....*..
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTH 203
Cdd:NF040905 162 ILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISH 197
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
26-201 |
3.14e-15 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 72.22 E-value: 3.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEegrARLRAEQVGFVFQSFLLLPTLSA 105
Cdd:PRK11614 21 LHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQT---AKIMREAVAIVPEGRRVFSRMTV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRGETRCEPRARELLAAVG-LGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVI 184
Cdd:PRK11614 98 EENLAMGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIF 177
|
170
....*....|....*..
gi 780224413 185 ELLFELnREHGTTLVVV 201
Cdd:PRK11614 178 DTIEQL-REQGMTIFLV 193
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
22-207 |
5.20e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 72.53 E-value: 5.20e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 22 SLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARLRaEQVGFVFQS---FL 98
Cdd:PRK13652 16 SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGE---PITKENIREVR-KFVGLVFQNpddQI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSAlENVMLPAEL-RGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDS 177
Cdd:PRK13652 92 FSPTVEQ-DIAFGPINLgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170
|
170 180 190
....*....|....*....|....*....|
gi 780224413 178 KTGERVIELLFELNREHGTTLVVVTHDHEL 207
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDL 200
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
25-217 |
5.40e-15 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 72.94 E-value: 5.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSllqldEEGRARLRAEQVGFVFQSFLLLPTLS 104
Cdd:PRK13536 56 VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVP-----VPARARLARARIGVVPQFDNLDLEFT 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAE-LRGETR-CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGER 182
Cdd:PRK13536 131 VRENLLVFGRyFGMSTReIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210
|
170 180 190
....*....|....*....|....*....|....*.
gi 780224413 183 VIELLFELnREHGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:PRK13536 211 IWERLRSL-LARGKTILLTTHFMEEAERlCDRLCVL 245
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
15-203 |
6.29e-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: 70.99 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLdeeGRARLRaEQVGFVF 94
Cdd:cd03244 9 SLRYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKI---GLHDLR-SRISIIP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 95 QSFLLLP-TL----------------SALENVMLpaelrgetrcepraRELLAAV--GLGERLHHLPPRLSGGEQQRVAI 155
Cdd:cd03244 85 QDPVLFSgTIrsnldpfgeysdeelwQALERVGL--------------KEFVESLpgGLDTVVEEGGENLSVGQRQLLCL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 156 ARAFMTRPSLLLADEPTGNLDSKTGERVIELLFElnREHGTTLVVVTH 203
Cdd:cd03244 151 ARALLRKSKILVLDEATASVDPETDALIQKTIRE--AFKDCTVLTIAH 196
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
21-206 |
7.26e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 72.58 E-value: 7.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 21 ESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEI----LGQSLLQLDEEGRA---------RLRa 87
Cdd:PRK13631 37 NELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHELITNPyskkiknfkELR- 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 88 EQVGFVFQ--SFLLLPTlSALENVML-PAELrGETRCEPR--ARELLAAVGLGER-LHHLPPRLSGGEQQRVAIARAFMT 161
Cdd:PRK13631 116 RRVSMVFQfpEYQLFKD-TIEKDIMFgPVAL-GVKKSEAKklAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAI 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 780224413 162 RPSLLLADEPTGNLDSKtGERVIELLFELNREHGTTLVVVTHDHE 206
Cdd:PRK13631 194 QPEILIFDEPTAGLDPK-GEHEMMQLILDAKANNKTVFVITHTME 237
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-217 |
7.32e-15 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 72.53 E-value: 7.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKS---------TLLGLLAGLDLPSQGDIEilgqsLL 75
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSliakaicgvTKDNWRVTADRMRFDDID-----LL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 76 QLDEEGRARLRAEQVGFVFQ--SFLLLPTLSALENVM--LPA---------ELRGETRcepRARELLAAVGLGER---LH 139
Cdd:PRK15093 77 RLSPRERRKLVGHNVSMIFQepQSCLDPSERVGRQLMqnIPGwtykgrwwqRFGWRKR---RAIELLHRVGIKDHkdaMR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 140 HLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:PRK15093 154 SFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKINVL 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
6-203 |
8.53e-15 |
|
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: 72.94 E-value: 8.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIL--GQSLlqldeEGRA 83
Cdd:TIGR02633 1 LLEMKGIVKTF----GGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTWDGEIYwsGSPL-----KASN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 84 RLRAEQVGFVF--QSFLLLPTLSALENVMLPAE--LRGETRCEP----RARELLAAVGLGERLHHLP-PRLSGGEQQRVA 154
Cdd:TIGR02633 72 IRDTERAGIVIihQELTLVPELSVAENIFLGNEitLPGGRMAYNamylRAKNLLRELQLDADNVTRPvGDYGGGQQQLVE 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 780224413 155 IARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNReHGTTLVVVTH 203
Cdd:TIGR02633 152 IAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISH 199
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-217 |
9.89e-15 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.97 E-value: 9.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLgkTVRLGQESLTI--LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILG------- 71
Cdd:PRK10261 7 LDARDVLAVENL--NIAFMQEQQKIaaVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrs 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 72 QSLLQLDEEGRA---RLRAEQVGFVFQSFL--LLPTLSALENVMLPAELR---GETRCEPRARELLAAVGLGER---LHH 140
Cdd:PRK10261 85 RQVIELSEQSAAqmrHVRGADMAMIFQEPMtsLNPVFTVGEQIAESIRLHqgaSREEAMVEAKRMLDQVRIPEAqtiLSR 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 141 LPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHE-LAQRCQRQLVM 217
Cdd:PRK10261 165 YPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVM 242
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
25-217 |
1.37e-14 |
|
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: 70.58 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEegraRLRAEQVGFVFQSflllPTLS 104
Cdd:cd03248 29 VLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEH----KYLHSKVSLVGQE----PVLF 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 A---LENVMLpaelrGETRCE-PRARELLAAVGLGERLHHLP-----------PRLSGGEQQRVAIARAFMTRPSLLLAD 169
Cdd:cd03248 101 ArslQDNIAY-----GLQSCSfECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 780224413 170 EPTGNLDSKTGERVIELLFELNREHgtTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERR--TVLVIAHRLSTVERADQILVL 221
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-210 |
2.72e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 70.20 E-value: 2.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLG--LLAGLDLPS---QGDIEILGQSLLQLD---EEGRARlraeqVGFVFQSF 97
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfNRLNDLIPGfrvEGKVTFHGKNLYAPDvdpVEVRRR-----IGMVFQKP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 98 LLLPTlSALENVMLPAELRGET--RCEPRARELLAAVGLGE---RLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPT 172
Cdd:PRK14243 101 NPFPK-SIYDNIAYGARINGYKgdMDELVERSLRQAALWDEvkdKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPC 179
|
170 180 190
....*....|....*....|....*....|....*...
gi 780224413 173 GNLDSKTGERVIELLFELNREHgtTLVVVTHDHELAQR 210
Cdd:PRK14243 180 SALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAAR 215
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
145-215 |
5.48e-14 |
|
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: 67.56 E-value: 5.48e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLfelnREHGTTLVVVTHDHELAQRCQRQL 215
Cdd:cd03223 92 LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLL----KELGITVISVGHRPSLWKFHDRVL 158
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
7-217 |
8.99e-14 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 67.82 E-value: 8.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEgraRLR 86
Cdd:cd03369 7 IEVENL--SVRYAPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLE---DLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aEQVGFVFQSflllPTLsalenvmlpaeLRGETRC------EPRARELLAAVGLGERLHHLpprlSGGEQQRVAIARAFM 160
Cdd:cd03369 82 -SSLTIIPQD----PTL-----------FSGTIRSnldpfdEYSDEEIYGALRVSEGGLNL----SQGQRQLLCLARALL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 161 TRPSLLLADEPTGNLDSKTG---ERVIELLFElnrehGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03369 142 KRPRVLVLDEATASIDYATDaliQKTIREEFT-----NSTILTIAHRLRTIIDYDKILVM 196
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
21-203 |
1.04e-13 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.17 E-value: 1.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 21 ESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLL--AGLDLPSQGDIEILGQSLLQLDEEGRARLRaeqVGFVFQ--- 95
Cdd:COG0396 11 EGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLmgHPKYEVTSGSILLDGEDILELSPDERARAG---IFLAFQypv 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 96 --------SFLLlptlSALENVMLPAELRGETRcePRARELLAAVGLGERLHHlppR-----LSGGEQQRVAIARAFMTR 162
Cdd:COG0396 88 eipgvsvsNFLR----TALNARRGEELSAREFL--KLLKEKMKELGLDEDFLD---RyvnegFSGGEKKRNEILQMLLLE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 780224413 163 PSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTH 203
Cdd:COG0396 159 PKLAILDETDSGLDIDALRIVAEGVNKL-RSPDRGILIITH 198
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
20-217 |
1.30e-13 |
|
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: 67.11 E-value: 1.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 20 QESLTILEGIDLQVNSGETVALVGASGSGKSTllgllagldlpsqgdieiLGQSLL-QLDEEGRARLRAEQVGFVFQ-SF 97
Cdd:cd03250 15 QETSFTLKDINLEVPKGELVAIVGPVGSGKSS------------------LLSALLgELEKLSGSVSVPGSIAYVSQePW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 98 LLLPTLsaLENVmlpaeLRGETRCEPRARELLAAVGLGERLHHLPPR-----------LSGGEQQRVAIARAFMTRPSLL 166
Cdd:cd03250 77 IQNGTI--RENI-----LFGKPFDEERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIY 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 780224413 167 LADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03250 150 LLDDPLSAVDAHVGRHIFENCILGLLLNNKTRILVTHQLQLLPHADQIVVL 200
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
6-204 |
1.82e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 69.19 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 6 IINVKGLGKTVRLGQEsltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLdlpsqgDIEILGQSLLQldeEGRarl 85
Cdd:TIGR03719 4 IYTMNRVSKVVPPKKE---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV------DKDFNGEARPQ---PGI--- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 86 raeQVGFVFQSFLLLPTLSALENVMLP-AELRG---------ETRCEPRA------------RELLAAVG---LGERLH- 139
Cdd:TIGR03719 69 ---KVGYLPQEPQLDPTKTVRENVEEGvAEIKDaldrfneisAKYAEPDAdfdklaaeqaelQEIIDAADawdLDSQLEi 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 140 -----HLPP------RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTgervIELLFELNREHGTTLVVVTHD 204
Cdd:TIGR03719 146 amdalRCPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAES----VAWLERHLQEYPGTVVAVTHD 217
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
21-203 |
7.83e-13 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 67.21 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 21 ESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQgdieILGQSLLQLDEEGRARLRaeQVGFVFQSFLLL 100
Cdd:PLN03211 79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNN----FTGTILANNRKPTKQILK--RTGFVTQDDILY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 101 PTLSALENVMLPAELR---GETRCEPR--ARELLAAVGLGERLHHLPPR-----LSGGEQQRVAIARAFMTRPSLLLADE 170
Cdd:PLN03211 153 PHLTVRETLVFCSLLRlpkSLTKQEKIlvAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDE 232
|
170 180 190
....*....|....*....|....*....|...
gi 780224413 171 PTGNLDSKTGERVIELLFELNREhGTTLVVVTH 203
Cdd:PLN03211 233 PTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMH 264
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
15-207 |
1.74e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 64.75 E-value: 1.74e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESltILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEilgqsllqldeegraRLRAEQVGFVF 94
Cdd:PRK09544 11 SVSFGQRR--VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------------RNGKLRIGYVP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 95 QSFLLLPTLsalenvmlPAELRGETRCEPRARE-----LLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLAD 169
Cdd:PRK09544 74 QKLYLDTTL--------PLTVNRFLRLRPGTKKedilpALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145
|
170 180 190
....*....|....*....|....*....|....*...
gi 780224413 170 EPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHEL 207
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHL 183
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
26-200 |
1.87e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 66.20 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqlDEEGRARLRaEQVGFVFQSFLLLPTLSA 105
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLR-NQVALVSQNVHLFNDTIA 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 lENVMLPAELRgETRCE-PRARELLAAVGLGERLHH-----------LpprLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:PRK11176 435 -NNIAYARTEQ-YSREQiEEAARMAYAMDFINKMDNgldtvigengvL---LSGGQRQRIAIARALLRDSPILILDEATS 509
|
170 180
....*....|....*....|....*..
gi 780224413 174 NLDSKTgERVIELLFELNREHGTTLVV 200
Cdd:PRK11176 510 ALDTES-ERAIQAALDELQKNRTSLVI 535
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
25-207 |
2.79e-12 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 64.64 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSlLQLDEEGRARLRaEQVGFVFQSflllPTLS 104
Cdd:PRK13638 16 VLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKP-LDYSKRGLLALR-QQVATVFQD----PEQQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ------------ALENVMLPaelrgETRCEPRARELLAAVGlGERLHHLPPR-LSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:PRK13638 90 ifytdidsdiafSLRNLGVP-----EAEITRRVDEALTLVD-AQHFRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEP 163
|
170 180 190
....*....|....*....|....*....|....*.
gi 780224413 172 TGNLDSKTGERVIELLFELNREhGTTLVVVTHDHEL 207
Cdd:PRK13638 164 TAGLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDIDL 198
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
26-203 |
2.96e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 65.32 E-value: 2.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSllQLDEEGRARLRAeQVGFVFQSFLLLPTLSA 105
Cdd:PRK11288 20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQE--MRFASTTAALAA-GVAIIYQELHLVPEMTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVML---PAEL----RGETRcePRARELLAavGLGERLHHLPP--RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PRK11288 97 AENLYLgqlPHKGgivnRRLLN--YEAREQLE--HLGVDIDPDTPlkYLSIGQRQMVEIAKALARNARVIAFDEPTSSLS 172
|
170 180 190
....*....|....*....|....*....|
gi 780224413 177 SktgeRVIELLFELNRE---HGTTLVVVTH 203
Cdd:PRK11288 173 A----REIEQLFRVIRElraEGRVILYVSH 198
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
32-204 |
3.48e-12 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 64.18 E-value: 3.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 32 QVNSGETVALVGASGSGKSTlLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARLRA---EQVGFVFqsflLLPTLSALEn 108
Cdd:PRK03695 18 EVRAGEILHLVGPNGAGKST-LLARMAGLLPGSGSIQFAGQPLEAWSAAELARHRAylsQQQTPPF----AMPVFQYLT- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 109 VMLPAELRgETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFM-----TRPS--LLLADEPTGNLDSkTGE 181
Cdd:PRK03695 92 LHQPDKTR-TEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNSLDV-AQQ 169
|
170 180
....*....|....*....|...
gi 780224413 182 RVIELLFELNREHGTTLVVVTHD 204
Cdd:PRK03695 170 AALDRLLSELCQQGIAVVMSSHD 192
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
16-217 |
3.96e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 64.08 E-value: 3.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 16 VRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPS--------QGDIEILGQSLLQLDEEGRARLRA 87
Cdd:PRK13547 7 LHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 88 -----EQVGFVFqsflllptlSALENVMLP----AELRGETRCEPR--ARELLAAVGLGERLHHLPPRLSGGEQQRVAIA 156
Cdd:PRK13547 87 vlpqaAQPAFAF---------SAREIVLLGryphARRAGALTHRDGeiAWQALALAGATALVGRDVTTLSGGELARVQFA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 157 RAF---------MTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK13547 158 RVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAM 227
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
26-217 |
4.24e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 65.04 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEegRARLRAeqvGFVF-----QSFLLL 100
Cdd:COG1129 268 VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSP--RDAIRA---GIAYvpedrKGEGLV 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 101 PTLSALENVMLPAeLRGETRC--EPRARELLAAVGLGERLHHLPPR-------LSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:COG1129 343 LDLSIRENITLAS-LDRLSRGglLDRRRERALAEEYIKRLRIKTPSpeqpvgnLSGGNQQKVVLAKWLATDPKVLILDEP 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 780224413 172 TGNLDSKTGERVIELLFELNREhGTTLVVVTHDH-ELAQRCQRQLVM 217
Cdd:COG1129 422 TRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELpELLGLSDRILVM 467
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
5-217 |
5.77e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.66 E-value: 5.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLgkTVRlGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegRAR 84
Cdd:COG3845 256 VVLEVENL--SVR-DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS---PRE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LRAEQVGFVFQSFL---LLPTLSALENVMLpaelrGETRCEPRARELL----AAVGLGERL----------HHLPPR-LS 146
Cdd:COG3845 330 RRRLGVAYIPEDRLgrgLVPDMSVAENLIL-----GRYRRPPFSRGGFldrkAIRAFAEELieefdvrtpgPDTPARsLS 404
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 780224413 147 GGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:COG3845 405 GGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDlDEILALSDRIAVM 475
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-217 |
9.99e-12 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 62.72 E-value: 9.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDeegrARLRAEQVGFVFQSFLLLPTL 103
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLS----SRQLARRLALLPQHHLTPEGI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENV------MLPAELRGETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDS 177
Cdd:PRK11231 92 TVRELVaygrspWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDI 171
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 178 KTGERVIELLFELNREhGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK11231 172 NHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVV 210
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
15-211 |
1.06e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.76 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLtiLEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEI-LGQSLlqldeegrARLRAEQvgFV 93
Cdd:PRK15064 8 TMQFGAKPL--FENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLdPNERL--------GKLRQDQ--FA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 94 FQSFLLLPTL----SALENVM--------LP-----------------AELRGETrCEPRARELLAAVGLGERLHHLPPR 144
Cdd:PRK15064 76 FEEFTVLDTVimghTELWEVKqerdriyaLPemseedgmkvadlevkfAEMDGYT-AEARAGELLLGVGIPEEQHYGLMS 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 145 -LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTgervIELLFELNREHGTTLVVVTHD-HELAQRC 211
Cdd:PRK15064 155 eVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHDrHFLNSVC 219
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-207 |
2.76e-11 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 62.88 E-value: 2.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 16 VRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIL-GQSLLQLDEEGRARLRAEQvgfvf 94
Cdd:PRK10636 318 VSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLGYFAQHQLEFLRADE----- 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 95 qsflllptlSALENV--MLPAELrgetrcEPRARELLAAVGL-GERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:PRK10636 393 ---------SPLQHLarLAPQEL------EQKLRDYLGGFGFqGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEP 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 780224413 172 TGNLDSKTGERVIELLFELNrehgTTLVVVTHDHEL 207
Cdd:PRK10636 458 TNHLDLDMRQALTEALIDFE----GALVVVSHDRHL 489
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
5-203 |
2.84e-11 |
|
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: 60.72 E-value: 2.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 5 PIINVKGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPS--QGDIEILGQsllQLDEEGR 82
Cdd:cd03232 2 SVLTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGR---PLDKNFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 83 ARlraeqVGFVFQSFLLLPTLSALENVMLPAELRGetrceprarellaavglgerlhhlpprLSGGEQQRVAIARAFMTR 162
Cdd:cd03232 79 RS-----TGYVEQQDVHSPNLTVREALRFSALLRG---------------------------LSVEQRKRLTIGVELAAK 126
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 780224413 163 PSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTH 203
Cdd:cd03232 127 PSILFLDEPTSGLDSQAAYNIVRFLKKL-ADSGQAILCTIH 166
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
18-204 |
2.92e-11 |
|
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: 61.27 E-value: 2.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 18 LGQESLTILEGidlQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSL------LQLDEEGRAR--LRAEQ 89
Cdd:cd03237 10 LGEFTLEVEGG---SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVsykpqyIKADYEGTVRdlLSSIT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 90 VGFVFQSFLllptlsalenvmlpaelrgETrceprarELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLAD 169
Cdd:cd03237 87 KDFYTHPYF-------------------KT-------EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLD 140
|
170 180 190
....*....|....*....|....*....|....*
gi 780224413 170 EPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:cd03237 141 EPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHD 175
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-176 |
3.17e-11 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 61.20 E-value: 3.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGKTVrlgqESLTILEGIDLQVNSGETVALVGASGSGKSTllGLLAGLDLPS----QGDIEILGQSLLQ 76
Cdd:CHL00131 2 NKNKPILEIKNLHASV----NENEILKGLNLSINKGEIHAIMGPNGSGKST--LSKVIAGHPAykilEGDILFKGESILD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 77 LDEEGRARLraeQVGFVFQSFLLLPTLSALENVMLPAELR----GETRCEPRA-----RELLAAVGLGERLHH--LPPRL 145
Cdd:CHL00131 76 LEPEERAHL---GIFLAFQYPIEIPGVSNADFLRLAYNSKrkfqGLPELDPLEfleiiNEKLKLVGMDPSFLSrnVNEGF 152
|
170 180 190
....*....|....*....|....*....|.
gi 780224413 146 SGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:CHL00131 153 SGGEKKRNEILQMALLDSELAILDETDSGLD 183
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
26-203 |
3.81e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 3.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARLRAEQVGFVFQSFLLLPTLSA 105
Cdd:PRK10762 20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGK---EVTFNGPKSSQEAGIGIIHQELNLIPQLTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRGE------TRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNL-DSK 178
Cdd:PRK10762 97 AENIFLGREFVNRfgridwKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALtDTE 176
|
170 180
....*....|....*....|....*....
gi 780224413 179 TgerviELLF----ELnREHGTTLVVVTH 203
Cdd:PRK10762 177 T-----ESLFrvirEL-KSQGRGIVYISH 199
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-203 |
5.82e-11 |
|
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: 61.89 E-value: 5.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTllgllagldlpsqgdieILGQSLLQLDE-EGRARLRAeQVGFVFQSfLLLPTLS 104
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSS-----------------LLSALLAEMDKvEGHVHMKG-SVAYVPQQ-AWIQNDS 714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRgetrcEPRARELLAAVGLGERLHHLPP-----------RLSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:TIGR00957 715 LRENILFGKALN-----EKYYQQVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDPLS 789
|
170 180 190
....*....|....*....|....*....|.
gi 780224413 174 NLDSKTGERVIE-LLFELNREHGTTLVVVTH 203
Cdd:TIGR00957 790 AVDAHVGKHIFEhVIGPEGVLKNKTRILVTH 820
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
37-203 |
5.92e-11 |
|
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: 61.95 E-value: 5.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 37 ETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllqlDEEGRARLRAEQVGFVFQSFLLLPTLSALENVMLPAELR 116
Cdd:TIGR01257 957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGK-----DIETNLDAVRQSLGMCPQHNILFHHLTVAEHILFYAQLK 1031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 117 GETRCEPR--ARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLfeLNREH 194
Cdd:TIGR01257 1032 GRSWEEAQleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL--LKYRS 1109
|
....*....
gi 780224413 195 GTTLVVVTH 203
Cdd:TIGR01257 1110 GRTIIMSTH 1118
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
1-176 |
6.00e-11 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 60.25 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 1 MNSTPIINVKGLGktvrLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDee 80
Cdd:PRK13543 6 HTAPPLLAAHALA----FSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 81 grarlRAEQVGFVFQSFLLLPTLSALENVMLPAELRGEtRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFM 160
Cdd:PRK13543 80 -----RSRFMAYLGHLPGLKADLSTLENLHFLCGLHGR-RAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWL 153
|
170
....*....|....*.
gi 780224413 161 TRPSLLLADEPTGNLD 176
Cdd:PRK13543 154 SPAPLWLLDEPYANLD 169
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
10-204 |
1.15e-10 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 60.90 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 10 KGLGKTVRLGQEsltILEGIDLQVNSGETVALVGASGSGKSTllgllagldlpsqgdieilgqsLLQ----LDEE--GRA 83
Cdd:PRK11819 10 NRVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKST----------------------LLRimagVDKEfeGEA 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 84 RLRAE-QVGFVFQSFLLLPTLSALENVMlpaELRGETR-------------CEPRAR--ELLAAVG-LGERLHH------ 140
Cdd:PRK11819 65 RPAPGiKVGYLPQEPQLDPEKTVRENVE---EGVAEVKaaldrfneiyaayAEPDADfdALAAEQGeLQEIIDAadawdl 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 141 ------------LPP------RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSktgERVIELLFELNREHGtTLVVVT 202
Cdd:PRK11819 142 dsqleiamdalrCPPwdakvtKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDA---ESVAWLEQFLHDYPG-TVVAVT 217
|
..
gi 780224413 203 HD 204
Cdd:PRK11819 218 HD 219
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-217 |
1.46e-10 |
|
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: 60.80 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 2 NSTPIINVKGLGKtVRLGQESLTIlEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEG 81
Cdd:TIGR01257 1933 NKTDILRLNELTK-VYSGTSSPAV-DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDV 2010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 82 RarlraEQVGFVFQSFLLLPTLSALENVMLPAELRG--ETRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAF 159
Cdd:TIGR01257 2011 H-----QNMGYCPQFDAIDDLLTGREHLYLYARLRGvpAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIAL 2085
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 160 MTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHDHELAQR-CQRQLVM 217
Cdd:TIGR01257 2086 IGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEAlCTRLAIM 2143
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
15-200 |
9.64e-10 |
|
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213200 [Multi-domain] Cd Length: 202 Bit Score: 56.50 E-value: 9.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPS---QGDIEILGQSLLQLDEEGRArlraeQVG 91
Cdd:cd03233 12 TTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPG-----EII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 92 FVFQSFLLLPTLSALENVmlpaelrgETRCEPRARELLAAVglgerlhhlpprlSGGEQQRVAIARAFMTRPSLLLADEP 171
Cdd:cd03233 87 YVSEEDVHFPTLTVRETL--------DFALRCKGNEFVRGI-------------SGGERKRVSIAEALVSRASVLCWDNS 145
|
170 180
....*....|....*....|....*....
gi 780224413 172 TGNLDSKTGERVIELLFELNREHGTTLVV 200
Cdd:cd03233 146 TRGLDSSTALEILKCIRTMADVLKTTTFV 174
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-172 |
1.68e-09 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 57.44 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldeeGRARLRAE---QVGFVFQSfL---L 99
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDM------ADARHRRAvcpRIAYMPQG-LgknL 89
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 100 LPTLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPT 172
Cdd:NF033858 90 YPTLSVFENLDFFGRLFGQDAAERRRRidELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPT 164
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
7-204 |
2.45e-09 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 55.86 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLGKtvRLGQEslTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEEGRARlr 86
Cdd:COG4604 2 IEIKNVSK--RYGGK--VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 aeqvgfvfqsflllpTLSAL--ENVMLP----AEL---------RGETRCEPRA--RELLAAVGLGErLHHlppR----L 145
Cdd:COG4604 76 ---------------RLAILrqENHINSrltvRELvafgrfpysKGRLTAEDREiiDEAIAYLDLED-LAD---RyldeL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 146 SGGEQQRVAIArafMT----RPSLLLaDEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:COG4604 137 SGGQRQRAFIA---MVlaqdTDYVLL-DEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHD 195
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
144-210 |
2.84e-09 |
|
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: 55.31 E-value: 2.84e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780224413 144 RLSGGEQQ------RVAIARAFMTRPSLLLADEPTGNLDS-KTGERVIELLFELNREHGTTLVVVTHDHELAQR 210
Cdd:cd03240 115 RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDA 188
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
25-203 |
9.37e-09 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 53.80 E-value: 9.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLlqldEEGRARLRaEQVGFVFQSFLLLPTLS 104
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELrgeTRCEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVI 184
Cdd:PRK13540 91 LRENCLYDIHF---SPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
|
170
....*....|....*....
gi 780224413 185 ELLfELNREHGTTLVVVTH 203
Cdd:PRK13540 168 TKI-QEHRAKGGAVLLTSH 185
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
25-185 |
9.99e-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: 54.48 E-value: 9.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEilgqsllqldEEGRarlraeqVGFVFQSFLLLPTlS 104
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIK----------HSGR-------ISFSSQFSWIMPG-T 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLpaelrGETRCEPRARELLAAVGLGERLHHLPPR-----------LSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:cd03291 114 IKENIIF-----GVSYDEYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
|
170
....*....|..
gi 780224413 174 NLDSKTGERVIE 185
Cdd:cd03291 189 YLDVFTEKEIFE 200
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
14-203 |
1.05e-08 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 54.03 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 14 KTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLD--LPSQGDIEILGQSLLQLDEEGRArlrAEQVG 91
Cdd:PRK09580 5 KDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRA---GEGIF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 92 FVFQSFLLLPTLSaleNVMLPAELRGETRcEPRARELLAAVGLGE------RLHHLPPRL---------SGGEQQRVAIA 156
Cdd:PRK09580 82 MAFQYPVEIPGVS---NQFFLQTALNAVR-SYRGQEPLDRFDFQDlmeekiALLKMPEDLltrsvnvgfSGGEKKRNDIL 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 780224413 157 RAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTH 203
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-204 |
1.06e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 54.96 E-value: 1.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 24 TILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIlGQSL--LQLDEEgrarlRAEqvgfvfqsflLLP 101
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHC-GTKLevAYFDQH-----RAE----------LDP 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLSALENVmlpAELRGETRCEPRARELLAAvgLGERLHHlPPR-------LSGGEQQRVAIARAFMtRPS-LLLADEPTG 173
Cdd:PRK11147 397 EKTVMDNL---AEGKQEVMVNGRPRHVLGY--LQDFLFH-PKRamtpvkaLSGGERNRLLLARLFL-KPSnLLILDEPTN 469
|
170 180 190
....*....|....*....|....*....|.
gi 780224413 174 NLDSKTgervIELLFELNREHGTTLVVVTHD 204
Cdd:PRK11147 470 DLDVET----LELLEELLDSYQGTVLLVSHD 496
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-203 |
1.50e-08 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 21 ESLTILEGIDLQVNSGETVALVGASGSGKSTllgllagldlpsqgdieiLGQSLLQLDEEGRARLRAEQ-VGFV-FQSFL 98
Cdd:PTZ00243 671 EPKVLLRDVSVSVPRGKLTVVLGATGSGKST------------------LLQSLLSQFEISEGRVWAERsIAYVpQQAWI 732
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSAleNVML-----PAELRGETR-CEPRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPT 172
Cdd:PTZ00243 733 MNATVRG--NILFfdeedAARLADAVRvSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
|
170 180 190
....*....|....*....|....*....|.
gi 780224413 173 GNLDSKTGERVIELLFeLNREHGTTLVVVTH 203
Cdd:PTZ00243 811 SALDAHVGERVVEECF-LGALAGKTRVLATH 840
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
145-203 |
1.60e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 54.65 E-value: 1.60e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTgERVIE-LLFELNREHGTTLVVVTH 203
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNS-EKLIEkTIVDIKDKADKTIITIAH 1417
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
25-185 |
1.76e-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: 54.53 E-value: 1.76e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEilgqsllqldEEGRarlraeqVGFVFQSFLLLPTlS 104
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIK----------HSGR-------ISFSPQTSWIMPG-T 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLpaelrGETRCEPRARELLAAVGLGERLHHLPPR-----------LSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:TIGR01271 503 IKDNIIF-----GLSYDEYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
|
170
....*....|..
gi 780224413 174 NLDSKTGERVIE 185
Cdd:TIGR01271 578 HLDVVTEKEIFE 589
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
145-176 |
2.04e-08 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 54.24 E-value: 2.04e-08
10 20 30
....*....|....*....|....*....|..
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
143-210 |
3.37e-08 |
|
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: 51.59 E-value: 3.37e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 780224413 143 PRLSGGEQQRVAIARAF----MTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQR 210
Cdd:cd03227 76 LQLSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEH-LVKGAQVIVITHLPELAEL 146
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
15-201 |
3.72e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.09 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLTILEgiDLQVNSGETVALVGASGSGKSTLLGLlagldlpsqgdieiLGQSLLQLDEEGR------ARLRAE 88
Cdd:PRK10938 10 TFRLSDTKTLQLP--SLTLNAGDSWAFVGANGSGKSALARA--------------LAGELPLLSGERQsqfshiTRLSFE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 89 QV-GFVFQSFLLLPT--LSALEN-------VMLPAELRGETRCEprarELLAAVGLGerlhHLPPR----LSGGEQQRVA 154
Cdd:PRK10938 74 QLqKLVSDEWQRNNTdmLSPGEDdtgrttaEIIQDEVKDPARCE----QLAQQFGIT----ALLDRrfkyLSTGETRKTL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 780224413 155 IARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVV 201
Cdd:PRK10938 146 LCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
|
|
| ABC_UvrA_I |
cd03270 |
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ... |
126-207 |
4.05e-08 |
|
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 52.26 E-value: 4.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 126 RELLAAVGLGER--------LHHL-----PPRLSGGEQQRVAIARAFMTRPS--LLLADEPTGNLDSKTGERVIELLFEL 190
Cdd:cd03270 106 RLLFARVGIRERlgflvdvgLGYLtlsrsAPTLSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL 185
|
90
....*....|....*..
gi 780224413 191 nREHGTTLVVVTHDHEL 207
Cdd:cd03270 186 -RDLGNTVLVVEHDEDT 201
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
20-203 |
4.90e-08 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 53.18 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 20 QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSL--LQLDeEGRARLR-AEQVGFVFQS 96
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLtkLQLD-SWRSRLAvVSQTPFLFSD 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 97 flllptlSALENVMLPAELRGETRCEPRARelLAAV-------------GLGERlhhlPPRLSGGEQQRVAIARAFMTRP 163
Cdd:PRK10789 404 -------TVANNIALGRPDATQQEIEHVAR--LASVhddilrlpqgydtEVGER----GVMLSGGQKQRISIARALLLNA 470
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 780224413 164 SLLLADEPTGNLDSKTGERVIELLFELNRehGTTLVVVTH 203
Cdd:PRK10789 471 EILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAH 508
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
26-217 |
4.97e-08 |
|
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: 51.17 E-value: 4.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTllgllagldlpsqgdieilgqsLLQ--LDEEGRARLRAeqvgfvfqsflLLPTL 103
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKST----------------------LVNegLYASGKARLIS-----------FLPKF 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 104 SALENVMLpAELRgetrceprareLLAAVGLGE-RLHHLPPRLSGGEQQRVAIARaFM---TRPSLLLADEPTGNLDSKT 179
Cdd:cd03238 58 SRNKLIFI-DQLQ-----------FLIDVGLGYlTLGQKLSTLSGGELQRVKLAS-ELfsePPGTLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*...
gi 780224413 180 GERVIELLFELnREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03238 125 INQLLEVIKGL-IDLGNTVILIEHNLDVLSSADWIIDF 161
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
102-217 |
5.12e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 52.82 E-value: 5.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 102 TLSALENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKT 179
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARadELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179
|
90 100 110
....*....|....*....|....*....|....*...
gi 780224413 180 GERVIELLFELNREhGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:NF000106 180 RNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTV 216
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
25-204 |
6.57e-08 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 52.65 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 25 ILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEI---LGQSLLQLD-------------EEGRARLrAE 88
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYeqdLIVARLQQDpprnvegtvydfvAEGIEEQ-AE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 89 QVGFVFQSFLLLPT------LSALENVMLPAELRGETRCEPRARELLAAVGLGErlHHLPPRLSGGEQQRVAIARAFMTR 162
Cdd:PRK11147 97 YLKRYHDISHLVETdpseknLNELAKLQEQLDHHNLWQLENRINEVLAQLGLDP--DAALSSLSGGWLRKAALGRALVSN 174
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 780224413 163 PSLLLADEPTGNLDSKTgervIELLFELNREHGTTLVVVTHD 204
Cdd:PRK11147 175 PDVLLLDEPTNHLDIET----IEWLEGFLKTFQGSIIFISHD 212
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
7-217 |
1.23e-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: 51.01 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLpSQGDIEILGQSL--LQLDEEGRAR 84
Cdd:cd03289 3 MTVKDL--TAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWnsVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LRAEQVGFVFQsflllptlSALENVMLPAELRGETRCEPRAREllaaVGLGERLHHLPPR-----------LSGGEQQRV 153
Cdd:cd03289 80 GVIPQKVFIFS--------GTFRKNLDPYGKWSDEEIWKVAEE----VGLKSVIEQFPGQldfvlvdggcvLSHGHKQLM 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 780224413 154 AIARAFMTRPSLLLADEPTGNLDSKTGE---RVIELLFElnrehGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQvirKTLKQAFA-----DCTVILSEHRIEAMLECQRFLVI 209
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
29-217 |
2.18e-07 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 51.13 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARLRAeQVGFVFQSFLLLPTLSALEN 108
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGK---PVTAEQPEDYRK-LFSAVFTDFHLFDQLLGPEG 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 109 VMLPAELrgetrceprARELLAAVGLGERLHH-----LPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:PRK10522 418 KPANPAL---------VEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAADQDPHFRREF 488
|
170 180 190
....*....|....*....|....*....|....
gi 780224413 184 IELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK10522 489 YQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEM 522
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
14-203 |
2.34e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.18 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 14 KTVRL---GQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQldeEGRARLRAEQV 90
Cdd:PTZ00265 386 KNVRFhydTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLK---DINLKWWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 91 GFVFQSFLL---------------LPTLSALENVM----------LPAELRGETRCEPRARELLAAVGLGERLH------ 139
Cdd:PTZ00265 463 GVVSQDPLLfsnsiknnikyslysLKDLEALSNYYnedgndsqenKNKRNSCRAKCAGDLNDMSNTTDSNELIEmrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 140 ---------------------HLP-----------PRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELL 187
Cdd:PTZ00265 543 tikdsevvdvskkvlihdfvsALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI 622
|
250
....*....|....*.
gi 780224413 188 FELNREHGTTLVVVTH 203
Cdd:PTZ00265 623 NNLKGNENRITIIIAH 638
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
23-203 |
2.73e-07 |
|
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: 49.64 E-value: 2.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 23 LTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEilgQSLLQLDEEGRARLRAEQ---VGFVFQ-SFL 98
Cdd:cd03290 14 LATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVH---WSNKNESEPSFEATRSRNrysVAYAAQkPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 99 LLPTLSalENVMLPAELRGEtrcepRARELLAAVGLGERLHHLP-----------PRLSGGEQQRVAIARAFMTRPSLLL 167
Cdd:cd03290 91 LNATVE--ENITFGSPFNKQ-----RYKAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190
....*....|....*....|....*....|....*..
gi 780224413 168 ADEPTGNLDSKTGERVI-ELLFELNREHGTTLVVVTH 203
Cdd:cd03290 164 LDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTH 200
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
10-203 |
3.56e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 50.49 E-value: 3.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 10 KGLGKTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPS--QGDIEILGqsllqldeeGRARLRA 87
Cdd:TIGR00956 763 RNLTYEVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGviTGGDRLVN---------GRPLDSS 833
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 88 EQ--VGFVFQSFLLLPTLSALENVMLPAELR--GETRCEPRAR------ELL-------AAVGL-GERLHhlpprlsgGE 149
Cdd:TIGR00956 834 FQrsIGYVQQQDLHLPTSTVRESLRFSAYLRqpKSVSKSEKMEyveeviKLLemesyadAVVGVpGEGLN--------VE 905
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 150 Q-QRVAIARAFMTRPSLLL-ADEPTGNLDSKTGERVIELLFELNrEHGTTLVVVTH 203
Cdd:TIGR00956 906 QrKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLA-DHGQAILCTIH 960
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
7-217 |
4.62e-07 |
|
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: 50.29 E-value: 4.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 7 INVKGLgkTVRLGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLpSQGDIEILGQSL--LQLDEEGRAR 84
Cdd:TIGR01271 1218 MDVQGL--TAKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWnsVTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 85 LRAEQVGFVFQsflllptlSALENVMLPAELRGETRCEPRAREllaaVGLGERLHHLPPR-----------LSGGEQQRV 153
Cdd:TIGR01271 1295 GVIPQKVFIFS--------GTFRKNLDPYEQWSDEEIWKVAEE----VGLKSVIEQFPDKldfvlvdggyvLSNGHKQLM 1362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 780224413 154 AIARAFMTRPSLLLADEPTGNLDSKTGE---RVIELLFElnrehGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQiirKTLKQSFS-----NCTVILSEHRVEALLECQQFLVI 1424
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
145-217 |
5.61e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 49.73 E-value: 5.61e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVM 464
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
29-204 |
8.04e-07 |
|
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];
Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 49.41 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQsllQLDEEGRARLRaEQVGFVFQSFLLLPTLSALEN 108
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNREAYR-QLFSAVFSDFHLFDRLLGLDG 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 109 VMLPAelrgetrcepRARELLAAVGLGERLHH-----LPPRLSGGEQQRVAIARAFMT-RPSLLLaDE------PTgnld 176
Cdd:COG4615 427 EADPA----------RARELLERLELDHKVSVedgrfSTTDLSQGQRKRLALLVALLEdRPILVF-DEwaadqdPE---- 491
|
170 180 190
....*....|....*....|....*....|.
gi 780224413 177 sktgERVI---ELLFELnREHGTTLVVVTHD 204
Cdd:COG4615 492 ----FRRVfytELLPEL-KARGKTVIAISHD 517
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
26-203 |
9.75e-07 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 49.12 E-value: 9.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIlgqsllqldeEGRARLRAEQVGFVFQsflllptLSA 105
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI----------KGSAALIAISSGLNGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRGETRcePRARELLAAV----GLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:PRK13545 103 IENIELKGLMMGLTK--EKIKEIIPEIiefaDIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTK 180
|
170 180
....*....|....*....|..
gi 780224413 182 RVIELLFELnREHGTTLVVVTH 203
Cdd:PRK13545 181 KCLDKMNEF-KEQGKTIFFISH 201
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
15-204 |
1.39e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLTILEGidlQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIlgqSL--------LQLDEEGRARLR 86
Cdd:PRK13409 347 TKKLGDFSLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELkisykpqyIKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 87 AEQVGFVFQSflllptlSALENvmlpaelrgetrceprarELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLL 166
Cdd:PRK13409 421 LRSITDDLGS-------SYYKS------------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLY 475
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 780224413 167 LADEPTGNLD-------SKTGERVIEllfelnrEHGTTLVVVTHD 204
Cdd:PRK13409 476 LLDEPSAHLDveqrlavAKAIRRIAE-------EREATALVVDHD 513
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
145-208 |
2.61e-06 |
|
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: 47.86 E-value: 2.61e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVvthDHELA 208
Cdd:COG1245 213 LSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLVV---EHDLA 273
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
145-204 |
2.69e-06 |
|
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: 46.98 E-value: 2.69e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNrEHGTTLVVVTHD 204
Cdd:cd03236 140 LSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARLIRELA-EDDNYVLVVEHD 198
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
26-203 |
2.74e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 48.05 E-value: 2.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQldeegrarlrAEQVGFVFQSflllptlSA 105
Cdd:PLN03232 633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVIRGSVAY----------VPQVSWIFNA-------TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRGEtrcepRARELLAAVGLGERLHHLPPR-----------LSGGEQQRVAIARAFMTRPSLLLADEPTGN 174
Cdd:PLN03232 696 RENILFGSDFESE-----RYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180
....*....|....*....|....*....
gi 780224413 175 LDSKTGERVIELLFElNREHGTTLVVVTH 203
Cdd:PLN03232 771 LDAHVAHQVFDSCMK-DELKGKTRVLVTN 798
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
144-217 |
2.83e-06 |
|
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: 47.51 E-value: 2.83e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 144 RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:TIGR02633 403 RLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSElAEVLGLSDRVLVI 476
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
145-203 |
3.19e-06 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 47.44 E-value: 3.19e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTgnldSKTGERVIELLFELNREHGTTLVVVTH 203
Cdd:TIGR00954 583 LSGGEKQRIAMARLFYHKPQFAILDECT----SAVSVDVEGYMYRLCREFGITLFSVSH 637
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
9-210 |
3.77e-06 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 47.19 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 9 VKGLGKtvrlGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEIlgqsllqldeegrarlrAE 88
Cdd:PRK15064 322 VENLTK----GFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW-----------------SE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 89 --QVGFVFQSflllpTLSALENVMLPAELRGETRcEPRARELLAAVGLGERLH-----HLPPR-LSGGEQQRVAIARAFM 160
Cdd:PRK15064 381 naNIGYYAQD-----HAYDFENDLTLFDWMSQWR-QEGDDEQAVRGTLGRLLFsqddiKKSVKvLSGGEKGRMLFGKLMM 454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 780224413 161 TRPSLLLADEPTGNLDSKTgervIELL-FELNREHGtTLVVVTHDHE----LAQR 210
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMES----IESLnMALEKYEG-TLIFVSHDREfvssLATR 504
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
145-204 |
4.89e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 45.64 E-value: 4.89e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHD 204
Cdd:cd03222 72 LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHD 131
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
125-211 |
4.94e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 46.93 E-value: 4.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 125 ARELLAAVGLGERLHHLPPR-LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTH 203
Cdd:PRK10938 381 AQQWLDILGIDKRTADAPFHsLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460
|
....*...
gi 780224413 204 DHELAQRC 211
Cdd:PRK10938 461 HAEDAPAC 468
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-204 |
5.20e-06 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 46.35 E-value: 5.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEilgqsllqldEEGRARLRAEQVGFVFQsflllptLSA 105
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD----------RNGEVSVIAISAGLSGQ-------LTG 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 106 LENVMLPAELRGETRCEPRAR--ELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERV 183
Cdd:PRK13546 103 IENIEFKMLCMGFKRKEIKAMtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|.
gi 780224413 184 IELLFELnREHGTTLVVVTHD 204
Cdd:PRK13546 183 LDKIYEF-KEQNKTIFFVSHN 202
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
15-204 |
5.38e-06 |
|
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: 46.70 E-value: 5.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 15 TVRLGQESLTILEGidlQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIeilgqsllqlDEEGR-----ARLRAEQ 89
Cdd:COG1245 348 TKSYGGFSLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEV----------DEDLKisykpQYISPDY 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 90 VGFVfQSFLLLPTLSALENVMLPAELrgetrceprARELlaavglgeRLHHLPPR----LSGGEQQRVAIARAFMTRPSL 165
Cdd:COG1245 415 DGTV-EEFLRSANTDDFGSSYYKTEI---------IKPL--------GLEKLLDKnvkdLSGGELQRVAIAACLSRDADL 476
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 780224413 166 LLADEPTGNLD-------SKTGERVIEllfelnrEHGTTLVVVTHD 204
Cdd:COG1245 477 YLLDEPSAHLDveqrlavAKAIRRFAE-------NRGKTAMVVDHD 515
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
144-217 |
5.71e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 46.85 E-value: 5.71e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 780224413 144 RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVThdHELAQ---RCQRQLVM 217
Cdd:PRK13549 405 RLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVIS--SELPEvlgLSDRVLVM 478
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
124-204 |
9.75e-06 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 45.96 E-value: 9.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 124 RARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHgtTLVVVTH 203
Cdd:PRK13409 192 KLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAEGK--YVLVVEH 269
|
.
gi 780224413 204 D 204
Cdd:PRK13409 270 D 270
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
122-176 |
1.16e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 46.01 E-value: 1.16e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 122 EPRARELLAAVGLGERLHHLPPR-LSGGEQQRVAIARAFMTRPSLLLADEPTGNLD 176
Cdd:PLN03073 321 EARAASILAGLSFTPEMQVKATKtFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
29-217 |
2.24e-05 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 45.04 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 29 IDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEILGQSLLQLDEegRARLRAeqvGFVF------QSFLLLPT 102
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALST--AQRLAR---GLVYlpedrqSSGLYLDA 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 103 -----LSALENVMLPAELRgetrcepRAREllAAV------GLGERLHHL--PPR-LSGGEQQRVAIARAFMTRPSLLLA 168
Cdd:PRK15439 357 plawnVCALTHNRRGFWIK-------PARE--NAVleryrrALNIKFNHAeqAARtLSGGNQQKVLIAKCLEASPQLLIV 427
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 780224413 169 DEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK15439 428 DEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVM 476
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-207 |
2.71e-05 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 44.85 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 28 GIDLQvnsgETVALVGASGSGKSTLLGLLAGLDLPSQGDIeilgqsllqldeegrarLRAEQVGFVFQSFLLLPTLSALE 107
Cdd:PLN03073 531 GIDLD----SRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMAVFSQHHVDGLDLSS 589
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 108 NVMLPAelrgeTRCEP-----RARELLAAVGLGERLHHLPP-RLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGE 181
Cdd:PLN03073 590 NPLLYM-----MRCFPgvpeqKLRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVE 664
|
170 180
....*....|....*....|....*...
gi 780224413 182 RVIE--LLFElnrehGTTLvVVTHDHEL 207
Cdd:PLN03073 665 ALIQglVLFQ-----GGVL-MVSHDEHL 686
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
124-203 |
2.76e-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: 44.62 E-value: 2.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 124 RARELLAAVGLGE-RLHHLPPRLSGGEQQRVAIARAFMTR---PSLLLADEPTgnldskTG---ERVIELLFELNR--EH 194
Cdd:TIGR00630 808 RKLQTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPT------TGlhfDDIKKLLEVLQRlvDK 881
|
....*....
gi 780224413 195 GTTLVVVTH 203
Cdd:TIGR00630 882 GNTVVVIEH 890
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
20-200 |
2.87e-05 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 44.71 E-value: 2.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 20 QESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPSQGDIEilgqSLLQLD----EEGRARLRAEqVGFVFQ 95
Cdd:TIGR00956 71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVE----GVITYDgitpEEIKKHYRGD-VVYNAE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 96 SFLLLPTLSALENVMLPAELRG----------ETRCEPRARELLAAVGLGerlHHLPPR--------LSGGEQQRVAIAR 157
Cdd:TIGR00956 146 TDVHFPHLTVGETLDFAARCKTpqnrpdgvsrEEYAKHIADVYMATYGLS---HTRNTKvgndfvrgVSGGERKRVSIAE 222
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 780224413 158 AFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVV 200
Cdd:TIGR00956 223 ASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLV 265
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
127-203 |
3.09e-05 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 44.63 E-value: 3.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 127 ELLAAVGLGE-RLHHLPPRLSGGEQQRVAIARAFM---TRPSLLLADEPTgnldskTG------ERVIELLFELnREHGT 196
Cdd:COG0178 808 QTLQDVGLGYiKLGQPATTLSGGEAQRVKLASELSkrsTGKTLYILDEPT------TGlhfhdiRKLLEVLHRL-VDKGN 880
|
....*..
gi 780224413 197 TLVVVTH 203
Cdd:COG0178 881 TVVVIEH 887
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
145-206 |
5.01e-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: 43.85 E-value: 5.01e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780224413 145 LSGGEQQRVAIARAFMTRPS--LLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHE 206
Cdd:TIGR00630 489 LSGGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDED 551
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
122-204 |
7.00e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.62 E-value: 7.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 122 EPRARELLAAVGLG-ERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSktgERVIELLFELNREHGtTLVV 200
Cdd:PRK10636 126 RSRAASLLHGLGFSnEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDL---DAVIWLEKWLKSYQG-TLIL 201
|
....
gi 780224413 201 VTHD 204
Cdd:PRK10636 202 ISHD 205
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
145-217 |
7.73e-05 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 43.23 E-value: 7.73e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELNREHGTTLVVVTHDHELAQRCQRQLVM 217
Cdd:PRK09700 410 LSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVF 482
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
123-204 |
8.33e-05 |
|
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: 42.60 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 123 PRARELLAA---VGLGE-RLHHLPPRLSGGEQQRVAIARAFM---TRPSLLLADEPTGNLDSKTGERVIELLFELnREHG 195
Cdd:cd03271 144 PKIARKLQTlcdVGLGYiKLGQPATTLSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRL-VDKG 222
|
....*....
gi 780224413 196 TTLVVVTHD 204
Cdd:cd03271 223 NTVVVIEHN 231
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
18-178 |
1.57e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 42.53 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 18 LGQESLTILEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLPS--QGDIEILGQSLLQldeEGRARLRaeqvGFVFQ 95
Cdd:PLN03140 888 VTEDRLQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFPKKQ---ETFARIS----GYCEQ 960
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 96 SFLLLPTLSALENVMLPAELR--GETRCEPRAR------ELLAAVGLGERLHHLP--PRLSGGEQQRVAIARAFMTRPSL 165
Cdd:PLN03140 961 NDIHSPQVTVRESLIYSAFLRlpKEVSKEEKMMfvdevmELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSI 1040
|
170
....*....|...
gi 780224413 166 LLADEPTGNLDSK 178
Cdd:PLN03140 1041 IFMDEPTSGLDAR 1053
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
137-204 |
1.59e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 42.51 E-value: 1.59e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 137 RLHHLP-----PRLSGGEQQRVAIARAFMT---RPSLLLADEPTGNLDSKTGERVIELLFELNREhGTTLVVVTHD 204
Cdd:PRK00635 797 GLDYLPlgrplSSLSGGEIQRLKLAYELLApskKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQ-GHTVVIIEHN 871
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
145-217 |
2.35e-04 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. 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: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 41.88 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 145 LSGGEQQRVAIARAFM----------TRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHELAQRCQRQ 214
Cdd:TIGR00618 951 LSGGETFLASLSLALAladllstsggTVLDSLFIDEGFGSLDEDSLDRAIGILDAI-REGSKMIGIISHVPEFRERIPHR 1029
|
...
gi 780224413 215 LVM 217
Cdd:TIGR00618 1030 ILV 1032
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
26-209 |
2.48e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.03 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 26 LEGIDLQVNSGETVALVGASGSGKSTLLGLLAGLDLP-SQGDIEILGQSLLqldeegrarlrAEQVGFVFQSflllptlS 104
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPrSDASVVIRGTVAY-----------VPQVSWIFNA-------T 694
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 105 ALENVMLPAELRGEtrcepRARELLAAVGLGERLHHLPPR-----------LSGGEQQRVAIARAFMTRPSLLLADEPTG 173
Cdd:PLN03130 695 VRDNILFGSPFDPE-----RYERAIDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPLS 769
|
170 180 190
....*....|....*....|....*....|....*....
gi 780224413 174 NLDSKTGERVIE--LLFELNrehGTTLVVVTHD-HELAQ 209
Cdd:PLN03130 770 ALDAHVGRQVFDkcIKDELR---GKTRVLVTNQlHFLSQ 805
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
122-213 |
3.78e-04 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 41.35 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 122 EPRARELLAavGLGERLHHL---------PPR----LSGGEQQRVAIARAFMTRPS--LLLADEPTGNLDSKTGERVIEL 186
Cdd:PRK00635 443 SLSIEEVLQ--GLKSRLSILidlglpyltPERalatLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINV 520
|
90 100
....*....|....*....|....*..
gi 780224413 187 LFELnREHGTTLVVVTHDHELAQRCQR 213
Cdd:PRK00635 521 IKKL-RDQGNTVLLVEHDEQMISLADR 546
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
152-213 |
7.48e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 40.42 E-value: 7.48e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 780224413 152 RVAIARAFMTRPSLLLADEPTGNLDSKTGER----VIELLFELNREHGTTLVVVTHDHELAQRCQR 213
Cdd:TIGR00606 1213 RLALAETFCLNCGIIALDEPTTNLDRENIESlahaLVEIIKSRSQQRNFQLLVITHDEDFVELLGR 1278
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
123-203 |
8.41e-04 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 40.06 E-value: 8.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 123 PRAR---ELLAAVGLGE-RLHHLPPRLSGGEQQRVAIARAFMTRP---SLLLADEPTgnldskTG---ERVIELLFELNR 192
Cdd:PRK00349 805 PKIArklQTLVDVGLGYiKLGQPATTLSGGEAQRVKLAKELSKRStgkTLYILDEPT------TGlhfEDIRKLLEVLHR 878
|
90
....*....|...
gi 780224413 193 --EHGTTLVVVTH 203
Cdd:PRK00349 879 lvDKGNTVVVIEH 891
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
145-204 |
1.10e-03 |
|
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: 39.92 E-value: 1.10e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnrehGTTLVVVTHD 204
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDVETLRALEEALLNF----AGCAVVISHD 499
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
35-204 |
1.30e-03 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 38.12 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 35 SGETVALVGASGSGKSTllgllagldlpsqgdieiLGQSLLQLdeegrarLRAEQVGFVFqsflllptlsalenvmlpae 114
Cdd:smart00382 1 PGEVILIVGPPGSGKTT------------------LARALARE-------LGPPGGGVIY-------------------- 35
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780224413 115 LRGEtrcepRARELLAAVGLGERLHHLPPRLSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIEL-----LFE 189
Cdd:smart00382 36 IDGE-----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLLL 110
|
170
....*....|....*
gi 780224413 190 LNREHGTTLVVVTHD 204
Cdd:smart00382 111 LKSEKNLTVILTTND 125
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
145-206 |
1.85e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 39.24 E-value: 1.85e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780224413 145 LSGGEQQRVAIARAFMTrpSL------LlaDEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHE 206
Cdd:COG0178 486 LSGGEAQRIRLATQIGS--GLvgvlyvL--DEPSIGLHQRDNDRLIETLKRL-RDLGNTVIVVEHDED 548
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
145-217 |
2.63e-03 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 38.35 E-value: 2.63e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780224413 145 LSGGEQQRVAIARAFMTRPSLLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHD-HELAQRCQRQLVM 217
Cdd:PRK11288 397 LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFVSSDlPEVLGVADRIVVM 469
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
144-172 |
3.31e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 38.23 E-value: 3.31e-03
10 20
....*....|....*....|....*....
gi 780224413 144 RLSGGEQQRVAIARAFMTRPSLLLADEPT 172
Cdd:NF040905 404 NLSGGNQQKVVLSKWLFTDPDVLILDEPT 432
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
145-206 |
5.84e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 37.74 E-value: 5.84e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 780224413 145 LSGGEQQRVAIArafmtrpS---------LLLADEPTGNLDSKTGERVIELLFELnREHGTTLVVVTHDHE 206
Cdd:PRK00349 490 LSGGEAQRIRLA-------TqigsgltgvLYVLDEPSIGLHQRDNDRLIETLKHL-RDLGNTLIVVEHDED 552
|
|
| |
