|
Name |
Accession |
Description |
Interval |
E-value |
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
1-211 |
4.38e-120 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 339.46 E-value: 4.38e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQRIDMLPTAQRQIGI 80
Cdd:COG4136 1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTALPAEQRRIGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLLLALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:COG4136 81 LFQDDLLFPHLSVGENLAFALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 300840748 161 FSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDVPADSSVLDMAQWSE 211
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGNWQH 211
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-196 |
4.49e-53 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 173.75 E-value: 4.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTAQRQIG 79
Cdd:COG3842 5 ALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTL----LRMIAGFETPDsGRILLDGRDVTGLPPEKRNVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQFSVGQNLllALPSTLKGTA---RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:COG3842 81 MVFQDYALFPHLTVAENV--AFGLRMRGVPkaeIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 157 LDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQD 196
Cdd:COG3842 159 LDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEE 198
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
1-197 |
5.44e-52 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 167.24 E-value: 5.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLltNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAG-QFSCTGELWLNEQRIDMLPTAQRQIG 79
Cdd:COG3840 1 MLRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLN----LIAGfLPPDSGRILWNGQDLTALPPAERPVS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQFSVGQNLLLALPSTLKGTAR-RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:COG3840 75 MLFQENNLFPHLTVAQNIGLGLRPGLKLTAEqRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLD 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:COG3840 155 EPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDA 193
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
4-196 |
5.46e-52 |
|
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: 166.93 E-value: 5.46e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAG-QFSCTGELWLNEQRIDMLPTAQRQIGILF 82
Cdd:cd03259 3 LKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTL----LRLIAGlERPDSGEILIDGRDVTGVPPERRNIGMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLLLAL-PSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:cd03259 79 QDYALFPHLTVAENIAFGLkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPL 158
|
170 180 190
....*....|....*....|....*....|....*
gi 300840748 162 SRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQD 196
Cdd:cd03259 159 SALDAKLREELREELKELQRELGITTIYVTHDQEE 193
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
2-197 |
8.50e-49 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 162.62 E-value: 8.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAG-QFSCTGELWLNEQ--RIDmLPTAQRQI 78
Cdd:COG1118 3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLR----IIAGlETPDSGRIVLNGRdlFTN-LPPRERRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLALPSTLKGTARRNA-VKDALDR---AGLAETYhqdPATLSGGQRARVALLRALLAQPKA 154
Cdd:COG1118 78 GFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRArVEELLELvqlEGLADRY---PSQLSGGQRQRVALARALAVEPEV 154
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 155 LLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:COG1118 155 LLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEA 197
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-194 |
2.66e-48 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 158.71 E-value: 2.66e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESR----LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPtaq 75
Cdd:COG1116 7 ALELRGVSKRFPTGGggvtALDDVSLTVAAGEFVALVGPSGCGKSTLLR----LIAGLEKPTsGEVLVDGKPVTGPG--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 RQIGILFQDALLFDQFSVGQNLLLALP-STLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKA 154
Cdd:COG1116 80 PDRGVVFQEPALLPWLTVLDNVALGLElRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 155 LLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDV 199
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
2-193 |
6.18e-47 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 153.82 E-value: 6.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFS-CTGELWLNEQRIDMLPTAQ--RQI 78
Cdd:COG4619 1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLR----ALADLDPpTSGEIYLDGKPLSAMPPPEwrRQV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQfSVGQNLllALPSTLKG-TARRNAVKDALDRAGLAETY-HQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:COG4619 77 AYVPQEPALWGG-TVRDNL--PFPFQLRErKFDRERALELLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190
....*....|....*....|....*....|....*..
gi 300840748 157 LDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHD 190
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
4-194 |
1.17e-46 |
|
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: 153.40 E-value: 1.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRL----LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIdmlPTAQRQI 78
Cdd:cd03293 3 VRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLR----IIAGLERPTsGEVLVDGEPV---TGPGPDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLALpsTLKGTARRNA---VKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKAL 155
Cdd:cd03293 76 GYVFQQDALLPWLTVLDNVALGL--ELQGVPKAEArerAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 156 LLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:cd03293 154 LLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDI 192
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
4-195 |
1.74e-46 |
|
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: 153.03 E-value: 1.74e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLP----ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSctGELWLNEQRIDMLPTAQR--- 76
Cdd:cd03255 3 LKNLSKTYGgggeKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLN-ILGGLDRPTS--GEVRVDGTDISKLSEKELaaf 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 ---QIGILFQDALLFDQFSVGQNLLLAL-PSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQP 152
Cdd:cd03255 80 rrrHIGFVFQSFNLLPDLTALENVELPLlLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 153 KALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQ 195
Cdd:cd03255 160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE 202
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
1-197 |
4.31e-46 |
|
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: 156.03 E-value: 4.31e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVkNVSLRLPESRLltNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAG-------QFSCTGELWLNEQRIDMLPT 73
Cdd:COG4148 2 MLEV-DFRLRRGGFTL--DVDFTLPGRGVTALFGPSGSGKTTL----LRAIAGlerpdsgRIRLGGEVLQDSARGIFLPP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 74 AQRQIGILFQDALLFDQFSVGQNLLLALPSTLKGtARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPK 153
Cdd:COG4148 75 HRRRIGYVFQEARLFPHLSVRGNLLYGRKRAPRA-ERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPR 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 300840748 154 ALLLDEPFSRLDVALRDnfrqwvfsEV--------RELAIPVVQVTHDLQDV 197
Cdd:COG4148 154 LLLMDEPLAALDLARKA--------EIlpylerlrDELDIPILYVSHSLDEV 197
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
1-197 |
1.47e-45 |
|
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: 150.52 E-value: 1.47e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKnVSLRLPESRLltNVNFTVDkGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLN-EQRIDmLPTAQR 76
Cdd:cd03297 1 MLCVD-IEKRLPDFTL--KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEkpdGGTIVLNGTVLFDsRKKIN-LPPQQR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQFSVGQNLLLALPSTLKGTaRRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:cd03297 76 KIGLVFQQYALFPHLNVRENLAFGLKRKRNRE-DRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 300840748 157 LDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03297 155 LDEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEA 195
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-195 |
3.85e-44 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 147.11 E-value: 3.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLP----ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAgqfSCT-GELWLNEQRIDMLPTAQ 75
Cdd:COG1136 4 LLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLN-ILGGLD---RPTsGEVLIDGQDISSLSERE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 R------QIGILFQDALLFDQFSVGQNLllALPSTLKGTARRNA---VKDALDRAGLAETYHQDPATLSGGQRARVALLR 146
Cdd:COG1136 80 LarlrrrHIGFVFQFFNLLPELTALENV--ALPLLLAGVSRKERrerARELLERVGLGDRLDHRPSQLSGGQQQRVAIAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 300840748 147 ALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQ 195
Cdd:COG1136 158 ALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE 206
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-193 |
1.07e-43 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 149.45 E-value: 1.07e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIgalAGQFSCT-GELWLNEQRIDMLPTAQRQIG 79
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLR-MI---AGLEDPTsGEILIGGRDVTDLPPKDRNIA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQFSVGQNLLLALpsTLKGTA---RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:COG3839 79 MVFQSYALYPHMTVYENIAFPL--KLRKVPkaeIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 300840748 157 LDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:COG3839 157 LDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHD 193
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
4-193 |
1.37e-43 |
|
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: 145.84 E-value: 1.37e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFswMIgaLAG-QFSCTGELWLNEQRIDMLPTAQRQIGILF 82
Cdd:cd03300 3 LENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLL--RL--IAGfETPTSGEILLDGKDITNLPPHKRPVNTVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLllALPSTLKGTAR---RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:cd03300 79 QNYALFPHLTVFENI--AFGLRLKKLPKaeiKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156
|
170 180 190
....*....|....*....|....*....|....
gi 300840748 160 PFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:cd03300 157 PLGALDLKLRKDMQLELKRLQKELGITFVFVTHD 190
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
4-197 |
1.53e-43 |
|
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: 145.72 E-value: 1.53e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRIDMLPTAqRQIGI 80
Cdd:cd03261 3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLrpdSGEVLIDGEDISGLSEAELYRLR-RRMGM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLllALP----STLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:cd03261 82 LFQSGALFDSLTVFENV--AFPlrehTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 300840748 157 LDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTA 200
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-197 |
2.61e-42 |
|
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: 142.81 E-value: 2.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQRQ--- 77
Cdd:COG1127 5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD---SGEILVDGQDITGLSEKELYelr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 --IGILFQDALLFDQFSVGQNLllALP----STLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQ 151
Cdd:COG1127 82 rrIGMLFQGGALFDSLTVFENV--AFPlrehTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 300840748 152 PKALLLDEPFSRLD-VALRdnfrqwVFSE-----VRELAIPVVQVTHDLQDV 197
Cdd:COG1127 160 PEILLYDEPTAGLDpITSA------VIDElirelRDELGLTSVVVTHDLDSA 205
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
4-197 |
1.23e-40 |
|
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: 136.55 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGAL----AGQFSCTGELWLNEQRIdmLPTAQRQIG 79
Cdd:cd03229 3 LKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLR-CIAGLeepdSGSILIDGEDLTDLEDE--LPPLRRRIG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQFSVGQNLLLALpstlkgtarrnavkdaldraglaetyhqdpatlSGGQRARVALLRALLAQPKALLLDE 159
Cdd:cd03229 80 MVFQDFALFPHLTVLENIALGL---------------------------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 300840748 160 PFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEA 164
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-197 |
1.04e-39 |
|
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: 135.29 E-value: 1.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLP--ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ--RQIG 79
Cdd:cd03225 2 LKNLSFSYPdgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT---SGEVLVDGKDLTKLSLKElrRKVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDAllFDQF---SVGQNLLLALPS-TLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKAL 155
Cdd:cd03225 79 LVFQNP--DDQFfgpTVEEEVAFGLENlGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 300840748 156 LLDEPFSRLDVALRDNFRQWVfSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELL-KKLKAEGKTIIIVTHDLDLL 197
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
2-197 |
1.73e-39 |
|
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: 135.54 E-value: 1.73e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLtNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQRQIGIL 81
Cdd:cd03299 1 LKVENLSKDWKEFKLK-NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPD---SGKILLNGKDITNLPPEKRDISYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDALLFDQFSVGQNLLLALPSTLKGTARRNA-VKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:cd03299 77 PQNYALFPHMTVYKNIAYGLKKRKVDKKEIERkVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEP 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 300840748 161 FSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03299 157 FSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEA 193
|
|
| 3a0106s01 |
TIGR00968 |
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions] |
4-193 |
2.80e-39 |
|
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 134.93 E-value: 2.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAG-QFSCTGELWLNEQRIDMLPTAQRQIGILF 82
Cdd:TIGR00968 3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLR----IIAGlEQPDSGRIRLNGQDATRVHARDRKIGFVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLLLAL----PSTLKGTARRNAVKDALDRAGLAETYhqdPATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:TIGR00968 79 QHYALFKHLTVRDNIAFGLeirkHPKAKIKARVEELLELVQLEGLGDRY---PNQLSGGQRQRVALARALAVEPQVLLLD 155
|
170 180 190
....*....|....*....|....*....|....*
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:TIGR00968 156 EPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHD 190
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
1-194 |
8.10e-39 |
|
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: 134.40 E-value: 8.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQ--RQ 77
Cdd:COG1120 1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLR----ALAGLLKPSsGEVLLDGRDLASLSRRElaRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQFSVGQNLLLALPSTLKGTAR-----RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQP 152
Cdd:COG1120 77 IAYVPQEPPAPFGLTVRELVALGRYPHLGLFGRpsaedREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEP 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 153 KALLLDEPFSRLDVAlrdnFRQWVFSEVRELA----IPVVQVTHDL 194
Cdd:COG1120 157 PLLLLDEPTSHLDLA----HQLEVLELLRRLArergRTVVMVLHDL 198
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
23-196 |
9.15e-39 |
|
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: 133.00 E-value: 9.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 23 TVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFsctGELWLNEQRIDMLPTAQRQIGILFQDALLFDQFSVGQNLLLALP 102
Cdd:cd03298 20 TFAQGEITAIVGPSGSGKSTLLNLIAGFETPQS---GRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 103 STLKGTA-RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVR 181
Cdd:cd03298 97 PGLKLTAeDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176
|
170
....*....|....*
gi 300840748 182 ELAIPVVQVTHDLQD 196
Cdd:cd03298 177 ETKMTVLMVTHQPED 191
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
4-193 |
9.93e-39 |
|
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: 133.62 E-value: 9.93e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQRQIGILF 82
Cdd:cd03296 5 VRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLR----LIAGLERPDsGTILFGGEDATDVPVQERNVGFVF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLLLAL--------PSTLKGTARRNAVKDALDRAGLAETYhqdPATLSGGQRARVALLRALLAQPKA 154
Cdd:cd03296 81 QHYALFRHMTVFDNVAFGLrvkprserPPEAEIRAKVHELLKLVQLDWLADRY---PAQLSGGQRQRVALARALAVEPKV 157
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 155 LLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:cd03296 158 LLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHD 196
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-195 |
3.11e-38 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 131.71 E-value: 3.11e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTAQ--- 75
Cdd:COG2884 1 MIRFENVSKRYPGGREaLSDVSLEIEKGEFVFLTGPSGAGKSTL----LKLLYGEERPTsGQVLVNGQDLSRLKRREipy 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 --RQIGILFQDALLFDQFSVGQNLLLALpsTLKGTAR---RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLA 150
Cdd:COG2884 77 lrRRIGVVFQDFRLLPDRTVYENVALPL--RVTGKSRkeiRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 300840748 151 QPKALLLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQ 195
Cdd:COG2884 155 RPELLLADEPTGNLDPETSWEIME-LLEEINRRGTTVLIATHDLE 198
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
4-197 |
7.52e-38 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 131.34 E-value: 7.52e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRI-DMLPTAQRQIGILF 82
Cdd:COG1131 3 VRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---SGEVRVLGEDVaRDPAEVRRRIGYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLLLAlpSTLKG---TARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:COG1131 80 QEPALYPDLTVRENLRFF--ARLYGlprKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157
|
170 180 190
....*....|....*....|....*....|....*...
gi 300840748 160 PFSRLDVALRDNFRQWVFSEVRELAIpVVQVTHDLQDV 197
Cdd:COG1131 158 PTSGLDPEARRELWELLRELAAEGKT-VLLSTHYLEEA 194
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
4-193 |
1.13e-37 |
|
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: 130.07 E-value: 1.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIgalAGQFSCT-GELWLNEQRIDMLPTAQRQIGILF 82
Cdd:cd03301 3 LENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLR-MI---AGLEEPTsGRIYIGGRDVTDLPPKDRDIAMVF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLllALPSTLKGTARRN---AVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:cd03301 79 QNYALYPHMTVYDNI--AFGLKLRKVPKDEideRVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156
|
170 180 190
....*....|....*....|....*....|....
gi 300840748 160 PFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:cd03301 157 PLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHD 190
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
21-196 |
1.14e-37 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 130.86 E-value: 1.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 21 NFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRIDMLPTAQRQIGILFQDALLFDQFSVGQNLLLA 100
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLT---PASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 101 LPSTLKGTA-RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSE 179
Cdd:PRK10771 96 LNPGLKLNAaQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQV 175
|
170
....*....|....*..
gi 300840748 180 VRELAIPVVQVTHDLQD 196
Cdd:PRK10771 176 CQERQLTLLMVSHSLED 192
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-197 |
3.29e-37 |
|
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: 135.42 E-value: 3.29e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQRIDMLPTAQR-- 76
Cdd:COG1123 4 LLEVRDLSVRYPGGDvpAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALRgr 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALL-FDQFSVGQNLLLALP-STLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKA 154
Cdd:COG1123 84 RIGMVFQDPMTqLNPVTVGDQIAEALEnLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 155 LLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:COG1123 164 LIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVV 206
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
4-195 |
3.62e-37 |
|
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: 128.80 E-value: 3.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFsctGELWLNEQRIDM----LPTAQRQIG 79
Cdd:cd03262 3 IKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDS---GTIIIDGLKLTDdkknINELRQKVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQFSVGQNLLLAlPSTLKGTARRNAVK---DALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:cd03262 80 MVFQQFNLFPHLTVLENITLA-PIKVKGMSKAEAEEralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVML 158
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 300840748 157 LDEPFSRLDVALRDNfrqwVFSEVRELA---IPVVQVTHDLQ 195
Cdd:cd03262 159 FDEPTSALDPELVGE----VLDVMKDLAeegMTMVVVTHEMG 196
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-195 |
4.46e-37 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 129.34 E-value: 4.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAG--QFScTGELWLNEQRIDM----LPTA 74
Cdd:COG1126 1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTL----LRCINLleEPD-SGTITVDGEDLTDskkdINKL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 QRQIGILFQDALLFDQFSVGQNLLLAlPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQ 151
Cdd:COG1126 76 RRKVGMVFQQFNLFPHLTVLENVTLA-PIKVKKMSKAEAEERAmelLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 300840748 152 PKALLLDEPFSRLDVALRdnfrqwvfSEV----RELA---IPVVQVTHDLQ 195
Cdd:COG1126 155 PKVMLFDEPTSALDPELV--------GEVldvmRDLAkegMTMVVVTHEMG 197
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
4-197 |
5.37e-37 |
|
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: 128.99 E-value: 5.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLP-ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ--RQIGI 80
Cdd:COG1122 3 LENLSFSYPgGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT---SGEVLVDGKDITKKNLRElrRKVGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDAllFDQF---SVGQNLL-----LALPstlKGTARRnAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQP 152
Cdd:COG1122 80 VFQNP--DDQLfapTVEEDVAfgpenLGLP---REEIRE-RVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 300840748 153 KALLLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:COG1122 154 EVLVLDEPTAGLDPRGRRELLE-LLKRLNKEGKTVIIVTHDLDLV 197
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-209 |
7.83e-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: 127.60 E-value: 7.83e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFswmiGALAGQFSCT-GELWLNEQRIDMLP-TAQRQI 78
Cdd:COG4133 2 MLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLL----RILAGLLPPSaGEVLWNGEPIRDAReDYRRRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLAlpSTLKGT-ARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:COG4133 78 AYLGHADGLKPELTVRENLRFW--AALYGLrADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 300840748 158 DEPFSRLDVALRDNFRQWVFSEVRELAIpVVQVTHDLQDVPADsSVLDMAQW 209
Cdd:COG4133 156 DEPFTALDAAGVALLAELIAAHLARGGA-VLLTTHQPLELAAA-RVLDLGDF 205
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-195 |
1.44e-36 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 128.25 E-value: 1.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ---- 75
Cdd:COG3638 2 MLELRNLSKRYPGGTPaLDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGEILVDGQDVTALRGRAlrrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 -RQIGILFQDALLFDQFSVGQNLLL-ALP--STLKGTAR------RNAVKDALDRAGLAETYHQDPATLSGGQRARVALL 145
Cdd:COG3638 79 rRRIGMIFQQFNLVPRLSVLTNVLAgRLGrtSTWRSLLGlfppedRERALEALERVGLADKAYQRADQLSGGQQQRVAIA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 300840748 146 RALLAQPKALLLDEPFSRLDVALR----DNFRQwvfsEVRELAIPVVQVTHDLQ 195
Cdd:COG3638 159 RALVQEPKLILADEPVASLDPKTArqvmDLLRR----IAREDGITVVVNLHQVD 208
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-195 |
3.13e-36 |
|
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: 127.23 E-value: 3.13e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPES----RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQ 75
Cdd:COG1124 1 MLEVRNLSVSYGQGgrrvPVLKDVSLEVAPGESFGLVGESGSGKSTLLR----ALAGLERPWsGEVTFDGRPVTRRRRKA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 --RQIGILFQDALL-FD-QFSVGQnlLLALPSTLKGTARRNA-VKDALDRAGLAETY-HQDPATLSGGQRARVALLRALL 149
Cdd:COG1124 77 frRRVQMVFQDPYAsLHpRHTVDR--ILAEPLRIHGLPDREErIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARALI 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 300840748 150 AQPKALLLDEPFSRLDVALRdnfrqwvfSEV--------RELAIPVVQVTHDLQ 195
Cdd:COG1124 155 LEPELLLLDEPTSALDVSVQ--------AEIlnllkdlrEERGLTYLFVSHDLA 200
|
|
| modC_ABC |
TIGR02142 |
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ... |
6-197 |
8.02e-36 |
|
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: 129.08 E-value: 8.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 6 NVSLRLPESRLltNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLN-EQRIDmLPTAQRQIGIL 81
Cdd:TIGR02142 4 RFSKRLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTrpdEGEIVLNGRTLFDsRKGIF-LPPEKRRIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDALLFDQFSVGQNLLLALPSTlKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:TIGR02142 81 FQEARLFPHLSVRGNLRYGMKRA-RPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159
|
170 180 190
....*....|....*....|....*....|....*.
gi 300840748 162 SRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEV 195
|
|
| thiQ |
TIGR01277 |
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ... |
21-202 |
1.04e-35 |
|
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: 124.97 E-value: 1.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 21 NFTVDKGDIVTLMGPSGCGKSTLFSWMIGALagqFSCTGELWLNEQRIDMLPTAQRQIGILFQDALLFDQFSVGQNLLLA 100
Cdd:TIGR01277 18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFI---EPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 101 LPSTLKGTA-RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSE 179
Cdd:TIGR01277 95 LHPGLKLNAeQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQL 174
|
170 180
....*....|....*....|...
gi 300840748 180 VRELAIPVVQVTHDLQDVPADSS 202
Cdd:TIGR01277 175 CSERQRTLLMVTHHLSDARAIAS 197
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
17-162 |
1.21e-35 |
|
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: 122.76 E-value: 1.21e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRI--DMLPTAQRQIGILFQDALLFDQFSV 93
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLK----LIAGLLSPTeGTILLDGQDLtdDERKSLRKEIGYVFQDPQLFPRLTV 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300840748 94 GQNLLLALPSTLKGTARRNA-VKDALDRAGLAETYHQ----DPATLSGGQRARVALLRALLAQPKALLLDEPFS 162
Cdd:pfam00005 77 RENLRLGLLLKGLSKREKDArAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-194 |
3.92e-35 |
|
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.
Pssm-ID: 213181 [Multi-domain] Cd Length: 180 Bit Score: 122.54 E-value: 3.92e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFS-CTGELWLNEQRIDMLPTAQ--RQIGI 80
Cdd:cd03214 2 VENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLK----TLAGLLKpSSGEILLDGKDLASLSPKElaRKIAY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQdallfdqfsvgqnlllalpstlkgtarrnavkdALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:cd03214 78 VPQ---------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124
|
170 180 190
....*....|....*....|....*....|....
gi 300840748 161 FSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:cd03214 125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDL 158
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
5-193 |
4.11e-35 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 127.45 E-value: 4.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSctGELWLNEQRIDMLPTAQRQIGILFQD 84
Cdd:PRK11000 7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLR-MIAGLEDITS--GDLFIGEKRMNDVPPAERGVGMVFQS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 85 ALLFDQFSVGQNLLLALpsTLKGTA------RRNAVKDALDRAGLAEtyhQDPATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:PRK11000 84 YALYPHLSVAENMSFGL--KLAGAKkeeinqRVNQVAEVLQLAHLLD---RKPKALSGGQRQRVAIGRTLVAEPSVFLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:PRK11000 159 EPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHD 193
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-193 |
5.81e-35 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 126.76 E-value: 5.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQRQIGI 80
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLR----LVAGLEKPTeGQIFIDGEDVTHRSIQQRDICM 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNL-----LLALPSTlkgtARRNAVKDAL---DRAGLAETYHQDpatLSGGQRARVALLRALLAQP 152
Cdd:PRK11432 83 VFQSYALFPHMSLGENVgyglkMLGVPKE----ERKQRVKEALelvDLAGFEDRYVDQ---ISGGQQQRVALARALILKP 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 300840748 153 KALLLDEPFSRLDVALRDNFRQwvfsEVREL----AIPVVQVTHD 193
Cdd:PRK11432 156 KVLLFDEPLSNLDANLRRSMRE----KIRELqqqfNITSLYVTHD 196
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-194 |
7.40e-35 |
|
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: 123.38 E-value: 7.40e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPES----RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALA---GQFSCTGELWLNEQRiDMLPT 73
Cdd:cd03257 1 LLEVKNLSVSFPTGggsvKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKptsGSIIFDGKDLLKLSR-RLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 74 AQRQIGILFQDAL--LFDQFSVGQNL---LLALPSTLKGTARRNAVKDALDRAGLAETY-HQDPATLSGGQRARVALLRA 147
Cdd:cd03257 80 RRKEIQMVFQDPMssLNPRMTIGEQIaepLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 300840748 148 LLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:cd03257 160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDL 206
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
5-196 |
1.23e-34 |
|
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: 123.18 E-value: 1.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSctGELWLNEQRIDMLPTAQ--RQIGIL 81
Cdd:cd03295 4 ENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMK-MINRLIEPTS--GEIFIDGEDIREQDPVElrRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDALLFDQFSVGQNLLLaLPSTLK-GTARRNA-VKDA-----LDRAGLAETYhqdPATLSGGQRARVALLRALLAQPKA 154
Cdd:cd03295 81 IQQIGLFPHMTVEENIAL-VPKLLKwPKEKIRErADELlalvgLDPAEFADRY---PHELSGGQQQRVGVARALAADPPL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 300840748 155 LLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQD 196
Cdd:cd03295 157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDE 198
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-195 |
2.89e-34 |
|
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: 122.29 E-value: 2.89e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRI-----DMLPTAQRQ 77
Cdd:cd03256 3 VENLSKTYPNGKkALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDInklkgKALRQLRRQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQFSVGQNLL---LALPSTLKGTARRNAVKD------ALDRAGLAETYHQDPATLSGGQRARVALLRAL 148
Cdd:cd03256 80 IGMIFQQFNLIERLSVLENVLsgrLGRRSTWRSLFGLFPKEEkqralaALERVGLLDKAYQRADQLSGGQQQRVAIARAL 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 300840748 149 LAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQ 195
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVD 206
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-195 |
5.53e-34 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 121.35 E-value: 5.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSctGELWLNEQRIDMLPTAQRQI-- 78
Cdd:PRK09493 1 MIEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLR-CINKLEEITS--GDLIVDGLKVNDPKVDERLIrq 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 --GILFQDALLFDQFSVGQNLLLAlPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQPK 153
Cdd:PRK09493 78 eaGMVFQQFYLFPHLTALENVMFG-PLRVRGASKEEAEKQArelLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPK 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 300840748 154 ALLLDEPFSRLDVALrdnfRQWVFSEVRELA---IPVVQVTHDLQ 195
Cdd:PRK09493 157 LMLFDEPTSALDPEL----RHEVLKVMQDLAeegMTMVIVTHEIG 197
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
4-197 |
1.28e-33 |
|
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: 118.27 E-value: 1.28e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgQFSctGELWLNEQRIDMLPT-AQRQIGILF 82
Cdd:cd03230 3 VRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLK-PDS--GEIKVLGKDIKKEPEeVKRRIGYLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLllalpstlkgtarrnavkdaldraglaetyhqdpaTLSGGQRARVALLRALLAQPKALLLDEPFS 162
Cdd:cd03230 80 EEPSLYENLTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190
....*....|....*....|....*....|....*
gi 300840748 163 RLDVALRDNFRQWVFSEVRELAIpVVQVTHDLQDV 197
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKT-ILLSSHILEEA 158
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-199 |
1.84e-33 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 120.19 E-value: 1.84e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDmlpTAQRQIGI 80
Cdd:COG1121 6 AIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT---SGTVRLFGKPPR---RARRRIGY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQF--SVGQNLLLALPSTLK-----GTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPK 153
Cdd:COG1121 80 VPQRAEVDWDFpiTVRDVVLMGRYGRRGlfrrpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPD 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 154 ALLLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDVPA 199
Cdd:COG1121 160 LLLLDEPFAGVDAATEEALYE-LLRELRREGKTILVVTHDLGAVRE 204
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-208 |
2.08e-33 |
|
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: 125.65 E-value: 2.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ--RQ 77
Cdd:COG4987 334 LELEDVSFRYPGAGrpVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ---SGSITLGGVDLRDLDEDDlrRR 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQfSVGQNLLLALPstlkgTARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALLR 146
Cdd:COG4987 411 IAVVPQRPHLFDT-TLRENLRLARP-----DATDEELWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300840748 147 ALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAipVVQVTHDLQDVPADSSVLDMAQ 208
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRT--VLLITHRLAGLERMDRILVLED 544
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-193 |
3.44e-33 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 122.36 E-value: 3.44e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIgalAGQFSCT-GELWLNEQRIDMLPTAQRQIGI 80
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLR-LI---AGFETPDsGRIMLDGQDITHVPAENRHVNT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLLLALpsTLKGTAR---RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:PRK09452 91 VFQSYALFPHMTVFENVAFGL--RMQKTPAaeiTPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168
|
170 180 190
....*....|....*....|....*....|....*.
gi 300840748 158 DEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKLGITFVFVTHD 204
|
|
| tungstate_WtpC |
NF040840 |
tungstate ABC transporter ATP-binding protein WtpC; |
1-196 |
4.93e-33 |
|
tungstate ABC transporter ATP-binding protein WtpC;
Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 121.34 E-value: 4.93e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLlTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALagqFSCTGELWLNEQRIDMLPTAQRQIGI 80
Cdd:NF040840 1 MIRIENLSKDWKEFKL-RDISLEVKEGEYFIILGPSGAGKTVLLELIAGIW---PPDSGKIYLDGKDITNLPPEKRGIAY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLLLALpsTLKGTARRN---AVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:NF040840 77 VYQNYMLFPHKTVFENIAFGL--KLRKVPKEEierKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLL 154
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 158 DEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQD 196
Cdd:NF040840 155 DEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEE 193
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-197 |
8.76e-33 |
|
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: 117.92 E-value: 8.76e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQR-QIGIL 81
Cdd:cd03219 3 VRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFN----LISGFLRPTsGSVLFDGEDITGLPPHEIaRLGIG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 --FQDALLFDQFSVGQNLLLALPSTLKGTAR-----------RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRAL 148
Cdd:cd03219 79 rtFQIPRLFPELTVLENVMVAAQARTGSGLLlararreereaRERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 300840748 149 LAQPKALLLDEPFSRLDVALRDNFRQWVfSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03219 159 ATDPKLLLLDEPAAGLNPEETEELAELI-RELRERGITVLLVEHDMDVV 206
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
4-195 |
1.93e-32 |
|
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: 116.90 E-value: 1.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSC--TGELWLNEQRI---DMLPTA-QRQ 77
Cdd:cd03260 3 LRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGApdEGEVLLDGKDIydlDVDVLElRRR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDqFSVGQNLLLALPstLKGTARRNA----VKDALDRAGLAETYH--QDPATLSGGQRARVALLRALLAQ 151
Cdd:cd03260 83 VGMVFQKPNPFP-GSIYDNVAYGLR--LHGIKLKEElderVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 300840748 152 PKALLLDEPFSRLD-VALRDnfrqwVFSEVRELA--IPVVQVTHDLQ 195
Cdd:cd03260 160 PEVLLLDEPTSALDpISTAK-----IEELIAELKkeYTIVIVTHNMQ 201
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
19-193 |
2.76e-32 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 120.33 E-value: 2.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAG-QFSCTGELWLNEQRIDMLPTAQRQIGILFQDALLFDQFSVGQNL 97
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLR----MLAGfEQPTAGQIMLDGVDLSHVPPYQRPINMMFQSYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 98 LLALPS-TLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWV 176
Cdd:PRK11607 113 AFGLKQdKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDRMQLEV 192
|
170
....*....|....*..
gi 300840748 177 FSEVRELAIPVVQVTHD 193
Cdd:PRK11607 193 VDILERVGVTCVMVTHD 209
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-208 |
3.97e-32 |
|
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: 121.79 E-value: 3.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTA--QRQ 77
Cdd:COG4988 337 IELEDVSFSYPGGRpALDGLSLTIPPGERVALVGPSGAGKSTL----LNLLLGFLPPYsGSILINGVDLSDLDPAswRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQfSVGQNLLLALPstlkgTARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALLR 146
Cdd:COG4988 413 IAWVPQNPYLFAG-TIRENLRLGRP-----DASDEELEAALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALAR 486
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300840748 147 ALLAQPKALLLDEPFSRLDVALrdnfRQWVFSEVRELAI--PVVQVTHDLQDVPADSSVLDMAQ 208
Cdd:COG4988 487 ALLRDAPLLLLDEPTAHLDAET----EAEILQALRRLAKgrTVILITHRLALLAQADRILVLDD 546
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-197 |
4.93e-32 |
|
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: 121.16 E-value: 4.93e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPES-----RLLTNVNFTVDKGDIVTLMGPSGCGKSTLfSWMIGALAGQFSctGELWLNEQRIDMLPTAQ 75
Cdd:COG1123 260 LLEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTL-ARLLLGLLRPTS--GSILFDGKDLTKLSRRS 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 -----RQIGILFQD--ALLFDQFSVGQNLL--LALPSTLKGTARRNAVKDALDRAGL-AETYHQDPATLSGGQRARVALL 145
Cdd:COG1123 337 lrelrRRVQMVFQDpySSLNPRMTVGDIIAepLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIA 416
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 300840748 146 RALLAQPKALLLDEPFSRLDVALR----DNFRQWvfseVRELAIPVVQVTHDLQDV 197
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQaqilNLLRDL----QRELGLTYLFISHDLAVV 468
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-197 |
5.58e-32 |
|
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: 114.02 E-value: 5.58e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPES--RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTA--QR 76
Cdd:cd03228 1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLK----LLLRLYDPTsGEILIDGVDLRDLDLEslRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQfSVGQNLllalpstlkgtarrnavkdaldraglaetyhqdpatLSGGQRARVALLRALLAQPKALL 156
Cdd:cd03228 77 NIAYVPQDPFLFSG-TIRENI------------------------------------LSGGQRQRIAIARALLRDPPILI 119
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 300840748 157 LDEPFSRLDVALRDNFRQWVFSEVRELAipVVQVTHDLQDV 197
Cdd:cd03228 120 LDEATSALDPETEALILEALRALAKGKT--VIVIAHRLSTI 158
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
17-196 |
8.55e-32 |
|
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: 115.64 E-value: 8.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSctGELWLNEQRIDMlPTAQRQIgiLFQDALLFDQFSVGQN 96
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLN-LISGLAQPTS--GGVILEGKQITE-PGPDRMV--VFQNYSLLPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 97 LLLALPS---TLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFR 173
Cdd:TIGR01184 75 IALAVDRvlpDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQ 154
|
170 180
....*....|....*....|...
gi 300840748 174 QWVFSEVRELAIPVVQVTHDLQD 196
Cdd:TIGR01184 155 EELMQIWEEHRVTVLMVTHDVDE 177
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
4-193 |
9.57e-32 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 118.26 E-value: 9.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSctGELWLNEQRIDMLPTAQRQIGILFQ 83
Cdd:PRK10851 5 IANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLR-IIAGLEHQTS--GHIRFHGTDVSRLHARDRKVGFVFQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 84 DALLFDQFSVGQNL---LLALP--STLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:PRK10851 82 HYALFRHMTVFDNIafgLTVLPrrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161
|
170 180 190
....*....|....*....|....*....|....*
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHD 196
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
3-197 |
1.88e-31 |
|
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: 112.34 E-value: 1.88e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 3 CVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQ-FSCTGELWLNEQRI--DMLPTAQRQIG 79
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLR----AIAGLlKPTSGEILIDGKDIakLPLEELRRRIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQdallfdqfsvgqnlllalpstlkgtarrnavkdaldraglaetyhqdpatLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:cd00267 77 YVPQ--------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190
....*....|....*....|....*....|....*...
gi 300840748 160 PFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:cd00267 107 PTSGLDPASRERLLE-LLRELAEEGRTVIIVTHDPELA 143
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
1-194 |
3.05e-31 |
|
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: 114.75 E-value: 3.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQR-QI 78
Cdd:COG0411 4 LLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFN----LITGFYRPTsGRILFDGRDITGLPPHRIaRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GIL--FQDALLFDQFSVGQNLLLALPSTLKGT----------------ARRNAVKDALDRAGLAETYHQDPATLSGGQRA 140
Cdd:COG0411 80 GIArtFQNPRLFPELTVLENVLVAAHARLGRGllaallrlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQR 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 300840748 141 RVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:COG0411 160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDM 213
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-165 |
3.87e-31 |
|
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: 113.79 E-value: 3.87e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL-AGQfsctGELWLNEQRIDMLPT---AQRQ 77
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkPDS----GKILLDGQDITKLPMhkrARLG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQFSVGQNLLLALPSTLKGTA-RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:cd03218 77 IGYLPQEASIFRKLTVEENILAVLEIRGLSKKeREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
|
....*....
gi 300840748 157 LDEPFSRLD 165
Cdd:cd03218 157 LDEPFAGVD 165
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-193 |
4.42e-31 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 114.57 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESR----LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMlPTAQR 76
Cdd:COG4525 3 MLTVRHVSVRYPGGGqpqpALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVPVTG-PGADR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 qiGILFQDALLFDQFSVGQNLllALPSTLKG---TARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPK 153
Cdd:COG4525 79 --GVVFQKDALLPWLNVLDNV--AFGLRLRGvpkAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 154 ALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:COG4525 155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHS 194
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-196 |
1.15e-30 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 113.26 E-value: 1.15e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMlPTAQRqiGI 80
Cdd:PRK11248 1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVEG-PGAER--GV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLLLALpsTLKGTA---RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:PRK11248 75 VFQNEGLLPWRNVQDNVAFGL--QLAGVEkmqRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLL 152
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 158 DEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQD 196
Cdd:PRK11248 153 DEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEE 191
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-197 |
1.53e-30 |
|
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: 112.64 E-value: 1.53e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFswmiGALAGQFSCT-GELWLNEQRIDMLP-TAQRQI 78
Cdd:COG4555 1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLL----RMLAGLLKPDsGSILIDGEDVRKEPrEARRQI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNL-LLALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:COG4555 77 GVLPDERGLYDRLTVRENIrYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 158 DEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:COG4555 157 DEPTNGLDVMARRLLRE-ILRALKKEGKTVLFSSHIMQEV 195
|
|
| potA |
TIGR01187 |
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ... |
32-193 |
2.21e-30 |
|
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: 114.13 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 32 LMGPSGCGKSTLFSWMIGALAGQFsctGELWLNEQRIDMLPTAQRQIGILFQDALLFDQFSVGQNLllALPSTLKGTAR- 110
Cdd:TIGR01187 1 LLGPSGCGKTTLLRLLAGFEQPDS---GSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENV--AFGLKMRKVPRa 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 111 --RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVV 188
Cdd:TIGR01187 76 eiKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFV 155
|
....*
gi 300840748 189 QVTHD 193
Cdd:TIGR01187 156 FVTHD 160
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-199 |
1.85e-29 |
|
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: 108.77 E-value: 1.85e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFS-CTGELWLNEQRIDMlptAQRQIGILF 82
Cdd:cd03235 2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLK----AILGLLKpTSGSIRVFGKPLEK---ERKRIGYVP 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQF--SVGQNLLLALPSTLK-----GTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKAL 155
Cdd:cd03235 75 QRRSIDRDFpiSVRDVVLMGLYGHKGlfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 300840748 156 LLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDVPA 199
Cdd:cd03235 155 LLDEPFAGVDPKTQEDIYE-LLRELRREGMTILVVTHDLGLVLE 197
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-165 |
2.19e-29 |
|
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: 109.70 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLF---SWMIGALAGQFSCTGELWLNEQRIDmLPTAQR 76
Cdd:TIGR02315 1 MLEVENLSKVYPNGKqALKNINLNINPGEFVAIIGPSGAGKSTLLrciNRLVEPSSGSILLEGTDITKLRGKK-LRKLRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQFSVGQNLL---LALPSTLKGTARRNAVKD------ALDRAGLAETYHQDPATLSGGQRARVALLRA 147
Cdd:TIGR02315 80 RIGMIFQHYNLIERLTVLENVLhgrLGYKPTWRSLLGRFSEEDkeralsALERVGLADKAYQRADQLSGGQQQRVAIARA 159
|
170
....*....|....*...
gi 300840748 148 LLAQPKALLLDEPFSRLD 165
Cdd:TIGR02315 160 LAQQPDLILADEPIASLD 177
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-167 |
3.79e-29 |
|
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: 114.16 E-value: 3.79e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFS-CTGELWLNEQRIDMLPTAQ--R 76
Cdd:COG2274 474 IELENVSFRYPGDSppVLDNISLTIKPGERVAIVGRSGSGKSTLLK----LLLGLYEpTSGRILIDGIDLRQIDPASlrR 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQfSVGQNLLLALPstlkgTARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALL 145
Cdd:COG2274 550 QIGVVLQDVFLFSG-TIRENITLGDP-----DATDEEIIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIA 623
|
170 180
....*....|....*....|..
gi 300840748 146 RALLAQPKALLLDEPFSRLDVA 167
Cdd:COG2274 624 RALLRNPRILILDEATSALDAE 645
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-197 |
1.72e-28 |
|
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: 106.90 E-value: 1.72e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVS----LRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALagQFSCTGELWLNEQRIDMLP---- 72
Cdd:cd03258 1 MIELKNVSkvfgDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIR-CINGL--ERPTSGSVLVDGTDLTLLSgkel 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 73 -TAQRQIGILFQDALLFDQFSVGQNLllALPSTLKGTARRNA---VKDALDRAGLAETYHQDPATLSGGQRARVALLRAL 148
Cdd:cd03258 78 rKARRRIGMIFQHFNLLSSRTVFENV--ALPLEIAGVPKAEIeerVLELLELVGLEDKADAYPAQLSGGQKQRVGIARAL 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 300840748 149 LAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03258 156 ANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVV 204
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
20-193 |
2.32e-28 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 109.16 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 20 VNFTVDKGDIVTLMGPSGCGKSTLFSwMIgalAGQFSCT-GELWLNEQRIDMLPTAQRQIGILFQDALLFDQFSVGQNLL 98
Cdd:PRK11650 23 IDLDVADGEFIVLVGPSGCGKSTLLR-MV---AGLERITsGEIWIGGRVVNELEPADRDIAMVFQNYALYPHMSVRENMA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 99 LALpsTLKGTAR---RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRqw 175
Cdd:PRK11650 99 YGL--KIRGMPKaeiEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKLRVQMR-- 174
|
170 180
....*....|....*....|..
gi 300840748 176 vfSEV----RELAIPVVQVTHD 193
Cdd:PRK11650 175 --LEIqrlhRRLKTTSLYVTHD 194
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
1-193 |
3.01e-28 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 105.95 E-value: 3.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLP--TAQRQI 78
Cdd:PRK10247 7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT---SGTLLFEGEDISTLKpeIYRQQV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQfSVGQNLLLalPSTLKGTA-RRNAVKDALDRAGLAETYHQDPAT-LSGGQRARVALLRALLAQPKALL 156
Cdd:PRK10247 84 SYCAQTPTLFGD-TVYDNLIF--PWQIRNQQpDPAIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLL 160
|
170 180 190
....*....|....*....|....*....|....*..
gi 300840748 157 LDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
2-161 |
6.60e-28 |
|
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: 105.21 E-value: 6.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRIDMLPTAQR-QIGI 80
Cdd:cd03224 1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLP---PRSGSIRFDGRDITGLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LF--QDALLFDQFSVGQNLLLALpstlkGTARRNAVKDALDRA-----GLAETYHQDPATLSGGQRARVALLRALLAQPK 153
Cdd:cd03224 78 GYvpEGRRIFPELTVEENLLLGA-----YARRRAKRKARLERVyelfpRLKERRKQLAGTLSGGEQQMLAIARALMSRPK 152
|
....*...
gi 300840748 154 ALLLDEPF 161
Cdd:cd03224 153 LLLLDEPS 160
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-165 |
1.36e-27 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 104.73 E-value: 1.36e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIgalAGQFSCT-GELWLNEQRIDMLPT---AQR 76
Cdd:COG1137 3 TLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFY-MI---VGLVKPDsGRIFLDGEDITHLPMhkrARL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQFSVGQNLLLAL-PSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKAL 155
Cdd:COG1137 79 GIGYLPQEASIFRKLTVEDNILAVLeLRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158
|
170
....*....|
gi 300840748 156 LLDEPFSRLD 165
Cdd:COG1137 159 LLDEPFAGVD 168
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
19-194 |
1.50e-27 |
|
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: 105.42 E-value: 1.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIGALAGQFSCTGELWLNEQRIDMLPTAQRQIGILFQDALLFDQFSVGQ 95
Cdd:cd03294 42 DVSLDVREGEIFVIMGLSGSGKSTLlrcINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLE 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 96 NLllALPSTLKGTA---RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNF 172
Cdd:cd03294 122 NV--AFGLEVQGVPraeREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREM 199
|
170 180
....*....|....*....|..
gi 300840748 173 RQWVFSEVRELAIPVVQVTHDL 194
Cdd:cd03294 200 QDELLRLQAELQKTIVFITHDL 221
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
4-193 |
1.51e-27 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 104.71 E-value: 1.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIGALAGQFSCTGELW-----LNEQRIDMLptaQ 75
Cdd:PRK11124 5 LNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLlrvLNLLEMPRSGTLNIAGNHFdfsktPSDKAIREL---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 RQIGILFQDALLFDQFSVGQNLLLAlPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQP 152
Cdd:PRK11124 82 RNVGMVFQQYNLWPHLTVQQNLIEA-PCRVLGLSKDQALARAeklLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 300840748 153 KALLLDEPFSRLDVALRDNfrqwVFSEVRELA---IPVVQVTHD 193
Cdd:PRK11124 161 QVLLFDEPTAALDPEITAQ----IVSIIRELAetgITQVIVTHE 200
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
2-193 |
1.71e-27 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 104.76 E-value: 1.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFsCTGELWLNEQRIDmlptaqrqI 78
Cdd:PRK11247 13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGletPSAGEL-LAGTAPLAEARED--------T 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLALpstlKGTARRNAvKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:PRK11247 84 RLMFQDARLLPWKKVIDNVGLGL----KGQWRDAA-LQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLD 158
|
170 180 190
....*....|....*....|....*....|....*
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD 193
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-165 |
2.52e-27 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 108.71 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQ--RQ 77
Cdd:COG1132 340 IEFENVSFSYPGDRpVLKDISLTIPPGETVALVGPSGSGKSTLVN----LLLRFYDPTsGRILIDGVDIRDLTLESlrRQ 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDqFSVGQNLLLALPstlkgTARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALLR 146
Cdd:COG1132 416 IGVVPQDTFLFS-GTIRENIRYGRP-----DATDEEVEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIAR 489
|
170
....*....|....*....
gi 300840748 147 ALLAQPKALLLDEPFSRLD 165
Cdd:COG1132 490 ALLKDPPILILDEATSALD 508
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
5-193 |
2.89e-27 |
|
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: 103.26 E-value: 2.89e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMigaLAGQFSCTGELWLNEQRIDML-----PTAQRQI 78
Cdd:cd03292 4 INVTKTYPNGTAaLDGINISISAGEFVFLVGPSGAGKSTLLKLI---YKEELPTSGTIRVNGQDVSDLrgraiPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLALPST-LKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:cd03292 81 GVVFQDFRLLPDRNVYENVAFALEVTgVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 300840748 158 DEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHD 193
Cdd:cd03292 161 DEPTGNLDPDTTWEIMN-LLKKINKAGTTVVVATHA 195
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
4-194 |
5.78e-27 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 103.17 E-value: 5.78e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIGALAGQFSCTGELW-----LNEQRIDMLptaQ 75
Cdd:COG4161 5 LKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLlrvLNLLETPDSGQLNIAGHQFdfsqkPSEKAIRLL---R 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 RQIGILFQDALLFDQFSVGQNLLLAlPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQP 152
Cdd:COG4161 82 QKVGMVFQQYNLWPHLTVMENLIEA-PCKVLGLSKEQAREKAmklLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEP 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 300840748 153 KALLLDEPFSRLDVALRDNfrqwVFSEVRELA---IPVVQVTHDL 194
Cdd:COG4161 161 QVLLFDEPTAALDPEITAQ----VVEIIRELSqtgITQVIVTHEV 201
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
2-197 |
6.03e-27 |
|
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: 102.27 E-value: 6.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGdIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTAQRQ-IG 79
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTL----MRILATLTPPSsGTIRIDGQDVLKQPQKLRRrIG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQFSVGQnlLLALPSTLKGTARRNA---VKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:cd03264 76 YLPQEFGVYPNFTVRE--FLDYIAWLKGIPSKEVkarVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 300840748 157 LDEPFSRLDVALRDNFRQwVFSEVRELAIpVVQVTHDLQDV 197
Cdd:cd03264 154 VDEPTAGLDPEERIRFRN-LLSELGEDRI-VILSTHIVEDV 192
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-197 |
2.54e-26 |
|
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: 101.04 E-value: 2.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLT--NVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFS-CTGELWLNEQRIDMLPTAQRQ- 77
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAvdDLSLNVYKGEIFGLLGHNGAGKTTTLK----MLTGELRpTSGTAYINGYSIRTDRKAARQs 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQFSVGQNLLL-ALpstLKG---TARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPK 153
Cdd:cd03263 77 LGYCPQFDALFDELTVREHLRFyAR---LKGlpkSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 300840748 154 ALLLDEPFSRLDVALRDNFRQWVFSEVRELAIpvVQVTHDLQDV 197
Cdd:cd03263 154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEA 195
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-194 |
2.98e-26 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 101.77 E-value: 2.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTAQ--RQ 77
Cdd:PRK13548 2 MLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTL----LRALSGELSPDsGEVRLNGRPLADWSPAElaRR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALL-FDqFSVGQNLLL-ALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRAlLAQ---- 151
Cdd:PRK13548 78 RAVLPQHSSLsFP-FTVEEVVAMgRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARV-LAQlwep 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 152 ---PKALLLDEPFSRLDVAlrdnFRQWVFSEVRELAIP----VVQVTHDL 194
Cdd:PRK13548 156 dgpPRWLLLDEPTSALDLA----HQHHVLRLARQLAHErglaVIVVLHDL 201
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
1-160 |
3.63e-26 |
|
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: 100.83 E-value: 3.63e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQR-QIG 79
Cdd:COG0410 3 MLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR---SGSIRFDGEDITGLPPHRIaRLG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILF--QDALLFDQFSVGQNLLLALpstlKGTARRNAVKDALDRAG-----LAETYHQDPATLSGGQRARVALLRALLAQP 152
Cdd:COG0410 80 IGYvpEGRRIFPSLTVEENLLLGA----YARRDRAEVRADLERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRP 155
|
....*...
gi 300840748 153 KALLLDEP 160
Cdd:COG0410 156 KLLLLDEP 163
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-196 |
3.80e-26 |
|
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase component [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 443338 [Multi-domain] Cd Length: 233 Bit Score: 100.59 E-value: 3.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESR----LLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTAQ 75
Cdd:COG4181 8 IIELRGLTKTVGTGAgeltILKGISLEVEAGESVAIVGASGSGKSTL----LGLLAGLDRPTsGTVRLAGQDLFALDEDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 R------QIGILFQDALLFDQFSVGQNLllALPSTLKGT--ARRNAvKDALDRAGLAETYHQDPATLSGGQRARVALLRA 147
Cdd:COG4181 84 RarlrarHVGFVFQSFQLLPTLTALENV--MLPLELAGRrdARARA-RALLERVGLGHRLDHYPAQLSGGEQQRVALARA 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 300840748 148 LLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQD 196
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPAL 209
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
3.92e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 105.06 E-value: 3.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTA--QRQ 77
Cdd:TIGR02857 322 LEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTL----LNLLLGFVDPTeGSIAVNGVPLADADADswRDQ 397
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQfSVGQNLLLALPStlkgtARRNAVKDALDRAGLAE-------TYH----QDPATLSGGQRARVALLR 146
Cdd:TIGR02857 398 IAWVPQHPFLFAG-TIAENIRLARPD-----ASDAEIREALERAGLDEfvaalpqGLDtpigEGGAGLSGGQAQRLALAR 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300840748 147 ALLAQPKALLLDEPFSRLDVALrdnfRQWVFSEVRELA--IPVVQVTHDLQDVPADSSVLDM 206
Cdd:TIGR02857 472 AFLRDAPLLLLDEPTAHLDAET----EAEVLEALRALAqgRTVLLVTHRLALAALADRIVVL 529
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-194 |
5.07e-26 |
|
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: 104.75 E-value: 5.07e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPES-RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ--RQI 78
Cdd:TIGR02868 335 LELRDLSAGYPGApPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVPVSSLDQDEvrRRV 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQfSVGQNLLLAlpstlKGTARRNAVKDALDRAGLAE-----------TYHQDPATLSGGQRARVALLRA 147
Cdd:TIGR02868 412 SVCAQDAHLFDT-TVRENLRLA-----RPDATDEELWAALERVGLADwlralpdgldtVLGEGGARLSGGERQRLALARA 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 300840748 148 LLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAipVVQVTHDL 194
Cdd:TIGR02868 486 LLADAPILLLDEPTEHLDAETADELLEDLLAALSGRT--VVLITHHL 530
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-166 |
5.08e-26 |
|
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: 104.77 E-value: 5.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLfswmiG-ALAGQFSCTGELWLNEQRIDMLPTAQ-----RQIGILFQD--ALLFDQ 90
Cdd:COG4172 304 GVSLTLRRGETLGLVGESGSGKSTL-----GlALLRLIPSEGEIRFDGQDLDGLSRRAlrplrRRMQVVFQDpfGSLSPR 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 91 FSVGQNL---LLALPSTLKGTARRNAVKDALDRAGL-AETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:COG4172 379 MTVGQIIaegLRVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDV 458
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-196 |
6.77e-26 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 100.93 E-value: 6.77e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLP-----ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFswmiGALAGQFSCT-GELWLNEQRIDMLPTA 74
Cdd:COG1101 1 MLELKNLSKTFNpgtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLL----NAIAGSLPPDsGSILIDGKDVTKLPEY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 QR--QIGILFQDALL--FDQFSVGQNLLLALpstLKG----------TARRNAVKDALDRAGLA-ETYHQDPA-TLSGGQ 138
Cdd:COG1101 77 KRakYIGRVFQDPMMgtAPSMTIEENLALAY---RRGkrrglrrgltKKRRELFRELLATLGLGlENRLDTKVgLLSGGQ 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300840748 139 RARVALLRALLAQPKALLLDEPFSRLD-------VALRDNFrqwvfseVRELAIPVVQVTHDLQD 196
Cdd:COG1101 154 RQALSLLMATLTKPKLLLLDEHTAALDpktaalvLELTEKI-------VEENNLTTLMVTHNMEQ 211
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-194 |
8.92e-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: 99.25 E-value: 8.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPES-RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAG-QFSCTGELWLNEQRIDmLPTAQRQIGIL 81
Cdd:cd03226 2 IENISFSYKKGtEILDDLSLDLYAGEIIALTGKNGAGKTTLAK----ILAGlIKESSGSILLNGKPIK-AKERRKSIGYV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDalLFDQF---SVGQNLLLALPSTLKGTARRNAVKDALDRAGLAEtyhQDPATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:cd03226 77 MQD--VDYQLftdSVREELLLGLKELDAGNEQAETVLKDLDLYALKE---RHPLSLSGGQKQRLAIAAALLSGKDLLIFD 151
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 159 EPFSRLDvalRDNFRQwVFSEVRELA---IPVVQVTHDL 194
Cdd:cd03226 152 EPTSGLD---YKNMER-VGELIRELAaqgKAVIVITHDY 186
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-193 |
5.23e-25 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 99.77 E-value: 5.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLP----ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTAQ 75
Cdd:COG1135 1 MIELENLSKTFPtkggPVTALDDVSLTIEKGEIFGIIGYSGAGKSTL----IRCINLLERPTsGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 -----RQIGILFQDALLFDQFSVGQNLllALPSTLKGT---ARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRA 147
Cdd:COG1135 77 lraarRKIGMIFQHFNLLSSRTVAENV--ALPLEIAGVpkaEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 300840748 148 LLAQPKALLLDEPFSRLDVA--------LRD-NfrqwvfsevRELAIPVVQVTHD 193
Cdd:COG1135 155 LANNPKVLLCDEATSALDPEttrsildlLKDiN---------RELGLTIVLITHE 200
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-197 |
6.67e-25 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 101.25 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPT--AQRQ 77
Cdd:COG1129 4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTL----MKILSGVYQPDsGEILLDGEPVRFRSPrdAQAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 -IGILFQDALLFDQFSVGQNLLLALPSTLKGTARRNAV----KDALDRAGLAEtyhqDPAT----LSGGQRARVALLRAL 148
Cdd:COG1129 80 gIAIIHQELNLVPNLSVAENIFLGREPRRGGLIDWRAMrrraRELLARLGLDI----DPDTpvgdLSVAQQQLVEIARAL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 300840748 149 LAQPKALLLDEPFSrldvALRDNFRQWVFSEVRELA---IPVVQVTHDLQDV 197
Cdd:COG1129 156 SRDARVLILDEPTA----SLTEREVERLFRIIRRLKaqgVAIIYISHRLDEV 203
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
17-194 |
1.21e-24 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 96.48 E-value: 1.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAlagQFSCTGELWLNEQRIDML-----PTAQRQIGILFQDALLFDQF 91
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGI---ERPSAGKIWFSGHDITRLknrevPFLRRQIGMIFQDHHLLMDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 92 SVGQNLllALPSTLKGTAR---RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVAL 168
Cdd:PRK10908 95 TVYDNV--AIPLIIAGASGddiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180
....*....|....*....|....*.
gi 300840748 169 RDNFRQwVFSEVRELAIPVVQVTHDL 194
Cdd:PRK10908 173 SEGILR-LFEEFNRVGVTVLMATHDI 197
|
|
| LolD_lipo_ex |
TIGR02211 |
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ... |
13-195 |
1.48e-24 |
|
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: 96.27 E-value: 1.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALagQFSCTGELWLNEQRIDMLPTAQR------QIGILFQDAL 86
Cdd:TIGR02211 17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLH-LLGGL--DNPTSGEVLFNGQSLSKLSSNERaklrnkKLGFIYQFHH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 87 LFDQFSVGQNLllALPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSR 163
Cdd:TIGR02211 94 LLPDFTALENV--AMPLLIGKKSVKEAKERAyemLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
|
170 180 190
....*....|....*....|....*....|..
gi 300840748 164 LDVALRDNFRQWVFSEVRELAIPVVQVTHDLQ 195
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTSFLVVTHDLE 203
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-197 |
1.57e-24 |
|
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: 94.80 E-value: 1.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIdmlptaqrqigi 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTL----MKILSGLYKPDsGEILVDGKEV------------ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 lfqdallfdqfsvgqnlllalpstlkgtaRRNAVKDALdRAGLAeTYHQdpatLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:cd03216 65 -----------------------------SFASPRDAR-RAGIA-MVYQ----LSVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 161 FSRLDVALRDNFrqwvFSEVRELA---IPVVQVTHDLQDV 197
Cdd:cd03216 110 TAALTPAEVERL----FKVIRRLRaqgVAVIFISHRLDEV 145
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
4-196 |
2.32e-24 |
|
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: 95.90 E-value: 2.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPT-AQRQIGILF 82
Cdd:cd03265 3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT---SGRATVAGHDVVREPReVRRRIGIVF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLLL-ALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:cd03265 80 QDLSVDDELTGWENLYIhARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPT 159
|
170 180 190
....*....|....*....|....*....|....*
gi 300840748 162 SRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQD 196
Cdd:cd03265 160 IGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEE 194
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-165 |
2.65e-24 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 96.12 E-value: 2.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLP---TAQRQI 78
Cdd:PRK10895 4 LTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD---AGNIIIDDEDISLLPlhaRARRGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLL--LALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:PRK10895 81 GYLPQEASIFRRLSVYDNLMavLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFIL 160
|
....*....
gi 300840748 157 LDEPFSRLD 165
Cdd:PRK10895 161 LDEPFAGVD 169
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
4-197 |
3.24e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 96.62 E-value: 3.24e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPE--SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFScTGELWLNEQRI-DMlptaQRQ 77
Cdd:PRK13635 8 VEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLlpeAGTIT-VGGMVLSEETVwDV----RRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDAllFDQF---SVGQNLLLALPStlKGTARRNAVK---DALDRAGLAETYHQDPATLSGGQRARVALLRALLAQ 151
Cdd:PRK13635 83 VGMVFQNP--DNQFvgaTVQDDVAFGLEN--IGVPREEMVErvdQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQ 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 152 PKALLLDEPFSRLDVAlrdnFRQWVFSEVREL----AIPVVQVTHDLQDV 197
Cdd:PRK13635 159 PDIIILDEATSMLDPR----GRREVLETVRQLkeqkGITVLSITHDLDEA 204
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
16-195 |
4.78e-24 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 95.23 E-value: 4.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAG-QFSCTGELWLNEQRIDMLPTAQR------QIGILFQDALLF 88
Cdd:PRK10584 25 ILTGVELVVKRGETIALIGESGSGKSTL----LAILAGlDDGSSGEVSLVGQPLHQMDEEARaklrakHVGFVFQSFMLI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 89 DQFSVGQNLllALPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:PRK10584 101 PTLNALENV--ELPALLRGESSRQSRNGAkalLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLD 178
|
170 180 190
....*....|....*....|....*....|
gi 300840748 166 VALRDNFRQWVFSEVRELAIPVVQVTHDLQ 195
Cdd:PRK10584 179 RQTGDKIADLLFSLNREHGTTLILVTHDLQ 208
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-194 |
5.19e-24 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.99 E-value: 5.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRIDMLP--TAQRQI 78
Cdd:PRK09536 3 MIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLT---PTAGTVLVAGDDVEALSarAASRRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLA-LPSTLK----GTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPK 153
Cdd:PRK09536 80 ASVPQDTSLSFEFDVRQVVEMGrTPHRSRfdtwTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 300840748 154 ALLLDEPFSRLDValrdNFRQWVFSEVRELA---IPVVQVTHDL 194
Cdd:PRK09536 160 VLLLDEPTASLDI----NHQVRTLELVRRLVddgKTAVAAIHDL 199
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-194 |
6.81e-24 |
|
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: 96.66 E-value: 6.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLP----ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQRIDMLPTAQ- 75
Cdd:COG0444 1 LLEVRNLKVYFPtrrgVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSEKEl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 -----RQIGILFQDAL--LFDQFSVGQNL--LLALPSTLKGTARRNAVKDALDRAGL---AETYHQDPATLSGGQRARVA 143
Cdd:COG0444 81 rkirgREIQMIFQDPMtsLNPVMTVGDQIaePLRIHGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 300840748 144 LLRALLAQPKALLLDEPFSRLDVALRdnfRQwVFSEVRELA----IPVVQVTHDL 194
Cdd:COG0444 161 IARALALEPKLLIADEPTTALDVTIQ---AQ-ILNLLKDLQrelgLAILFITHDL 211
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-197 |
7.28e-24 |
|
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: 95.60 E-value: 7.28e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLR----LP-ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRID-----MLPT 73
Cdd:TIGR04521 3 LKNVSYIyqpgTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPT---SGTVTIDGRDITakkkkKLKD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 74 AQRQIGILFQ--DALLF-----DQFSVG-QNLLLAlpstlKGTARRnAVKDALDRAGLAETY-HQDPATLSGGQRARVAL 144
Cdd:TIGR04521 80 LRKKVGLVFQfpEHQLFeetvyKDIAFGpKNLGLS-----EEEAEE-RVKEALELVGLDEEYlERSPFELSGGQMRRVAI 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 300840748 145 LRALLAQPKALLLDEPFSRLDVALRDN----FRQWvfseVRELAIPVVQVTHDLQDV 197
Cdd:TIGR04521 154 AGVLAMEPEVLILDEPTAGLDPKGRKEildlFKRL----HKEKGLTVILVTHSMEDV 206
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
5-199 |
7.44e-24 |
|
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: 95.15 E-value: 7.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIgalagqfscTGELW---------LNEQRIDM-LPTA 74
Cdd:COG1119 7 RNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLS-LI---------TGDLPptygndvrlFGERRGGEdVWEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 QRQIGILfqDALLFDQFSVGQNLLLALPSTLKGT---------ARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALL 145
Cdd:COG1119 77 RKRIGLV--SPALQLRFPRDETVLDVVLSGFFDSiglyreptdEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIA 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 300840748 146 RALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDVPA 199
Cdd:COG1119 155 RALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPP 208
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
4-197 |
8.97e-24 |
|
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: 95.19 E-value: 8.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPES--RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRIdmlPTAQRQI 78
Cdd:TIGR04520 3 VENVSFSYPESekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLlptSGKVTVDGLDTLDEENL---WEIRKKV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQ--DallfDQFsVG-----------QNLllALPStlKGTARRnaVKDALDRAGLAETYHQDPATLSGGQRARVALL 145
Cdd:TIGR04520 80 GMVFQnpD----NQF-VGatveddvafglENL--GVPR--EEMRKR--VDEALKLVGMEDFRDREPHLLSGGQKQRVAIA 148
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 300840748 146 RALLAQPKALLLDEPFSRLDValrdNFRQWVFSEVREL----AIPVVQVTHDLQDV 197
Cdd:TIGR04520 149 GVLAMRPDIIILDEATSMLDP----KGRKEVLETIRKLnkeeGITVISITHDMEEA 200
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
4-192 |
9.41e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 94.19 E-value: 9.41e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRL--LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTA--QRQI 78
Cdd:cd03245 5 FRNVSFSYPNQEIpaLDNVSLTIRAGEKVAIIGRVGSGKSTLLK----LLAGLYKPTsGSVLLDGTDIRQLDPAdlRRNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQfSVGQNLLLALPStlkgtARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALLRA 147
Cdd:cd03245 81 GYVPQDVTLFYG-TLRDNITLGAPL-----ADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARA 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 300840748 148 LLAQPKALLLDEPFSRLDVALRDNFrqwvFSEVRELAIP--VVQVTH 192
Cdd:cd03245 155 LLNDPPILLLDEPTSAMDMNSEERL----KERLRQLLGDktLIIITH 197
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
5-165 |
1.01e-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: 1.01e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLP---ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTlfswmIGALAGQF--SCTGELWLNEQRIDML--PTAQRQ 77
Cdd:cd03249 4 KNVSFRYPsrpDVPILKGLSLTIPPGKTVALVGSSGCGKST-----VVSLLERFydPTSGEILLDGVDIRDLnlRWLRSQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQfSVGQNLLLALPSTLKGTARRNAVKDALDR--AGLAETYH----QDPATLSGGQRARVALLRALLAQ 151
Cdd:cd03249 79 IGLVSQEPVLFDG-TIAENIRYGKPDATDEEVEEAAKKANIHDfiMSLPDGYDtlvgERGSQLSGGQKQRIAIARALLRN 157
|
170
....*....|....
gi 300840748 152 PKALLLDEPFSRLD 165
Cdd:cd03249 158 PKILLLDEATSALD 171
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
4-165 |
1.95e-23 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 94.31 E-value: 1.95e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSctgelwlNEQRIDML-PTAQR------ 76
Cdd:PRK09984 7 VEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKS-------AGSHIELLgRTVQRegrlar 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 -------QIGILFQDALLFDQFSVGQNLLL-ALPST---------LKGTARRNAVKdALDRAGLAETYHQDPATLSGGQR 139
Cdd:PRK09984 80 dirksraNTGYIFQQFNLVNRLSVLENVLIgALGSTpfwrtcfswFTREQKQRALQ-ALTRVGMVHFAHQRVSTLSGGQQ 158
|
170 180
....*....|....*....|....*.
gi 300840748 140 ARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:PRK09984 159 QRVAIARALMQQAKVILADEPIASLD 184
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-197 |
3.31e-23 |
|
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: 92.34 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGE-LWLNEQridMLPTAQRQIGI 80
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIIL---PDSGEvLFDGKP---LDIAARNRIGY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLL-LAlpsTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:cd03269 75 LPEERGLYPKMKVIDQLVyLA---QLKGLKKEEARRRIdewLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 300840748 157 LDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03269 152 LDEPFSGLDPVNVELLKD-VIRELARAGKTVILSTHQMELV 191
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-160 |
6.32e-23 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.90 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQ-RIDMLPtaqrqigil 81
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLK----ILAGELEPDsGEVSIPKGlRIGYLP--------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 fQDALLFDQFSVGQNLLLALPSTLKGTARRNA---------------------------------VKDALDRAGLAETYH 128
Cdd:COG0488 68 -QEPPLDDDLTVLDTVLDGDAELRALEAELEEleaklaepdedlerlaelqeefealggweaearAEEILSGLGFPEEDL 146
|
170 180 190
....*....|....*....|....*....|...
gi 300840748 129 QDP-ATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:COG0488 147 DRPvSELSGGWRRRVALARALLSEPDLLLLDEP 179
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-208 |
6.82e-23 |
|
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: 90.74 E-value: 6.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELwlneqRIDMLPTAQ------ 75
Cdd:cd03246 3 VENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT---SGRV-----RLDGADISQwdpnel 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 -RQIGILFQDALLFDqfsvgqnlllalpstlkGTARRNavkdaldraglaetyhqdpaTLSGGQRARVALLRALLAQPKA 154
Cdd:cd03246 75 gDHVGYLPQDDELFS-----------------GSIAEN--------------------ILSGGQRQRLGLARALYGNPRI 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 155 LLLDEPFSRLDV----ALRDNFRQwvfseVRELAIPVVQVTHDLQDVPADSSVLDMAQ 208
Cdd:cd03246 118 LVLDEPNSHLDVegerALNQAIAA-----LKAAGATRIVIAHRPETLASADRILVLED 170
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
19-166 |
2.29e-22 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 92.49 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLfswmiG-ALAGQFSCT-GELWLNEQRIDMLPTAQ-----RQIGILFQD--ALLFD 89
Cdd:COG4608 36 GVSFDIRRGETLGLVGESGCGKSTL-----GrLLLRLEEPTsGEILFDGQDITGLSGRElrplrRRMQMVFQDpyASLNP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 90 QFSVGQnlLLALP----STLKGTARRNAVKDALDRAGL-AETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRL 164
Cdd:COG4608 111 RMTVGD--IIAEPlrihGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSAL 188
|
..
gi 300840748 165 DV 166
Cdd:COG4608 189 DV 190
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
4-195 |
2.92e-22 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 90.87 E-value: 2.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIgALAGQFSCTGELWLNEQRI---DMLPTA-QR 76
Cdd:COG1117 14 VRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLlrcLNRMN-DLIPGARVEGEILLDGEDIydpDVDVVElRR 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFdQFSVGQNLLLALPstLKGTARRN----AVKDALDRAGL-AETYH--QDPAT-LSGGQRARVALLRAL 148
Cdd:COG1117 93 RVGMVFQKPNPF-PKSIYDNVAYGLR--LHGIKSKSeldeIVEESLRKAALwDEVKDrlKKSALgLSGGQQQRLCIARAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 149 LAQPKALLLDEPFSRLD-----------VALRDNFrqwvfsevrelaiPVVQVTHDLQ 195
Cdd:COG1117 170 AVEPEVLLMDEPTSALDpistakieeliLELKKDY-------------TIVIVTHNMQ 214
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-197 |
4.94e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 90.43 E-value: 4.94e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQ-RQI 78
Cdd:PRK11300 5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFN----CLTGFYKPTgGTILLRGQHIEGLPGHQiARM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GIL--FQDALLFDQFSVGQNLLLA---------LPSTLKGTARRNAVKDALDRA-------GLAETYHQDPATLSGGQRA 140
Cdd:PRK11300 81 GVVrtFQHVRLFREMTVIENLLVAqhqqlktglFSGLLKTPAFRRAESEALDRAatwlervGLLEHANRQAGNLAYGQQR 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 300840748 141 RVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLV 217
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
4-207 |
8.27e-22 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 90.21 E-value: 8.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLP-----TAQRQI 78
Cdd:PRK11831 10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD---HGEILFDGENIPAMSrsrlyTVRKRM 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNllLALP----STLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKA 154
Cdd:PRK11831 87 SMLFQSGALFTDMNVFDN--VAYPlrehTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 155 LLLDEPFSRLD-------VALRDNFRQwvfsevrELAIPVVQVTHdlqDVPADSSVLDMA 207
Cdd:PRK11831 165 IMFDEPFVGQDpitmgvlVKLISELNS-------ALGVTCVVVSH---DVPEVLSIADHA 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
17-192 |
1.47e-21 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 90.63 E-value: 1.47e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALagQFSCTGELWLNEQRIDMLPT-----AQRQIGILFQDALLFDQF 91
Cdd:PRK11153 21 LNNVSLHIPAGEIFGVIGASGAGKSTLIR-CINLL--ERPTSGRVLVDGQDLTALSEkelrkARRQIGMIFQHFNLLSSR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 92 SVGQNllLALPSTLKGTAR---RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVA- 167
Cdd:PRK11153 98 TVFDN--VALPLELAGTPKaeiKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDPAt 175
|
170 180 190
....*....|....*....|....*....|...
gi 300840748 168 -------LRD-NfrqwvfsevRELAIPVVQVTH 192
Cdd:PRK11153 176 trsilelLKDiN---------RELGLTIVLITH 199
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
6-197 |
1.64e-21 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 90.70 E-value: 1.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 6 NVSLRLPESRLltNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAG----QfscTGELWLN-------EQRIDmLPTA 74
Cdd:PRK11144 5 NFKQQLGDLCL--TVNLTLPAQGITAIFGRSGAGKTSL----INAISGltrpQ---KGRIVLNgrvlfdaEKGIC-LPPE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 QRQIGILFQDALLFDQFSVGQNLLLALPSTLKgtARRNAVKDALDRAGLAETYhqdPATLSGGQRARVALLRALLAQPKA 154
Cdd:PRK11144 75 KRRIGYVFQDARLFPHYKVRGNLRYGMAKSMV--AQFDKIVALLGIEPLLDRY---PGSLSGGEKQRVAIGRALLTAPEL 149
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 155 LLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK11144 150 LLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEI 192
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-194 |
2.25e-21 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 88.65 E-value: 2.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLF----------SWMIGAlaGQFSCTGELWLNEQRiDM 70
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLrcinlleqpeAGTIRV--GDITIDTARSLSQQK-GL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 71 LPTAQRQIGILFQDALLFDQFSVGQNLLLAlPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRA 147
Cdd:PRK11264 80 IRQLRQHVGFVFQNFNLFPHRTVLENIIEG-PVIVKGEPKEEATARArelLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 148 LLAQPKALLLDEPFSRLDVALRDNfrqwVFSEVRELA---IPVVQVTHDL 194
Cdd:PRK11264 159 LAMRPEVILFDEPTSALDPELVGE----VLNTIRQLAqekRTMVIVTHEM 204
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
17-165 |
2.59e-21 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 88.70 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALagQFSCTGELWLNEQRIDM--------LPTAQRQI-------GIL 81
Cdd:COG4598 24 LKGVSLTARKGDVISIIGSSGSGKSTFLR-CINLL--ETPDSGEIRVGGEEIRLkpdrdgelVPADRRQLqrirtrlGMV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDALLFDQFSVGQNLLLAlPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:COG4598 101 FQSFNLWSHMTVLENVIEA-PVHVLGRPKAEAIERAealLAKVGLADKRDAYPAHLSGGQQQRAAIARALAMEPEVMLFD 179
|
....*..
gi 300840748 159 EPFSRLD 165
Cdd:COG4598 180 EPTSALD 186
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
5-165 |
2.91e-21 |
|
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: 88.06 E-value: 2.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLP--ESRLLTNVNFTVDKGDIVTLMGPSGCGKST---LFSWMIGALAGQFSCTG----ELWLNEQRidmlptaq 75
Cdd:cd03251 4 KNVTFRYPgdGPPVLRDISLDIPAGETVALVGPSGSGKSTlvnLIPRFYDVDSGRILIDGhdvrDYTLASLR-------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 RQIGILFQDALLFDQfSVGQNLLLALPStlkgtARRNAVKDALDRA-------GLAETYHQD----PATLSGGQRARVAL 144
Cdd:cd03251 76 RQIGLVSQDVFLFND-TVAENIAYGRPG-----ATREEVEEAARAAnahefimELPEGYDTVigerGVKLSGGQRQRIAI 149
|
170 180
....*....|....*....|.
gi 300840748 145 LRALLAQPKALLLDEPFSRLD 165
Cdd:cd03251 150 ARALLKDPPILILDEATSALD 170
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
17-194 |
2.92e-21 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 88.36 E-value: 2.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfsctGELWLNEQRIDMLPTAQ--RQIGILFQDALLFDQFSVG 94
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLPGQ----GEILLNGRPLSDWSAAElaRHRAYLSQQQSPPFAMPVF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 95 QNLLLALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALL-------AQPKALLLDEPFSRLDVA 167
Cdd:COG4138 88 QYLALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptinPEGQLLLLDEPMNSLDVA 167
|
170 180
....*....|....*....|....*..
gi 300840748 168 LRDNFRQWVfSEVRELAIPVVQVTHDL 194
Cdd:COG4138 168 QQAALDRLL-RELCQQGITVVMSSHDL 193
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
20-199 |
2.99e-21 |
|
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: 87.42 E-value: 2.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 20 VNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRidmlpTAQRQIGILFQDALLFDQFSVGQN 96
Cdd:cd03266 24 VSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLepdAGFATVDGFDVVKEPA-----EARRRLGFVSDSTGLYDRLTAREN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 97 LL-LALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQw 175
Cdd:cd03266 99 LEyFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALRE- 177
|
170 180
....*....|....*....|....
gi 300840748 176 VFSEVRELAIPVVQVTHDLQDVPA 199
Cdd:cd03266 178 FIRQLRALGKCILFSTHIMQEVER 201
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-198 |
6.45e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 87.98 E-value: 6.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPE-SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRIDM----LPTAQ 75
Cdd:PRK13636 5 ILKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILK---PSSGRILFDGKPIDYsrkgLMKLR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 RQIGILFQD-------ALLFDQFSVGQnLLLALPStlKGTARRnaVKDALDRAGLAETYHQDPATLSGGQRARVALLRAL 148
Cdd:PRK13636 82 ESVGMVFQDpdnqlfsASVYQDVSFGA-VNLKLPE--DEVRKR--VDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 149 LAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDVP 198
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVP 206
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-165 |
8.37e-21 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.14 E-value: 8.37e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWM--IGALAGQFSCTGELWLNEQRIdMLPTA---- 74
Cdd:PRK14239 5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNI-YSPRTdtvd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 -QRQIGILFQDALLFdQFSVGQNLLL---------------ALPSTLKGTARRNAVKDALdraglaetyHQDPATLSGGQ 138
Cdd:PRK14239 84 lRKEIGMVFQQPNPF-PMSIYENVVYglrlkgikdkqvldeAVEKSLKGASIWDEVKDRL---------HDSALGLSGGQ 153
|
170 180
....*....|....*....|....*..
gi 300840748 139 RARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:PRK14239 154 QQRVCIARVLATSPKIILLDEPTSALD 180
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
1-198 |
8.48e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 87.44 E-value: 8.48e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPE-SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDM----LPTAQ 75
Cdd:PRK13639 1 ILETRDLKYSYPDgTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT---SGEVLIKGEPIKYdkksLLEVR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 RQIGILFQ--DALLFDQfSVGQN-----LLLALPStlKGTARRnaVKDALDRAGLAETYHQDPATLSGGQRARVALLRAL 148
Cdd:PRK13639 78 KTVGIVFQnpDDQLFAP-TVEEDvafgpLNLGLSK--EEVEKR--VKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 149 LAQPKALLLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDVP 198
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMK-LLYDLNKEGITIIISTHDVDLVP 201
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-165 |
1.21e-20 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 89.38 E-value: 1.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfsctGELWLNEQ------RIDMLPTaQRQIGILFQD-- 84
Cdd:PRK15134 298 HNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ----GEIWFDGQplhnlnRRQLLPV-RHRIQVVFQDpn 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 85 ALLFDQFSVGQNLLLALP---STLKGTARRNAVKDALDRAGL-AETYHQDPATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:PRK15134 373 SSLNPRLNVLQIIEEGLRvhqPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452
|
....*
gi 300840748 161 FSRLD 165
Cdd:PRK15134 453 TSSLD 457
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
1-195 |
1.26e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.41 E-value: 1.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLT----NVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSctGELWLNEQRIDMLPTA-- 74
Cdd:PRK11629 5 LLQCDNLCKRYQEGSVQTdvlhNVSFSIGEGEMMAIVGSSGSGKSTLLH-LLGGLDTPTS--GDVIFNGQPMSKLSSAak 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 ----QRQIGILFQDALLFDQFSVGQNLllALPSTLKGTARRNAVKDALDR---AGLAETYHQDPATLSGGQRARVALLRA 147
Cdd:PRK11629 82 aelrNQKLGFIYQFHHLLPDFTALENV--AMPLLIGKKKPAEINSRALEMlaaVGLEHRANHRPSELSGGERQRVAIARA 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 300840748 148 LLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQ 195
Cdd:PRK11629 160 LVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQ 207
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
17-169 |
1.50e-20 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 87.71 E-value: 1.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLfswmigalAGQFS-----CTGELWLNEQriDML---PTAQ----RQIGILFQD 84
Cdd:PRK11308 31 LDGVSFTLERGKTLAVVGESGCGKSTL--------ARLLTmietpTGGELYYQGQ--DLLkadPEAQkllrQKIQIVFQN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 85 --ALLFDQFSVGQNLL--LALPSTLKGTARRNAVKDALDRAGL-AETYHQDPATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:PRK11308 101 pyGSLNPRKKVGQILEepLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADE 180
|
170
....*....|
gi 300840748 160 PFSRLDVALR 169
Cdd:PRK11308 181 PVSALDVSVQ 190
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-197 |
1.56e-20 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 89.14 E-value: 1.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLP-----------ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRID 69
Cdd:PRK10261 313 ILQVRNLVTRFPlrsgllnrvtrEVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQ---GGEIIFNGQRID 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 70 MLPTAQ-----RQIGILFQD--ALLFDQFSVGQNLL--LALPSTLKGTARRNAVKDALDRAGL-AETYHQDPATLSGGQR 139
Cdd:PRK10261 390 TLSPGKlqalrRDIQFIFQDpyASLDPRQTVGDSIMepLRVHGLLPGKAAAARVAWLLERVGLlPEHAWRYPHEFSGGQR 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 140 ARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK10261 470 QRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVV 527
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
17-199 |
1.69e-20 |
|
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: 85.85 E-value: 1.69e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGEL-WlnEQRIDMLptaqRQIGILF-QDALLFDQF 91
Cdd:cd03267 37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLqptSGEVRVAGLVpW--KRRKKFL----RRIGVVFgQKTQLWWDL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 92 SVGQ--NLLLALPSTLKGTARRNAVK--DALDragLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVA 167
Cdd:cd03267 111 PVIDsfYLLAAIYDLPPARFKKRLDElsELLD---LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
|
170 180 190
....*....|....*....|....*....|..
gi 300840748 168 LRDNFRQWVFSEVRELAIPVVQVTHDLQDVPA 199
Cdd:cd03267 188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEA 219
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
2-160 |
2.48e-20 |
|
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: 85.27 E-value: 2.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGqfsCTGELWLNEQRIDMLPTAQR-QIGI 80
Cdd:TIGR03410 1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPV---KSGSIRLDGEDITKLPPHERaRAGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LF--QDALLFDQFSVGQNLLLALPstlkGTARRN------------AVKDALDRAGlaetyhqdpATLSGGQRARVALLR 146
Cdd:TIGR03410 78 AYvpQGREIFPRLTVEENLLTGLA----ALPRRSrkipdeiyelfpVLKEMLGRRG---------GDLSGGQQQQLAIAR 144
|
170
....*....|....
gi 300840748 147 ALLAQPKALLLDEP 160
Cdd:TIGR03410 145 ALVTRPKLLLLDEP 158
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
2-208 |
3.41e-20 |
|
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: 84.47 E-value: 3.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRID-MLPTAQRQIGI 80
Cdd:cd03231 1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL---AGRVLLNGGPLDfQRDSIARGLLY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLLLalpstLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:cd03231 78 LGHAPGIKTTLSVLENLRF-----WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 300840748 161 FSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDVPADSSVLDMAQ 208
Cdd:cd03231 153 TTALDKAGVARFAEAMAGHCARGGMVVLTTHQDLGLSEAGARELDLGF 200
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-197 |
3.85e-20 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 85.93 E-value: 3.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDmlPTAQRQIGI 80
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGEPLD--PEDRRRIGY 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLL-LAlpsTLKGTARRNAVKDA---LDRAGLAEtYHQDPA-TLSGGQRARVALLRALLAQPKAL 155
Cdd:COG4152 76 LPEERGLYPKMKVGEQLVyLA---RLKGLSKAEAKRRAdewLERLGLGD-RANKKVeELSKGNQQKVQLIAALLHDPELL 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 156 LLDEPFSRLD-VAlrdnfRQWVFSEVRELA---IPVVQVTHDLQDV 197
Cdd:COG4152 152 ILDEPFSGLDpVN-----VELLKDVIRELAakgTTVIFSSHQMELV 192
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
1-167 |
5.96e-20 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 83.70 E-value: 5.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGaLAGQFSctGELWLNEQRIdmlpTAQRQIgi 80
Cdd:PRK13538 1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAG-LARPDA--GEVLWQGEPI----RRQRDE-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 lFQDALLF--------DQFSVGQNLLLALPstLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQP 152
Cdd:PRK13538 72 -YHQDLLYlghqpgikTELTALENLRFYQR--LHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRA 148
|
170
....*....|....*
gi 300840748 153 KALLLDEPFSRLDVA 167
Cdd:PRK13538 149 PLWILDEPFTAIDKQ 163
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
15-165 |
6.23e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 83.37 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 15 RLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSC---TGELWLNEQRIDmLPTAQRQIGILFQDALLFDQF 91
Cdd:cd03213 23 QLLKNVSGKAKPGELTAIMGPSGAGKSTL----LNALAGRRTGlgvSGEVLINGRPLD-KRSFRKIIGYVPQDDILHPTL 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300840748 92 SVGQNLLLAlpSTLKGtarrnavkdaldraglaetyhqdpatLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:cd03213 98 TVRETLMFA--AKLRG--------------------------LSGGERKRVSIALELVSNPSLLFLDEPTSGLD 143
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
19-197 |
7.31e-20 |
|
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: 87.17 E-value: 7.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELW--LNEQRIDMLPT-------AQRQIGILFQDALLFD 89
Cdd:TIGR03269 302 NVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLE---PTSGEVNvrVGDEWVDMTKPgpdgrgrAKRYIGILHQEYDLYP 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 90 QFSVGQNLL----LALPSTLkgtARRNAVKdALDRAGLAETYHQD-----PATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:TIGR03269 379 HRTVLDNLTeaigLELPDEL---ARMKAVI-TLKMVGFDEEKAEEildkyPDELSEGERHRVALAQVLIKEPRIVILDEP 454
|
170 180 190
....*....|....*....|....*....|....*..
gi 300840748 161 FSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFV 491
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
14-165 |
8.32e-20 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 86.82 E-value: 8.32e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 14 SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCTGELWLNEQRIDMLPTAQ--RQIGILFQDALLFDQf 91
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSL----LNALLGFLPYQGSLKINGIELRELDPESwrKHLSWVGQNPQLPHG- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 92 SVGQNLLLALPStlkgtARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:PRK11174 438 TLRDNVLLGNPD-----ASDEQLQQALENAWVSEFLPLLPqgldtpigdqaAGLSVGQAQRLALARALLQPCQLLLLDEP 512
|
....*
gi 300840748 161 FSRLD 165
Cdd:PRK11174 513 TASLD 517
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
15-165 |
8.58e-20 |
|
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: 83.86 E-value: 8.58e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 15 RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQRIDMlPTAQRQIGILFQDALLFDQFSVG 94
Cdd:cd03234 21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKP-DQFQKCVAYVRQDDILLPGLTVR 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300840748 95 QNL----LLALPSTLKGTARRNAVKD-ALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:cd03234 100 ETLtytaILRLPRKSSDAIRKKRVEDvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
2-192 |
1.39e-19 |
|
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: 86.25 E-value: 1.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAlagqfsctgelWLNEQ---RIDMLPTAQ- 75
Cdd:TIGR01842 317 LSVENVTIVPPGGKkpTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGI-----------WPPTSgsvRLDGADLKQw 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 ------RQIGILFQDALLFDQfSVGQNLllalpSTLKGTARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQ 138
Cdd:TIGR01842 386 dretfgKHIGYLPQDVELFPG-TVAENI-----ARFGENADPEKIIEAAKLAGVHELILRLPdgydtvigpggATLSGGQ 459
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 139 RARVALLRALLAQPKALLLDEPFSRLD----VALRDnfrqwVFSEVRELAIPVVQVTH 192
Cdd:TIGR01842 460 RQRIALARALYGDPKLVVLDEPNSNLDeegeQALAN-----AIKALKARGITVVVITH 512
|
|
| sufC |
TIGR01978 |
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ... |
2-192 |
1.69e-19 |
|
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 83.46 E-value: 1.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT---GELWLNEQRIDMLPTAQRQI 78
Cdd:TIGR01978 1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTL----SKTIAGHPSYEvtsGTILFKGQDLLELEPDERAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFqdaLLFdQFSV---GQNLLLALPSTLkgTARRNA-VKDALDRA-------GLAETYHQDPATL--------SGGQR 139
Cdd:TIGR01978 77 AGLF---LAF-QYPEeipGVSNLEFLRSAL--NARRSArGEEPLDLLdfekllkEKLALLDMDEEFLnrsvnegfSGGEK 150
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 300840748 140 ARVALLRALLAQPKALLLDEPFSRLDV-ALRDnfrqwVFSEVRELAIP---VVQVTH 192
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIdALKI-----VAEGINRLREPdrsFLIITH 202
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
2-192 |
2.16e-19 |
|
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: 82.19 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT---GELWLNEQRI-DMLPT--AQ 75
Cdd:cd03217 1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAK----TIMGHPKYEvteGEILFKGEDItDLPPEerAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 RQIGILFQDallfdqfsvgqnlllalPSTLKGTARRNAVKDaLDraglaetyhqdpATLSGGQRARVALLRALLAQPKAL 155
Cdd:cd03217 77 LGIFLAFQY-----------------PPEIPGVKNADFLRY-VN------------EGFSGGEKKRNEILQLLLLEPDLA 126
|
170 180 190
....*....|....*....|....*....|....*...
gi 300840748 156 LLDEPFSRLDV-ALRDNFRqwVFSEVRELAIPVVQVTH 192
Cdd:cd03217 127 ILDEPDSGLDIdALRLVAE--VINKLREEGKSVLIITH 162
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-199 |
3.98e-19 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 82.47 E-value: 3.98e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQ-RIDMLPtaQRqig 79
Cdd:PRK09544 4 LVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVA---PDEGVIKRNGKlRIGYVP--QK--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 iLFQDALLfdQFSVGQNLllalpsTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:PRK09544 76 -LYLDTTL--PLTVNRFL------RLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDE 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 300840748 160 PFSRLDV----ALRDNFRQWvfseVRELAIPVVQVTHDLQDVPA 199
Cdd:PRK09544 147 PTQGVDVngqvALYDLIDQL----RRELDCAVLMVSHDLHLVMA 186
|
|
| type_I_sec_LssB |
TIGR03375 |
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ... |
5-176 |
4.65e-19 |
|
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]
Pssm-ID: 274550 [Multi-domain] Cd Length: 694 Bit Score: 84.92 E-value: 4.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGelwLNEQRIDMlPTAQRQIG 79
Cdd:TIGR03375 467 RNVSFAYPGQEtpALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYqptEGSVLLDG---VDIRQIDP-ADLRRNIG 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFdQFSVGQNLLLALPStlkgtARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALLRAL 148
Cdd:TIGR03375 543 YVPQDPRLF-YGTLRDNIALGAPY-----ADDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARAL 616
|
170 180 190
....*....|....*....|....*....|..
gi 300840748 149 LAQPKALLLDEPFSRLDVA----LRDNFRQWV 176
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRseerFKDRLKRWL 648
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
4-208 |
4.70e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 82.86 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRL---PESRLLTNVNFTVDKGDIVTLMGPSGCGKST---LFSWMIGALAGQFSCTGELWLNEQRIDMlptaQRQ 77
Cdd:PRK13650 7 VKNLTFKYkedQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTtvrLIDGLLEAESGQIIIDGDLLTEENVWDI----RHK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDAllFDQF---SVGQNLLLALPStlKGTAR---RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQ 151
Cdd:PRK13650 83 IGMVFQNP--DNQFvgaTVEDDVAFGLEN--KGIPHeemKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMR 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 300840748 152 PKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDVPADSSVLDMAQ 208
Cdd:PRK13650 159 PKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKN 215
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
2-197 |
5.09e-19 |
|
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: 80.82 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQRQ-I 78
Cdd:cd03247 1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGVPVSDLEKALSSlI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQfSVGQNLllalpstlkgtARRnavkdaldraglaetyhqdpatLSGGQRARVALLRALLAQPKALLLD 158
Cdd:cd03247 78 SVLNQRPYLFDT-TLRNNL-----------GRR----------------------FSGGERQRLALARILLQDAPIVLLD 123
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIpvVQVTHDLQDV 197
Cdd:cd03247 124 EPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGI 160
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
1-192 |
6.72e-19 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 84.47 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGqfsctgeLWLNEQ-RIDmLPTAQRqi 78
Cdd:COG4178 362 ALALEDLTLRTPDGRpLLEDLSLSLKPGERLLITGPSGSGKSTLLR----AIAG-------LWPYGSgRIA-RPAGAR-- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 gILF--Q----------DALLF----DQFSvgqnlllalpstlkgtarRNAVKDALDRAGL---AETYHQD---PATLSG 136
Cdd:COG4178 428 -VLFlpQrpylplgtlrEALLYpataEAFS------------------DAELREALEAVGLghlAERLDEEadwDQVLSL 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 300840748 137 GQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIpvVQVTH 192
Cdd:COG4178 489 GEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTV--ISVGH 542
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
5-166 |
9.57e-19 |
|
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: 81.12 E-value: 9.57e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ--RQIGIL 81
Cdd:cd03254 6 ENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDIRDISRKSlrSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDALLFdQFSVGQNLLLALPstlkgTARRNAVKDALDRAG-------LAETYHQDP----ATLSGGQRARVALLRALLA 150
Cdd:cd03254 83 LQDTFLF-SGTIMENIRLGRP-----NATDEEVIEAAKEAGahdfimkLPNGYDTVLgengGNLSQGERQLLAIARAMLR 156
|
170
....*....|....*.
gi 300840748 151 QPKALLLDEPFSRLDV 166
Cdd:cd03254 157 DPKILILDEATSNIDT 172
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
2-192 |
1.35e-18 |
|
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: 79.12 E-value: 1.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGqfsctgeLWlneqridmlPTAQRQIGI 80
Cdd:cd03223 1 IELENLSLATPDGRvLLKDLSFEIKPGDRLLITGPSGTGKSSLFR----ALAG-------LW---------PWGSGRIGM 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFdqfsvgqnlllaLPstlkgtaRRNAVKDALDRAGLAETYHQdpaTLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:cd03223 61 PEGEDLLF------------LP-------QRPYLPLGTLREQLIYPWDD---VLSGGEQQRLAFARLLLHKPKFVFLDEA 118
|
170 180 190
....*....|....*....|....*....|..
gi 300840748 161 FSRLDVALRDNFRQwvfsEVRELAIPVVQVTH 192
Cdd:cd03223 119 TSALDEESEDRLYQ----LLKELGITVISVGH 146
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
12-166 |
1.61e-18 |
|
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: 80.74 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 12 PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigaLAGQF--SCTGELWLNEQRID--MLPTAQRQIGILFQDALL 87
Cdd:cd03253 12 PGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILR-----LLFRFydVSSGSILIDGQDIRevTLDSLRRAIGVVPQDTVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 88 FDQfSVGQNLLLALPStlkgtARRNAVKDALDRAGLAETYHQDP---AT--------LSGGQRARVALLRALLAQPKALL 156
Cdd:cd03253 87 FND-TIGYNIRYGRPD-----ATDEEVIEAAKAAQIHDKIMRFPdgyDTivgerglkLSGGEKQRVAIARAILKNPPILL 160
|
170
....*....|
gi 300840748 157 LDEPFSRLDV 166
Cdd:cd03253 161 LDEATSALDT 170
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-194 |
1.78e-18 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.90 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSctGELWLNEQRIDMLPTAQ--RQI 78
Cdd:COG4604 1 MIEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLS-MISRLLPPDS--GEVLVDGLDVATTPSRElaKRL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQnlLLAL---PSTlKG--TAR-RNAVKDALDRAGLAETYHQDPATLSGGQRARvALLRALLAQ- 151
Cdd:COG4604 78 AILRQENHINSRLTVRE--LVAFgrfPYS-KGrlTAEdREIIDEAIAYLDLEDLADRYLDELSGGQRQR-AFIAMVLAQd 153
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 300840748 152 PKALLLDEPFSRLD----VALRDNFRQwvfsEVRELAIPVVQVTHDL 194
Cdd:COG4604 154 TDYVLLDEPLNNLDmkhsVQMMKLLRR----LADELGKTVVIVLHDI 196
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
2-195 |
2.24e-18 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 80.78 E-value: 2.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALagQFSCTGELWLNEQRIDMLPTAQRQIGI- 80
Cdd:PRK10619 6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLR-CINFL--EKPSEGSIVVNGQTINLVRDKDGQLKVa 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 --------------LFQDALLFDQFSVGQNLLLALPSTL---KGTARRNAVKdALDRAGLAETYHQD-PATLSGGQRARV 142
Cdd:PRK10619 83 dknqlrllrtrltmVFQHFNLWSHMTVLENVMEAPIQVLglsKQEARERAVK-YLAKVGIDERAQGKyPVHLSGGQQQRV 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 300840748 143 ALLRALLAQPKALLLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQ 195
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLR-IMQQLAEEGKTMVVVTHEMG 213
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-197 |
3.15e-18 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 80.47 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWM--IGALAGQFSCTGELW-----LNEQRIDmLPTAQR 76
Cdd:PRK14258 10 VNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLnrMNELESEVRVEGRVEffnqnIYERRVN-LNRLRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLF-----DQFSVGQNLLLALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQ 151
Cdd:PRK14258 89 QVSMVHPKPNLFpmsvyDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVK 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 152 PKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK14258 169 PKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQV 214
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
4-193 |
3.85e-18 |
|
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: 82.10 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFsctgelwlneqRIDMLPTAQ--- 75
Cdd:COG4618 333 VENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWpptAGSV-----------RLDGADLSQwdr 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 ----RQIGILFQDALLFDQfSVGQNLllalpstlkgtAR-----RNAVKDALDRAG-------LAETYH----QDPATLS 135
Cdd:COG4618 402 eelgRHIGYLPQDVELFDG-TIAENI-----------ARfgdadPEKVVAAAKLAGvhemilrLPDGYDtrigEGGARLS 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300840748 136 GGQRARVALLRALLAQPKALLLDEPFSRLD----VALRDNFRQwvfseVRELAIPVVQVTHD 193
Cdd:COG4618 470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDdegeAALAAAIRA-----LKARGATVVVITHR 526
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
13-197 |
3.91e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 80.48 E-value: 3.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLN-----EQRIDmLPTAQRQIGILFQ--DA 85
Cdd:PRK13637 19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLK---PTSGKIIIDgvditDKKVK-LSDIRKKVGLVFQypEY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 86 LLFDQ-----FSVG-QNLLLALPSTlkgtarRNAVKDALDRAGLA-ETYH-QDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:PRK13637 95 QLFEEtiekdIAFGpINLGLSEEEI------ENRVKRAMNIVGLDyEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILIL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 300840748 158 DEPFSRLDVALRDNfrqwVFSEVREL----AIPVVQVTHDLQDV 197
Cdd:PRK13637 169 DEPTAGLDPKGRDE----ILNKIKELhkeyNMTIILVSHSMEDV 208
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
16-197 |
5.69e-18 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 78.04 E-value: 5.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGqfSCTGelwlneqridmlpTAQRQIGILFQDALLFDQFS 92
Cdd:NF040873 7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLrptSG--TVRR-------------AGGARVAYVPQRSEVPDSLP 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 93 VGQNLLLAL-------PSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:NF040873 72 LTVRDLVAMgrwarrgLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151
|
170 180 190
....*....|....*....|....*....|..
gi 300840748 166 VALRDNFRQWVFSEVRELAIpVVQVTHDLQDV 197
Cdd:NF040873 152 AESRERIIALLAEEHARGAT-VVVVTHDLELV 182
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-193 |
6.20e-18 |
|
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: 76.72 E-value: 6.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQfsctgelwlneqridMLPTAqrqiGIL 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLK----LIAGE---------------LEPDE----GIV 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 fqdallfdqfSVGQNLLLALpstlkgtarrnavkdaldraglaetYHQdpatLSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:cd03221 58 ----------TWGSTVKIGY-------------------------FEQ----LSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190
....*....|....*....|....*....|..
gi 300840748 162 SRLDVALrdnfRQWVFSEVRELAIPVVQVTHD 193
Cdd:cd03221 99 NHLDLES----IEALEEALKEYPGTVILVSHD 126
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-170 |
7.03e-18 |
|
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: 78.63 E-value: 7.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVS----------LRLPesrLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLN--EQR 67
Cdd:COG4778 4 LLEVENLSktftlhlqggKRLP---VLDGVSFSVAAGECVALTGPSGAGKSTL----LKCIYGNYLPDsGSILVRhdGGW 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 68 IDMLPTAQRQIGILFQDALLF-DQFsvgqnlLLALP--STL-------------KGTARRNAvKDALDRAGLAET-YHQD 130
Cdd:COG4778 77 VDLAQASPREILALRRRTIGYvSQF------LRVIPrvSALdvvaepllergvdREEARARA-RELLARLNLPERlWDLP 149
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 131 PATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRD 170
Cdd:COG4778 150 PATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA 189
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
16-197 |
7.09e-18 |
|
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: 79.46 E-value: 7.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFSCTGELWLNEQRIDMlPTAQRQIGILFQDAL--LFDQ 90
Cdd:TIGR02769 26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGlekPAQGTVSFRGQDLYQLDRKQR-RAFRRDVQLVFQDSPsaVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 91 FSVGQnlLLALP----STLKGTARRNAVKDALDRAGL-AETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:TIGR02769 105 MTVRQ--IIGEPlrhlTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
|
170 180 190
....*....|....*....|....*....|..
gi 300840748 166 VALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAYLFITHDLRLV 214
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-160 |
8.20e-18 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 78.77 E-value: 8.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDMLPTAQ---R 76
Cdd:PRK11614 5 MLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTL----LGTLCGDPRATsGRIVFDGKDITDWQTAKimrE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQFSVGQNLLLA--LPSTLKGTARRNAVKDALDRagLAETYHQDPATLSGGQRARVALLRALLAQPKA 154
Cdd:PRK11614 81 AVAIVPEGRRVFSRMTVEENLAMGgfFAERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALMSQPRL 158
|
....*.
gi 300840748 155 LLLDEP 160
Cdd:PRK11614 159 LLLDEP 164
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-192 |
8.98e-18 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 78.57 E-value: 8.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT---GELWLNEQRI-DMLPT--AQRQ 77
Cdd:COG0396 3 IKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAK----VLMGHPKYEvtsGSILLDGEDIlELSPDerARAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQFSVGQNLLLALPS----TLKGTARRNAVKDALDRAGLAETYHQDP--ATLSGGQRARVALLRALLAQ 151
Cdd:COG0396 79 IFLAFQYPVEIPGVSVSNFLRTALNArrgeELSAREFLKLLKEKMKELGLDEDFLDRYvnEGFSGGEKKRNEILQMLLLE 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 300840748 152 PKALLLDEPFSRLDValrDNFRQwVFSEVRELAIP---VVQVTH 192
Cdd:COG0396 159 PKLAILDETDSGLDI---DALRI-VAEGVNKLRSPdrgILIITH 198
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-160 |
1.05e-17 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 80.84 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLfswM-IgaLAGQFSCT-GELWLNEQRIDML-PTAQRQ--IGILFQDALLFDQFSV 93
Cdd:COG3845 23 DVSLTVRPGEIHALLGENGAGKSTL---MkI--LYGLYQPDsGEILIDGKPVRIRsPRDAIAlgIGMVHQHFMLVPNLTV 97
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300840748 94 GQNLLLALPSTLKGTARRNAVKDALDRagLAETY--HQDP----ATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:COG3845 98 AENIVLGLEPTKGGRLDRKAARARIRE--LSERYglDVDPdakvEDLSVGEQQRVEILKALYRGARILILDEP 168
|
|
| anch_rpt_ABC |
TIGR03771 |
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ... |
22-194 |
1.07e-17 |
|
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 78.35 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 22 FTVDKGDIVTLMGPSGCGKSTLFSWMIGALA---GQFSCTGElwlneqridMLPTAQRQIGILFQDALLFDQFSVG-QNL 97
Cdd:TIGR03771 1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPpakGTVKVAGA---------SPGKGWRHIGYVPQRHEFAWDFPISvAHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 98 LLALPSTLKGTARRN------AVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDN 171
Cdd:TIGR03771 72 VMSGRTGHIGWLRRPcvadfaAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
|
170 180
....*....|....*....|...
gi 300840748 172 FRQwVFSEVRELAIPVVQVTHDL 194
Cdd:TIGR03771 152 LTE-LFIELAGAGTAILMTTHDL 173
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-206 |
1.08e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 79.26 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPE-SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGelwLNEQRIDMLPTAQR 76
Cdd:PRK13644 1 MIRLENVSYSYPDgTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrpqKGKVLVSG---IDTGDFSKLQGIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALlfDQF---SVGQNLL-----LALPSTlkgtARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRAL 148
Cdd:PRK13644 78 LVGIVFQNPE--TQFvgrTVEEDLAfgpenLCLPPI----EIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGIL 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300840748 149 LAQPKALLLDEPFSRLD----VALRDNFRQwvfseVRELAIPVVQVTHDLQDVPADSSVLDM 206
Cdd:PRK13644 152 TMEPECLIFDEVTSMLDpdsgIAVLERIKK-----LHEKGKTIVYITHNLEELHDADRIIVM 208
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
12-197 |
1.30e-17 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 78.96 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 12 PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALA---GQFSCTGELWLNEQRIDMlPTAQRQIGILFQDAL-- 86
Cdd:PRK10419 23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESpsqGNVSWRGEPLAKLNRAQR-KAFRRDIQMVFQDSIsa 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 87 LFDQFSVGQnlLLALP----STLKGTARRNAVKDALDRAGLAETYHQD-PATLSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:PRK10419 102 VNPRKTVRE--IIREPlrhlLSLDKAERLARASEMLRAVDLDDSVLDKrPPQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190
....*....|....*....|....*....|....*.
gi 300840748 162 SRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLV 215
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-170 |
1.55e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 80.11 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEqridmlpTAqrQIGILFQ 83
Cdd:COG0488 318 LEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD---SGTVKLGE-------TV--KIGYFDQ 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 84 DallFDQFSVGQNLLLALpSTLKGTARRNAVKDALDRAGLAETYHQDP-ATLSGGQRARVALLRALLAQPKALLLDEPFS 162
Cdd:COG0488 386 H---QEELDPDKTVLDEL-RDGAPGGTEQEVRGYLGRFLFSGDDAFKPvGVLSGGEKARLALAKLLLSPPNVLLLDEPTN 461
|
....*...
gi 300840748 163 RLDVALRD 170
Cdd:COG0488 462 HLDIETLE 469
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
4-197 |
2.06e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 78.17 E-value: 2.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLF---SWMIGALAGQFSCTGE-LWLNEQ--RIDMLpTAQRQ 77
Cdd:PRK14246 13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLkvlNRLIEIYDSKIKVDGKvLYFGKDifQIDAI-KLRKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQFSVGQNLLLALPSTLKGTAR--RNAVKDALDRAGLAETYH---QDPAT-LSGGQRARVALLRALLAQ 151
Cdd:PRK14246 92 VGMVFQQPNPFPHLSIYDNIAYPLKSHGIKEKReiKKIVEECLRKVGLWKEVYdrlNSPASqLSGGQQQRLTIARALALK 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 152 PKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIpvVQVTHDLQDV 197
Cdd:PRK14246 172 PKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAI--VIVSHNPQQV 215
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-167 |
3.28e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.45 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFSCTGElwlnEQRIDMLPTAQRQ 77
Cdd:PRK13539 2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGllpPAAGTIKLDGG----DIDDPDVAEACHY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGilFQDALLfDQFSVGQNllLALPSTLKGTARRnAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:PRK13539 78 LG--HRNAMK-PALTVAEN--LEFWAAFLGGEEL-DIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWIL 151
|
170
....*....|
gi 300840748 158 DEPFSRLDVA 167
Cdd:PRK13539 152 DEPTAALDAA 161
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
12-165 |
3.78e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 79.32 E-value: 3.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 12 PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQRIDmLPTAQRQIGILFQDALLFDQF 91
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPID-AKEMRAISAYVQQDDLFIPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 92 SVGQNLL----LALPSTLKGTARRNAVKDALDRAGL---AETYHQDPAT---LSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:TIGR00955 115 TVREHLMfqahLRMPRRVTKKEKRERVDEVLQALGLrkcANTRIGVPGRvkgLSGGERKRLAFASELLTDPPLLFCDEPT 194
|
....
gi 300840748 162 SRLD 165
Cdd:TIGR00955 195 SGLD 198
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
14-166 |
4.38e-17 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 79.01 E-value: 4.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 14 SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLP-TAQRQ-IGILFQDALLFDQf 91
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR---SGEILLNGFSLKDIDrHTLRQfINYLPQEPYIFSG- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 92 SVGQNLLLAlpstlkgtARRNAVKDALDRA---------------GLAETYHQDPATLSGGQRARVALLRALLAQPKALL 156
Cdd:TIGR01193 563 SILENLLLG--------AKENVSQDEIWAAceiaeikddienmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLI 634
|
170
....*....|
gi 300840748 157 LDEPFSRLDV 166
Cdd:TIGR01193 635 LDESTSNLDT 644
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
12-197 |
4.70e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 79.00 E-value: 4.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 12 PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTlfswmIGALAGQF--SCTGELWLNEQRIDMLP--TAQRQIGILFQDALL 87
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKST-----VAALLQNLyqPTGGQVLLDGVPLVQYDhhYLHRQVALVGQEPVL 566
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 88 FDQfSVGQNLLLALPSTLKGTARRNAVKDALDR--AGLAETYHQDPAT----LSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:TIGR00958 567 FSG-SVRENIAYGLTDTPDEEIMAAAKAANAHDfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190
....*....|....*....|....*....|....*.
gi 300840748 162 SRLDVALRDNFRQWVFSEVRelaiPVVQVTHDLQDV 197
Cdd:TIGR00958 646 SALDAECEQLLQESRSRASR----TVLLIAHRLSTV 677
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-194 |
5.41e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 77.84 E-value: 5.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKN--VSLRLPESrLLTNVN---FTVDKGDIVTLMGPSGCGKS-TLFSWMiGALAGQFSCTGELWLNEQRIDMLPTA 74
Cdd:PRK09473 12 LLDVKDlrVTFSTPDG-DVTAVNdlnFSLRAGETLGIVGESGSGKSqTAFALM-GLLAANGRIGGSATFNGREILNLPEK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 Q------RQIGILFQDAL--LFDQFSVGQNLL--LALPSTL-KGTARRNAVKdALDRAGLAET------YhqdPATLSGG 137
Cdd:PRK09473 90 ElnklraEQISMIFQDPMtsLNPYMRVGEQLMevLMLHKGMsKAEAFEESVR-MLDAVKMPEArkrmkmY---PHEFSGG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 300840748 138 QRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:PRK09473 166 MRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDL 222
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
6-200 |
5.52e-17 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 76.15 E-value: 5.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 6 NVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAG-QFSCTGELWLNEqridmlptaqrqigiLFQD 84
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGtPVAGCVDVPDNQ---------------FGRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 85 ALLFDQFSVGQNLllalpstlkgtarrNAVKDALDRAGLAE--TYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFS 162
Cdd:COG2401 100 ASLIDAIGRKGDF--------------KDAVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 163 RLD--VALRDNFRqwVFSEVRELAIPVVQVTHDlQDVPAD 200
Cdd:COG2401 166 HLDrqTAKRVARN--LQKLARRAGITLVVATHH-YDVIDD 202
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
5-194 |
5.89e-17 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 77.10 E-value: 5.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLP--ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDM--LPTAQRQIGI 80
Cdd:PRK13648 11 KNVSFQYQsdASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK---SGEIFYNNQAITDdnFEKLRKHIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALlfDQFsVGQNLLLALPSTLKGTA-----RRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKAL 155
Cdd:PRK13648 88 VFQNPD--NQF-VGSIVKYDVAFGLENHAvpydeMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVI 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 156 LLDEPFSRLDVALRDNfrqwVFSEVRELA----IPVVQVTHDL 194
Cdd:PRK13648 165 ILDEATSMLDPDARQN----LLDLVRKVKsehnITIISITHDL 203
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
4-204 |
6.30e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 77.15 E-value: 6.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFsctgelwLNEQRIDMLPTA------- 74
Cdd:PRK13640 8 FKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDD-------NPNSKITVDGITltaktvw 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 --QRQIGILFQDAllFDQF---SVGQNLLLALPStlKGTARRNAVK---DALDRAGLAETYHQDPATLSGGQRARVALLR 146
Cdd:PRK13640 81 diREKVGIVFQNP--DNQFvgaTVGDDVAFGLEN--RAVPRPEMIKivrDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 147 ALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDVPADSSVL 204
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVL 214
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
2-192 |
7.31e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 76.49 E-value: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIgALAGQFSCTGELWLNEQRIDMLPTAQ--R 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLlrvFNRLI-ELYPEARVSGEVYLDGQDIFKMDVIElrR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQFSVGQNLLLALPSTLKGTARRN---AVKDALDRAGLAETYHQD---PA-TLSGGQRARVALLRALL 149
Cdd:PRK14247 83 RVQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKElqeRVRWALEKAQLWDEVKDRldaPAgKLSGGQQQRLCIARALA 162
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 150 AQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIpvVQVTH 192
Cdd:PRK14247 163 FQPEVLLADEPTANLDPENTAKIESLFLELKKDMTI--VLVTH 203
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
6-167 |
8.15e-17 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 78.46 E-value: 8.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 6 NVSLRLPESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGAL-------AGQFSCTGelwlneqrIDM----LPT 73
Cdd:PRK13657 339 DVSFSYDNSRQgVEDVSFEAKPGQTVAIVGPTGAGKSTL----INLLqrvfdpqSGRILIDG--------TDIrtvtRAS 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 74 AQRQIGILFQDALLFDQfSVGQNLLL----ALPSTLKGTARRNAVKDALDRA--GLAETYHQDPATLSGGQRARVALLRA 147
Cdd:PRK13657 407 LRRNIAVVFQDAGLFNR-SIEDNIRVgrpdATDEEMRAAAERAQAHDFIERKpdGYDTVVGERGRQLSGGERQRLAIARA 485
|
170 180
....*....|....*....|
gi 300840748 148 LLAQPKALLLDEPFSRLDVA 167
Cdd:PRK13657 486 LLKDPPILILDEATSALDVE 505
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
1-192 |
1.39e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.65 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRL--PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIgALAGQFSCTGELWLNEQRI---DMLP 72
Cdd:PRK14267 2 KFAIETVNLRVyyGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtFNRLL-ELNEEARVEGEVRLFGRNIyspDVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 73 T-AQRQIGILFQDALLFDQFSVGQNLLLALpsTLKGTARRNA-----VKDALDRAGLAET----YHQDPATLSGGQRARV 142
Cdd:PRK14267 81 IeVRREVGMVFQYPNPFPHLTIYDNVAIGV--KLNGLVKSKKelderVEWALKKAALWDEvkdrLNDYPSNLSGGQRQRL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 143 ALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIpvVQVTH 192
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTH 206
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
17-196 |
1.54e-16 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 77.00 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKST---LFSWMIGALAGQFSCTGELWLNEQRIDMLPTAQRQIGILFQDALLFDQFSV 93
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTmvrLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 94 GQNLLLALP-STLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNF 172
Cdd:PRK10070 124 LDNTAFGMElAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180
....*....|....*....|....
gi 300840748 173 RQWVFSEVRELAIPVVQVTHDLQD 196
Cdd:PRK10070 204 QDELVKLQAKHQRTIVFISHDLDE 227
|
|
| CP_lyasePhnK |
TIGR02323 |
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ... |
19-194 |
1.77e-16 |
|
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: 75.64 E-value: 1.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQRIDM--LPTAQRQI------GILFQDAL--LF 88
Cdd:TIGR02323 21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELyqLSEAERRRlmrtewGFVHQNPRdgLR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 89 DQFSVGQNL---LLALPSTLKGTARRNAVkDALDRAGLAETYHQD-PATLSGGQRARVALLRALLAQPKALLLDEPFSRL 164
Cdd:TIGR02323 101 MRVSAGANIgerLMAIGARHYGNIRATAQ-DWLEEVEIDPTRIDDlPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGGL 179
|
170 180 190
....*....|....*....|....*....|
gi 300840748 165 DVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:TIGR02323 180 DVSVQARLLDLLRGLVRDLGLAVIIVTHDL 209
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
2-199 |
1.83e-16 |
|
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: 74.32 E-value: 1.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELwLNEQRidmlPTAQRQI 78
Cdd:TIGR01189 1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLrpdSGEVRWNGTP-LAEQR----DEPHENI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLALPstLKGTARRNaVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:TIGR01189 76 LYLGHLPGLKPELSALENLHFWAA--IHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILD 152
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDVPA 199
Cdd:TIGR01189 153 EPTTALDKAGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
1-193 |
1.94e-16 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 75.63 E-value: 1.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQF---------SCTGELWLNEQ---RI 68
Cdd:PRK13547 1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTL----LKALAGDLtgggaprgaRVTGDVTLNGEplaAI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 69 DMLPTAQRQiGILFQDALLFDQFSVGQNLLLA-LPSTLKGTARRNAVKD----ALDRAGLAETYHQDPATLSGGQRARVA 143
Cdd:PRK13547 77 DAPRLARLR-AVLPQAAQPAFAFSAREIVLLGrYPHARRAGALTHRDGEiawqALALAGATALVGRDVTTLSGGELARVQ 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 144 LLRAlLAQ----------PKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:PRK13547 156 FARV-LAQlwpphdaaqpPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHD 214
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
2-206 |
2.00e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 75.59 E-value: 2.00e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPesrlltnvnftvdKGDIVTLMGPSGCGKSTL---FSWMIGALAGqFSCTGELW-----LNEQRIDmlPT 73
Cdd:PRK14243 24 LAVKNVWLDIP-------------KNQITAFIGPSGCGKSTIlrcFNRLNDLIPG-FRVEGKVTfhgknLYAPDVD--PV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 74 A-QRQIGILFQDALLF-----DQFSVGQ-------NLLLALPSTLKGTARRNAVKDALDRAGLAetyhqdpatLSGGQRA 140
Cdd:PRK14243 88 EvRRRIGMVFQKPNPFpksiyDNIAYGAringykgDMDELVERSLRQAALWDEVKDKLKQSGLS---------LSGGQQQ 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300840748 141 RVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIpvVQVTHDLQDVpadSSVLDM 206
Cdd:PRK14243 159 RLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQA---ARVSDM 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-166 |
2.26e-16 |
|
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: 77.03 E-value: 2.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRL----PESRLLTNVNFTVDKGDIVTLMGPSGCGKStlfswmIGALA-------GQFSCTGELWLNEQRID 69
Cdd:COG4172 6 LLSVEDLSVAFgqggGTVEAVKGVSFDIAAGETLALVGESGSGKS------VTALSilrllpdPAAHPSGSILFDGQDLL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 70 MLPTAQ------RQIGILFQD---AL--LFdqfSVGQNL--LLALPSTLKGTARRNAVKDALDRAGLAET------Y-HQ 129
Cdd:COG4172 80 GLSERElrrirgNRIAMIFQEpmtSLnpLH---TIGKQIaeVLRLHRGLSGAAARARALELLERVGIPDPerrldaYpHQ 156
|
170 180 190
....*....|....*....|....*....|....*..
gi 300840748 130 dpatLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:COG4172 157 ----LSGGQRQRVMIAMALANEPDLLIADEPTTALDV 189
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
4-194 |
3.51e-16 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 74.58 E-value: 3.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRlpeSRLLTnVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCTGELWLNEQRIDMLPTAQ--RQIGIL 81
Cdd:PRK03695 3 LNDVAVS---TRLGP-LSAEVRAGEILHLVGPNGAGKSTLLA----RMAGLLPGSGSIQFAGQPLEAWSAAElaRHRAYL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDALLFDQFSVGQNLLLALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALL-------AQPKA 154
Cdd:PRK03695 75 SQQQTPPFAMPVFQYLTLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQL 154
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 155 LLLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDL 194
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDR-LLSELCQQGIAVVMSSHDL 193
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
5-165 |
3.71e-16 |
|
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a central component of the secretion machinery that translocates the toxin, hemolysin A, in a Sec-independent fashion across both membranes of E. coli. The hemolysin A (HlyA) transport machinery is composed of the ATP-binding cassette (ABC) transporter HlyB located in the inner membrane, hemolysin D (HlyD), also anchored in the inner membrane, and TolC, which resides in the outer membrane. HlyD apparently forms a continuous channel that bridges the entire periplasm, interacting with TolC and HlyB. This arrangement prevents the appearance of periplasmic intermediates of HlyA during substrate transport. Little is known about the molecular details of HlyA transport, but it is evident that ATP-hydrolysis by the ABC-transporter HlyB is a necessary source of energy.
Pssm-ID: 213219 [Multi-domain] Cd Length: 237 Bit Score: 74.44 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRL-PESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFSCTGelwlNEQRIDMLPTAQRQIG 79
Cdd:cd03252 4 EHVRFRYkPDGPViLDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRfyvPENGRVLVDG----HDLALADPAWLRRQVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQfSVGQNLLLALPStlkgtARRNAVKDALDRAG-------LAETYHQ----DPATLSGGQRARVALLRAL 148
Cdd:cd03252 80 VVLQENVLFNR-SIRDNIALADPG-----MSMERVIEAAKLAGahdfiseLPEGYDTivgeQGAGLSGGQRQRIAIARAL 153
|
170
....*....|....*..
gi 300840748 149 LAQPKALLLDEPFSRLD 165
Cdd:cd03252 154 IHNPRILIFDEATSALD 170
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
1-197 |
5.28e-16 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 75.86 E-value: 5.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRIDML-PTAQRQIG 79
Cdd:PRK15439 11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVP---PDSGTLEIGGNPCARLtPAKAHQLG 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILF--QDALLFDQFSVGQNLLLALPSTLKGTARrnaVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:PRK15439 88 IYLvpQEPLLFPNLSVKENILFGLPKRQASMQK---MKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILIL 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 158 DEPFSRLDVALRDNFrqwvFSEVREL---AIPVVQVTHDLQDV 197
Cdd:PRK15439 165 DEPTASLTPAETERL----FSRIRELlaqGVGIVFISHKLPEI 203
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
4-197 |
5.90e-16 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 75.13 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPEsrlltnvnftvdkGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFsctgeLWLNEQRIDMLPTAQRQ--- 77
Cdd:PRK15079 37 VDGVTLRLYE-------------GETLGVVGESGCGKSTFARAIIGlvkATDGEV-----AWLGKDLLGMKDDEWRAvrs 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 -IGILFQDAL--LFDQFSVGQnlLLALP-----STLKGTARRNAVKDALDRAGLAETY-HQDPATLSGGQRARVALLRAL 148
Cdd:PRK15079 99 dIQMIFQDPLasLNPRMTIGE--IIAEPlrtyhPKLSRQEVKDRVKAMMLKVGLLPNLiNRYPHEFSGGQCQRIGIARAL 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 300840748 149 LAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK15079 177 ILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVV 225
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
13-197 |
6.27e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 74.29 E-value: 6.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRIDMLPTAQRQIGILFQ--DALL 87
Cdd:PRK13634 19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLqptSGTVTIGERVITAGKKNKKLKPLRKKVGIVFQfpEHQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 88 FDQfSVGQNLLLAlPSTL---KGTARRNAvKDALDRAGLAETY-HQDPATLSGGQRARVALLRALLAQPKALLLDEPFSR 163
Cdd:PRK13634 99 FEE-TVEKDICFG-PMNFgvsEEDAKQKA-REMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|....
gi 300840748 164 LDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK13634 176 LDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDA 209
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
14-197 |
9.58e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 9.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 14 SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALA---GQFSCTGELWLNEQRIDMLPTAQRQIGILFQ--DALLF 88
Cdd:PRK13643 19 SRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQpteGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQfpESQLF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 89 DQfSVGQNLLLAlPSTLkGTARRNAVKDA---LDRAGLA-ETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRL 164
Cdd:PRK13643 99 EE-TVLKDVAFG-PQNF-GIPKEKAEKIAaekLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGL 175
|
170 180 190
....*....|....*....|....*....|...
gi 300840748 165 DVALRDNFRQwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK13643 176 DPKARIEMMQ-LFESIHQSGQTVVLVTHLMDDV 207
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-206 |
1.52e-15 |
|
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: 72.12 E-value: 1.52e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLR-----LPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigalagqfSCTGELWLNEQRIDMLPTaqr 76
Cdd:cd03250 1 ISVEDASFTwdsgeQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLS----------ALLGELEKLSGSVSVPGS--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 qIGILFQDALLFDQfSVGQNLLLALP-------STLKGTArrnavkdaLDR------AGLAETYHQDPATLSGGQRARVA 143
Cdd:cd03250 68 -IAYVSQEPWIQNG-TIRENILFGKPfdeeryeKVIKACA--------LEPdleilpDGDLTEIGEKGINLSGGQKQRIS 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300840748 144 LLRALLAQPKALLLDEPFSRLD--VAlRDNFRQWVFSEVRELAIpVVQVTHDLQDVPADSSVLDM 206
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDahVG-RHIFENCILGLLLNNKT-RILVTHQLQLLPHADQIVVL 200
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
12-197 |
1.53e-15 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 72.50 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 12 PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTA--QRQIGILFQDALLFD 89
Cdd:cd03248 25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ---GGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 90 QfSVGQNLLLALPStlkgtARRNAVKDALDRAG-------LAETYHQDP----ATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:cd03248 102 R-SLQDNIAYGLQS-----CSFECVKEAAQKAHahsfiseLASGYDTEVgekgSQLSGGQKQRVAIARALIRNPQVLILD 175
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIPVvqVTHDLQDV 197
Cdd:cd03248 176 EATSALDAESEQQVQQALYDWPERRTVLV--IAHRLSTV 212
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
13-197 |
1.73e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 73.32 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIGALAGQFSCTGELWLNEQRIDMLPTAQRQIGILFQ--DALL 87
Cdd:PRK13641 19 EKKGLDNISFELEEGSFVALVGHTGSGKSTLmqhFNALLKPSSGTITIAGYHITPETGNKNLKKLRKKVSLVFQfpEAQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 88 FDQfSVGQNLLLAlPSTLKGT---ARRNAVKdALDRAGLAETY-HQDPATLSGGQRARVALLRALLAQPKALLLDEPFSR 163
Cdd:PRK13641 99 FEN-TVLKDVEFG-PKNFGFSedeAKEKALK-WLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAG 175
|
170 180 190
....*....|....*....|....*....|....
gi 300840748 164 LDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK13641 176 LDPEGRKEMMQ-LFKDYQKAGHTVILVTHNMDDV 208
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
13-165 |
2.02e-15 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 74.15 E-value: 2.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfSCTGELWLNEQRidmlPTAQ--RQIGILFQDALLFDQ 90
Cdd:PLN03211 80 ERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN-NFTGTILANNRK----PTKQilKRTGFVTQDDILYPH 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 91 FSVGQNL----LLALPSTLKGTARRNAVKDALDRAGLAETYHQDPAT-----LSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:PLN03211 155 LTVRETLvfcsLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPT 234
|
....
gi 300840748 162 SRLD 165
Cdd:PLN03211 235 SGLD 238
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-208 |
2.03e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 72.72 E-value: 2.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRI--DMLPTAQR 76
Cdd:PRK13632 7 MIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ---SGEIKIDGITIskENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQ--DallfDQF---SVGQNLLLAL------PSTLKgtarrNAVKDALDRAGLAETYHQDPATLSGGQRARVALL 145
Cdd:PRK13632 84 KIGIIFQnpD----NQFigaTVEDDIAFGLenkkvpPKKMK-----DIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300840748 146 RALLAQPKALLLDEPFSRLDVALRDNFRQwVFSEVRELAIP-VVQVTHDLQDVPADSSVLDMAQ 208
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKK-IMVDLRKTRKKtLISITHDMDEAILADKVIVFSE 217
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-194 |
2.88e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.71 E-value: 2.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRL--LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQ--R 76
Cdd:PRK11160 339 LTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQ----LLTRAWDPQqGEILLNGQPIADYSEAAlrQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQfSVGQNLLLALPstlkgTARRNAVKDALDRAGLAETYHQDPA----------TLSGGQRARVALLR 146
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLLAAP-----NASDEALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIAR 488
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 147 ALLAQPKALLLDEPFSRLDvalRDNFRQwVFSEVRELAI--PVVQVTHDL 194
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLD---AETERQ-ILELLAEHAQnkTVLMITHRL 534
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-194 |
4.28e-15 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 71.58 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ--RQI 78
Cdd:PRK11231 2 TLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ---SGTVFLGDKPISMLSSRQlaRRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSV------GQNLLLALPSTLkGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARvALLRALLAQP 152
Cdd:PRK11231 79 ALLPQHHLTPEGITVrelvayGRSPWLSLWGRL-SAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQR-AFLAMVLAQD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 153 KAL-LLDEPFSRLDValrdNFRQWVFSEVRELAI---PVVQVTHDL 194
Cdd:PRK11231 157 TPVvLLDEPTTYLDI----NHQVELMRLMRELNTqgkTVVTVLHDL 198
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
4-165 |
4.36e-15 |
|
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: 73.21 E-value: 4.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLP--ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigaLAGQF--SCTGELWLNEQRID--MLPTAQRQ 77
Cdd:TIGR02203 333 FRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVN-----LIPRFyePDSGQILLDGHDLAdyTLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQfSVGQNLLLALPstlkGTARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALLR 146
Cdd:TIGR02203 408 VALVSQDVVLFND-TIANNIAYGRT----EQADRAEIERALAAAYAQDFVDKLPlgldtpigengVLLSGGQRQRLAIAR 482
|
170
....*....|....*....
gi 300840748 147 ALLAQPKALLLDEPFSRLD 165
Cdd:TIGR02203 483 ALLKDAPILILDEATSALD 501
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
19-194 |
4.44e-15 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 71.94 E-value: 4.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ--RQIGILFQDALLFDQFSVgQN 96
Cdd:PRK10253 25 NLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPA---HGHVWLDGEHIQHYASKEvaRRIGLLAQNATTPGDITV-QE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 97 LLLA--LPSTLKGTARRNAVKDALDRA----GLAETYHQDPATLSGGQRARvALLRALLAQPKA-LLLDEPFSRLDVALR 169
Cdd:PRK10253 101 LVARgrYPHQPLFTRWRKEDEEAVTKAmqatGITHLADQSVDTLSGGQRQR-AWIAMVLAQETAiMLLDEPTTWLDISHQ 179
|
170 180
....*....|....*....|....*
gi 300840748 170 DNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:PRK10253 180 IDLLELLSELNREKGYTLAAVLHDL 204
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-195 |
6.06e-15 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 72.83 E-value: 6.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGAL----AGQFSCTGELwLNEQRIDMLPTAQRQ-IGILFQDALLFDQF 91
Cdd:PRK10535 24 LKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdkptSGTYRVAGQD-VATLDADALAQLRREhFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 92 SVGQNLllALPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVAL 168
Cdd:PRK10535 102 TAAQNV--EVPAVYAGLERKQRLLRAqelLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHS 179
|
170 180
....*....|....*....|....*..
gi 300840748 169 RDNFRQwVFSEVRELAIPVVQVTHDLQ 195
Cdd:PRK10535 180 GEEVMA-ILHQLRDRGHTVIIVTHDPQ 205
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
17-166 |
8.35e-15 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 71.07 E-value: 8.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFSCTGE---LWLNEQRIDMLPTAQR---QIGILFQDALL 87
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGfvrLASGKISILGQptrQALQKNLVAYVPQSEEvdwSFPVLVEDVVM 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300840748 88 FDQFsvGQNLLLALPSTlkgtARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PRK15056 103 MGRY--GHMGWLRRAKK----RDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDV 175
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
17-206 |
9.87e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 70.89 E-value: 9.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKST---LFSWMIGALAGQFSCTGELWLNEQRIDMlptaQRQIGILFQDAllfDQFSV 93
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTtarLIDGLFEEFEGKVKIDGELLTAENVWNL----RRKIGMVFQNP---DNQFV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 94 GQNLL--LALPSTLKGTARRNAVK---DALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVAL 168
Cdd:PRK13642 96 GATVEddVAFGMENQGIPREEMIKrvdEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTG 175
|
170 180 190
....*....|....*....|....*....|....*...
gi 300840748 169 RDNFRQWVFSEVRELAIPVVQVTHDLQDVPADSSVLDM 206
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVM 213
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
17-206 |
1.03e-14 |
|
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: 70.05 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFSCTGELWLNEQRIDMLPTAQRQIGILFQDALLFDQfSV 93
Cdd:cd03290 17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGemqTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 94 GQNLLLALPSTLKgtaRRNAVKDAL------------DRAGLAETyhqdPATLSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:cd03290 96 EENITFGSPFNKQ---RYKAVTDACslqpdidllpfgDQTEIGER----GINLSGGQRQRICVARALYQNTNIVFLDDPF 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 162 SRLDVALRDNFRQ-WVFSEVRELAIPVVQVTHDLQDVPADSSVLDM 206
Cdd:cd03290 169 SALDIHLSDHLMQeGILKFLQDDKRTLVLVTHKLQYLPHADWIIAM 214
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-166 |
1.05e-14 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 71.88 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESR---LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfsCTGELWLNEQRID-------- 69
Cdd:PRK13549 259 ILEVRNLTAWDPVNPhikRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGR--WEGEIFIDGKPVKirnpqqai 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 70 -----MLPTAQRQIGILfqdallfDQFSVGQNLLLA------LPSTLKGTARRNAVKDALDRAGL-AETYHQDPATLSGG 137
Cdd:PRK13549 337 aqgiaMVPEDRKRDGIV-------PVMGVGKNITLAaldrftGGSRIDDAAELKTILESIQRLKVkTASPELAIARLSGG 409
|
170 180
....*....|....*....|....*....
gi 300840748 138 QRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PRK13549 410 NQQKAVLAKCLLLNPKILILDEPTRGIDV 438
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
17-198 |
1.08e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 70.99 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQridmLPTAQRQIGILFQDAllFDQ-FS 92
Cdd:PRK13652 20 LNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILkptSGSVLIRGEPITKEN----IREVRKFVGLVFQNP--DDQiFS 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 93 --VGQNLLLAlPST--LKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVAL 168
Cdd:PRK13652 94 ptVEQDIAFG-PINlgLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQG 172
|
170 180 190
....*....|....*....|....*....|
gi 300840748 169 RDNFRQWVFSEVRELAIPVVQVTHDLQDVP 198
Cdd:PRK13652 173 VKELIDFLNDLPETYGMTVIFSTHQLDLVP 202
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
1-208 |
1.17e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 72.20 E-value: 1.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLT----NVNFTVDKGDIVTLMGPSGCGKS-TLFSWM--IGALAGQFSCtGELWL---NEQRIDM 70
Cdd:PRK10261 12 VLAVENLNIAFMQEQQKIaavrNLSFSLQRGETLAIVGESGSGKSvTALALMrlLEQAGGLVQC-DKMLLrrrSRQVIEL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 71 LPTAQRQ--------IGILFQDAL--LFDQFSVGQNLLLALpSTLKGTARRNAVKDA---LDRAGLAETY---HQDPATL 134
Cdd:PRK10261 91 SEQSAAQmrhvrgadMAMIFQEPMtsLNPVFTVGEQIAESI-RLHQGASREEAMVEAkrmLDQVRIPEAQtilSRYPHQL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300840748 135 SGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLqDVPADSS--VLDMAQ 208
Cdd:PRK10261 170 SGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDM-GVVAEIAdrVLVMYQ 244
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
12-197 |
1.22e-14 |
|
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: 71.78 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 12 PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfsCTGELWLNEQRID-------------MLPTAQRQI 78
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGK--FEGNVFINGKPVDirnpaqairagiaMVPEDRKRH 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILfqdallfDQFSVGQNLLLALPSTLKGTARRNAVK--DALDRAGL---AETYHQD--PATLSGGQRARVALLRALLAQ 151
Cdd:TIGR02633 349 GIV-------PILGVGKNITLSVLKSFCFKMRIDAAAelQIIGSAIQrlkVKTASPFlpIGRLSGGNQQKAVLAKMLLTN 421
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 152 PKALLLDEPFSRLDVALRDNFRQWVFSEVRElAIPVVQVTHDLQDV 197
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEV 466
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
19-169 |
1.90e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 70.20 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRI---DMLPTAQRqIGILFQDAL--LFDQFSV 93
Cdd:PRK15112 31 PLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIE---PTSGELLIDDHPLhfgDYSYRSQR-IRMIFQDPStsLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 94 GQ--NLLLALPSTLKGTARRNAVKDALDRAGL----AETYhqdPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVA 167
Cdd:PRK15112 107 SQilDFPLRLNTDLEPEQREKQIIETLRQVGLlpdhASYY---PHMLAPGQKQRLGLARALILRPKVIIADEALASLDMS 183
|
..
gi 300840748 168 LR 169
Cdd:PRK15112 184 MR 185
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
1-194 |
2.16e-14 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 69.95 E-value: 2.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQRIDM--LPTAQRQI 78
Cdd:PRK11701 6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLyaLSEAERRR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 ------GILFQDAL--LFDQFSVGQNL---LLALPSTLKGTARRNAVkDALDRAGLAETYHQD-PATLSGGQRARVALLR 146
Cdd:PRK11701 86 llrtewGFVHQHPRdgLRMQVSAGGNIgerLMAVGARHYGDIRATAG-DWLERVEIDAARIDDlPTTFSGGMQQRLQIAR 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 300840748 147 ALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:PRK11701 165 NLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDL 212
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
13-197 |
2.22e-14 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 70.16 E-value: 2.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRIDMLPTAQRQIGILFQ--DALL 87
Cdd:PRK13649 19 EGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHvptQGSVRVDDTLITSTSKNKDIKQIRKKVGLVFQfpESQL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 88 FDQfSVGQNLLLAlPSTLkGTARRNAVKDALDR---AGLAET-YHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSR 163
Cdd:PRK13649 99 FEE-TVLKDVAFG-PQNF-GVSQEEAEALAREKlalVGISESlFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAG 175
|
170 180 190
....*....|....*....|....*....|....
gi 300840748 164 LDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK13649 176 LDPKGRKELMT-LFKKLHQSGMTIVLVTHLMDDV 208
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
1-184 |
3.32e-14 |
|
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: 67.84 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRlpesRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFS-CTGELWLNEQRIDMLPTAQR-QI 78
Cdd:cd03215 4 VLEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAE----ALFGLRPpASGEITLDGKPVTRRSPRDAiRA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILF-----QDALLFDQFSVGQNLLLalpstlkgtarrnavkdaldraglaetyhqdPATLSGGQRARVALLRALLAQPK 153
Cdd:cd03215 76 GIAYvpedrKREGLVLDLSVAENIAL-------------------------------SSLLSGGNQQKVVLARWLARDPR 124
|
170 180 190
....*....|....*....|....*....|.
gi 300840748 154 ALLLDEPFSRLDVALRDNfrqwVFSEVRELA 184
Cdd:cd03215 125 VLILDEPTRGVDVGAKAE----IYRLIRELA 151
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-169 |
6.61e-14 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 68.50 E-value: 6.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGE-LW----LNEQRIDMLPTAQ 75
Cdd:PRK13638 1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQ---KGAvLWqgkpLDYSKRGLLALRQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 rQIGILFQDAllfDQ------------FSVgQNLLLALPSTlkgtARRnaVKDALDRAGLAETYHQDPATLSGGQRARVA 143
Cdd:PRK13638 78 -QVATVFQDP---EQqifytdidsdiaFSL-RNLGVPEAEI----TRR--VDEALTLVDAQHFRHQPIQCLSHGQKKRVA 146
|
170 180
....*....|....*....|....*.
gi 300840748 144 LLRALLAQPKALLLDEPFSRLDVALR 169
Cdd:PRK13638 147 IAGALVLQARYLLLDEPTAGLDPAGR 172
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
4-197 |
7.20e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 68.96 E-value: 7.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVS----LRLP-ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQF------------SCTGELWL 63
Cdd:PRK13651 5 VKNIVkifnKKLPtELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLlpdTGTIewifkdeknkkkTKEKEKVL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 64 NE--------QRIDMLPTAQRQIGILFQDA--LLFDQfSVGQNLLLALPSTlkGTARRNAVKDA---LDRAGLAETYHQ- 129
Cdd:PRK13651 85 EKlviqktrfKKIKKIKEIRRRVGVVFQFAeyQLFEQ-TIEKDIIFGPVSM--GVSKEEAKKRAakyIELVGLDESYLQr 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300840748 130 DPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD-VALRDNFRqwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK13651 162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEILE--IFDNLNKQGKTIILVTHDLDNV 228
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
4-174 |
9.26e-14 |
|
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: 67.52 E-value: 9.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRL-PESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLP--TAQRQI 78
Cdd:cd03244 5 FKNVSLRYrPNLPPvLKNISFSIKPGEKVGIVGRTGSGKSSLLL----ALFRLVELSsGSILIDGVDISKIGlhDLRSRI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDqfsvgqnlllalpstlkGTARRN----------AVKDALDRAGLAETYHQDP-----------ATLSGG 137
Cdd:cd03244 81 SIIPQDPVLFS-----------------GTIRSNldpfgeysdeELWQALERVGLKEFVESLPggldtvveeggENLSVG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 300840748 138 QRARVALLRALLAQPKALLLDEPFSRLDVA--------LRDNFRQ 174
Cdd:cd03244 144 QRQLLCLARALLRKSKILVLDEATASVDPEtdaliqktIREAFKD 188
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
6-183 |
1.23e-13 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 68.78 E-value: 1.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 6 NVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTA---QRQIGILF 82
Cdd:PRK11288 9 GIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPD---AGSILIDGQEMRFASTTaalAAGVAIIY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQNLLL-ALPSTL----KGTARRNAvKDALDRAGLaetyHQDPAT----LSGGQRARVALLRALLAQPK 153
Cdd:PRK11288 86 QELHLVPEMTVAENLYLgQLPHKGgivnRRLLNYEA-REQLEHLGV----DIDPDTplkyLSIGQRQMVEIAKALARNAR 160
|
170 180 190
....*....|....*....|....*....|
gi 300840748 154 ALLLDEPFSRLDVALRDNfrqwVFSEVREL 183
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQ----LFRVIREL 186
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
13-197 |
2.43e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 67.34 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQfSCTGELWL--NEQRIDMLPTAQRQIGILFQdall 87
Cdd:PRK13645 23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIiseTGQ-TIVGDYAIpaNLKKIKEVKRLRKEIGLVFQ---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 88 FDQFSVGQNLL---LALPSTLKGTARRNAVK---DALDRAGLAETY-HQDPATLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:PRK13645 98 FPEYQLFQETIekdIAFGPVNLGENKQEAYKkvpELLKLVQLPEDYvKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 300840748 161 FSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQV 214
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
19-172 |
2.69e-13 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 68.23 E-value: 2.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRI---DMlpTAQRQIGILFQDALLFDQFSVGQ 95
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLP---ASEGEAWLFGQPVdagDI--ATRRRVGYMSQAFSLYGELTVRQ 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 96 NLLL-----ALPstlkGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRD 170
Cdd:NF033858 359 NLELharlfHLP----AAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARD 434
|
..
gi 300840748 171 NF 172
Cdd:NF033858 435 MF 436
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
5-193 |
3.26e-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: 67.65 E-value: 3.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGaLAGQFSctGELWlneqridmlPTAQRQIGILFQ 83
Cdd:TIGR03719 8 NRVSKVVPPKKeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAG-VDKDFN--GEAR---------PQPGIKVGYLPQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 84 DALLFDQFSVGQNLLLALPSTLKGTARRNAV---------------------KDALDRAGLAETYHQ------------- 129
Cdd:TIGR03719 76 EPQLDPTKTVRENVEEGVAEIKDALDRFNEIsakyaepdadfdklaaeqaelQEIIDAADAWDLDSQleiamdalrcppw 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300840748 130 --DPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD---VAlrdnfrqWVFSEVRELAIPVVQVTHD 193
Cdd:TIGR03719 156 daDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDaesVA-------WLERHLQEYPGTVVAVTHD 217
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
4-194 |
8.18e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 65.58 E-value: 8.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGalAGQFSCTGELWLNEQRIDMLPTA--QRQIGIL 81
Cdd:PRK10575 14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLK-MLG--RHQPPSEGEILLDAQPLESWSSKafARKVAYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDALLFDQFSVGQnlLLAL---P--STLK--GTARRNAVKDALDRAGLAETYHQDPATLSGGQRARvALLRALLAQ-PK 153
Cdd:PRK10575 91 PQQLPAAEGMTVRE--LVAIgryPwhGALGrfGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQR-AWIAMLVAQdSR 167
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 300840748 154 ALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDI 208
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
4-167 |
9.69e-13 |
|
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: 64.36 E-value: 9.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLR----LPEsrLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLP--TAQRQ 77
Cdd:cd03369 9 VENLSVRyapdLPP--VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE---EGKIEIDGIDISTIPleDLRSS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDqfsvgqnlllalpstlkGTARRNAvkDALDRAGLAETY-----HQDPATLSGGQRARVALLRALLAQP 152
Cdd:cd03369 84 LTIIPQDPTLFS-----------------GTIRSNL--DPFDEYSDEEIYgalrvSEGGLNLSQGQRQLLCLARALLKRP 144
|
170
....*....|....*
gi 300840748 153 KALLLDEPFSRLDVA 167
Cdd:cd03369 145 RVLVLDEATASIDYA 159
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
17-200 |
1.02e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 65.49 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGelwLNEQRIDMLPTAQRQIGILFQD-------AL 86
Cdd:PRK13633 26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLipsEGKVYVDG---LDTSDEENLWDIRNKAGMVFQNpdnqivaTI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 87 LFDQFSVGQNLLLALPSTLkgtarRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PRK13633 103 VEEDVAFGPENLGIPPEEI-----RERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 167 ALRDNfrqwVFSEVREL----AIPVVQVTHDLQD-VPAD 200
Cdd:PRK13633 178 SGRRE----VVNTIKELnkkyGITIILITHYMEEaVEAD 212
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
4-212 |
4.19e-12 |
|
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: 64.44 E-value: 4.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---------------------------ALAGQ-- 54
Cdd:TIGR03269 3 VKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdqyeptsgriiyhvalcekcgyverpSKVGEpc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 55 FSCTGELwlNEQRIDMLPTAQ-------RQIGILFQDAL-LFDQFSVGQNLLLALPSTlkGTARRNAVKDALDRAGLAET 126
Cdd:TIGR03269 83 PVCGGTL--EPEEVDFWNLSDklrrrirKRIAIMLQRTFaLYGDDTVLDNVLEALEEI--GYEGKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 127 YHQD---PATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHdLQDVPADssV 203
Cdd:TIGR03269 159 SHRIthiARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH-WPEVIED--L 235
|
....*....
gi 300840748 204 LDMAQWSEN 212
Cdd:TIGR03269 236 SDKAIWLEN 244
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
12-165 |
6.13e-12 |
|
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: 64.07 E-value: 6.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 12 PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTlfswmIGALAGQF--SCTGELWLNEQRIDMLPTA--QRQIGILFQDALL 87
Cdd:COG5265 369 PERPILKGVSFEVPAGKTVAIVGPSGAGKST-----LARLLFRFydVTSGRILIDGQDIRDVTQAslRAAIGIVPQDTVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 88 FDQfSVGQNLLLALPStlkgtARRNAVKDALDRA-------GLAETYHqdpaT--------LSGGQRARVALLRALLAQP 152
Cdd:COG5265 444 FND-TIAYNIAYGRPD-----ASEEEVEAAARAAqihdfieSLPDGYD----TrvgerglkLSGGEKQRVAIARTLLKNP 513
|
170
....*....|...
gi 300840748 153 KALLLDEPFSRLD 165
Cdd:COG5265 514 PILIFDEATSALD 526
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
1-165 |
6.34e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.27 E-value: 6.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDM-LPTAQRQIG 79
Cdd:PRK13540 1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPE---KGEILFERQSIKKdLCTYQKQLC 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQFSVGQNLLLALpstlkGTARRNAVKDALDRAGLAETYHQDP-ATLSGGQRARVALLRALLAQPKALLLD 158
Cdd:PRK13540 78 FVGHRSGINPYLTLRENCLYDI-----HFSPGAVGITELCRLFSLEHLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLD 152
|
....*..
gi 300840748 159 EPFSRLD 165
Cdd:PRK13540 153 EPLVALD 159
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-203 |
7.64e-12 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 64.03 E-value: 7.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLnEQRIDMLP------TAQRQIGILFQD---- 84
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTL----LQSLLSQFEISeGRVWA-ERSIAYVPqqawimNATVRGNILFFDeeda 749
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 85 ALLFDQFSVGQnlLLALPSTLKGtarrnavkdaldraGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRL 164
Cdd:PTZ00243 750 ARLADAVRVSQ--LEADLAQLGG--------------GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 300840748 165 DV-----ALRDNFRQWVFSEVRELAipvvqvTHDLQDVP-ADSSV 203
Cdd:PTZ00243 814 DAhvgerVVEECFLGALAGKTRVLA------THQVHVVPrADYVV 852
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
4-165 |
8.06e-12 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 63.50 E-value: 8.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLP--ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTlfswmIGALAGQF--SCTGELWLNEQRID--MLPTAQRQ 77
Cdd:PRK11176 344 FRNVTFTYPgkEVPALRNINFKIPAGKTVALVGRSGSGKST-----IANLLTRFydIDEGEILLDGHDLRdyTLASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQfSVGQNLLLALPSTLKGTARRNAVKDA--------LDRaGLAETYHQDPATLSGGQRARVALLRALL 149
Cdd:PRK11176 419 VALVSQNVHLFND-TIANNIAYARTEQYSREQIEEAARMAyamdfinkMDN-GLDTVIGENGVLLSGGQRQRIAIARALL 496
|
170
....*....|....*.
gi 300840748 150 AQPKALLLDEPFSRLD 165
Cdd:PRK11176 497 RDSPILILDEATSALD 512
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
13-165 |
8.13e-12 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 63.33 E-value: 8.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFsctGELWL------------------NEQRIDMLPTA 74
Cdd:PRK13631 38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKY---GTIQVgdiyigdkknnhelitnpYSKKIKNFKEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 QRQIGILFQ--DALLFDQfSVGQNLLLAlPSTL---KGTARRNAvKDALDRAGLAETY-HQDPATLSGGQRARVALLRAL 148
Cdd:PRK13631 115 RRRVSMVFQfpEYQLFKD-TIEKDIMFG-PVALgvkKSEAKKLA-KFYLNKMGLDDSYlERSPFGLSGGQKRRVAIAGIL 191
|
170
....*....|....*..
gi 300840748 149 LAQPKALLLDEPFSRLD 165
Cdd:PRK13631 192 AIQPEILIFDEPTAGLD 208
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
19-208 |
1.06e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 63.15 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQR-QIGILF-----QDALLFDQFS 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPAR---GGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAP 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 93 VGQN---LLLALPSTLKGTARRNAVKDALDRA-GLAETYHQDPA-TLSGGQRARVALLRALLAQPKALLLDEPFSRLDVA 167
Cdd:PRK15439 358 LAWNvcaLTHNRRGFWIKPARENAVLERYRRAlNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 168 LRDNFRQWVFSeVRELAIPVVQVTHDLQDVP--ADsSVLDMAQ 208
Cdd:PRK15439 438 ARNDIYQLIRS-IAAQNVAVLFISSDLEEIEqmAD-RVLVMHQ 478
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-165 |
1.14e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 62.93 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 20 VNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRIdmlptAQRQIGILFQDALLFDQFSVGQN 96
Cdd:PRK13536 60 LSFTVASGECFGLLGPNGAGKSTIARMILGMTspdAGKITVLGVPVPARARL-----ARARIGVVPQFDNLDLEFTVREN 134
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300840748 97 LLLaLPSTLKGTARR--NAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:PRK13536 135 LLV-FGRYFGMSTREieAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLD 204
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
5-193 |
1.20e-11 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 63.07 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLFswMIgaLAGQFSCT-GELWLNEQRIDML-PTAQRQ-IGI 80
Cdd:PRK10522 326 RNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLA--ML--LTGLYQPQsGEILLDGKPVTAEqPEDYRKlFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNlllalpstlkGTARRNAVKDALDRAGLAETYHQDPAT-----LSGGQRARVALLRALLAQPKAL 155
Cdd:PRK10522 402 VFTDFHLFDQLLGPEG----------KPANPALVEKWLERLKMAHKLELEDGRisnlkLSKGQKKRLALLLALAEERDIL 471
|
170 180 190
....*....|....*....|....*....|....*...
gi 300840748 156 LLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHD 193
Cdd:PRK10522 472 LLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD 509
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-197 |
1.24e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.19 E-value: 1.24e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKS-TLFSWM-------IGALAGQFSCTGELWLN--EQRIDMLptAQRQIGILF 82
Cdd:PRK15134 21 VRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsppVVYPSGDIRFHGESLLHasEQTLRGV--RGNKIAMIF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDAL--LFDQFSVGQNL--LLALPSTLKGTARRNAVKDALDRAGL---AETYHQDPATLSGGQRARVALLRALLAQPKAL 155
Cdd:PRK15134 99 QEPMvsLNPLHTLEKQLyeVLSLHRGMRREAARGEILNCLDRVGIrqaAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 300840748 156 LLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIV 220
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
4-194 |
1.47e-11 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 62.06 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPE-SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFSCTGELwLNEQRIDMLptaQRQIG 79
Cdd:PRK13647 7 VEDLHFRYKDgTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiylPQRGRVKVMGRE-VNAENEKWV---RSKVG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQD-------ALLFDQFSVG-QNLLLAlPSTLKgtarrNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQ 151
Cdd:PRK13647 83 LVFQDpddqvfsSTVWDDVAFGpVNMGLD-KDEVE-----RRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 152 PKALLLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDL 194
Cdd:PRK13647 157 PDVIVLDEPMAYLDPRGQETLME-ILDRLHNQGKTVIVATHDV 198
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-166 |
1.53e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 1.53e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALA---GQFSCTGELWLNEQRIDMLPTAQRQiGILFqdALLFDQFs 92
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEpseGKIKHSGRISFSPQTSWIMPGTIKD-NIIF--GLSYDEY- 516
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 93 vgqnlllalpstlKGTARRNAVKDALDRAGLAE----TYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:TIGR01271 517 -------------RYTSVIKACQLEEDIALFPEkdktVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
34-193 |
1.80e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 34 GPSGCGKSTLFSWMIGaLAGQFscTGELWlneqridmlPTAQRQIGILFQDALLFDQFSVGQNLLLALPSTLKGTARRNA 113
Cdd:PRK11819 40 GLNGAGKSTLLRIMAG-VDKEF--EGEAR---------PAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 114 V---------------------KDALDRAGLAETYHQ---------------DPATLSGGQRARVALLRALLAQPKALLL 157
Cdd:PRK11819 108 IyaayaepdadfdalaaeqgelQEIIDAADAWDLDSQleiamdalrcppwdaKVTKLSGGERRRVALCRLLLEKPDMLLL 187
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 158 DEPFSRLD---VAlrdnfrqWVFSEVRELAIPVVQVTHD 193
Cdd:PRK11819 188 DEPTNHLDaesVA-------WLEQFLHDYPGTVVAVTHD 219
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-167 |
2.55e-11 |
|
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: 61.41 E-value: 2.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRIDMLPTAQRQiGILFqdALLFDQF- 91
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELepsEGKIKHSGRISFSSQFSWIMPGTIKE-NIIF--GVSYDEYr 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 92 --SVGQNLLLAlPSTLKGTARRNAVkdaLDRAGLaetyhqdpaTLSGGQRARVALLRALLAQPKALLLDEPFSRLDVA 167
Cdd:cd03291 129 ykSVVKACQLE-EDITKFPEKDNTV---LGEGGI---------TLSGGQRARISLARAVYKDADLYLLDSPFGYLDVF 193
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
4-169 |
2.93e-11 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 61.36 E-value: 2.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRIdmlptAQRQIGI 80
Cdd:PRK13537 10 FRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLThpdAGSISLCGEPVPSRARH-----ARQRVGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLLL-ALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:PRK13537 85 VPQFDNLDPDFTVRENLLVfGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDE 164
|
170
....*....|
gi 300840748 160 PFSRLDVALR 169
Cdd:PRK13537 165 PTTGLDPQAR 174
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
6-194 |
3.05e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 61.27 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 6 NVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLF---SWMIGALAGqFSCTGELWLNEQRI----DMLpTAQRQI 78
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLrtlNRMNDKVSG-YRYSGDVLLGGRSIfnyrDVL-EFRRRV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFdQFSVGQNLLLALPS-------TLKGTARR--------NAVKDALDRAglaetyhqdPATLSGGQRARVA 143
Cdd:PRK14271 104 GMLFQRPNPF-PMSIMDNVLAGVRAhklvprkEFRGVAQArltevglwDAVKDRLSDS---------PFRLSGGQQQLLC 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 300840748 144 LLRALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAipVVQVTHDL 194
Cdd:PRK14271 174 LARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLT--VIIVTHNL 222
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-199 |
8.77e-11 |
|
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: 60.61 E-value: 8.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSC---TGELWLNEQRI---DMLPTA 74
Cdd:TIGR02633 1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK----ILSGVYPHgtwDGEIYWSGSPLkasNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 QRQIGILFQDALLFDQFSVGQNLLLALPSTLKGTARRNAVKDALDRAGLAE-TYHQDPAT-----LSGGQRARVALLRAL 148
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGNEITLPGGRMAYNAMYLRAKNLLRElQLDADNVTrpvgdYGGGQQQLVEIAKAL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 300840748 149 LAQPKALLLDEPFSrldvALRDNFRQWVFSEVREL---AIPVVQVTHDLQDVPA 199
Cdd:TIGR02633 157 NKQARLLILDEPSS----SLTEKETEILLDIIRDLkahGVACVYISHKLNEVKA 206
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-166 |
1.17e-10 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 60.35 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELwlneqridmlptaqrqigi 80
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLqadSGRIHCGTKL------------------- 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 lfqDALLFDQF--------SVGQNLllalpstlkGTARRNAVKDALDRAGLAetYHQD----PA-------TLSGGQRAR 141
Cdd:PRK11147 383 ---EVAYFDQHraeldpekTVMDNL---------AEGKQEVMVNGRPRHVLG--YLQDflfhPKramtpvkALSGGERNR 448
|
170 180
....*....|....*....|....*
gi 300840748 142 VALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PRK11147 449 LLLARLFLKPSNLLILDEPTNDLDV 473
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-160 |
1.41e-10 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 60.03 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRlpesRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDmLPTAQRQI- 78
Cdd:COG1129 256 VLEVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELAR----ALFGADPADsGEIRLDGKPVR-IRSPRDAIr 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 -GILF------QDALLFDQfSVGQNLLLAlpsTLKGTARRNAVKDALDRAgLAETY-----------HQDPATLSGGQRA 140
Cdd:COG1129 327 aGIAYvpedrkGEGLVLDL-SIRENITLA---SLDRLSRGGLLDRRRERA-LAEEYikrlriktpspEQPVGNLSGGNQQ 401
|
170 180
....*....|....*....|
gi 300840748 141 RVALLRALLAQPKALLLDEP 160
Cdd:COG1129 402 KVVLAKWLATDPKVLILDEP 421
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-165 |
1.45e-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: 60.41 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKN-VSLRLPESR-LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRIDMLPTAQRQ-I 78
Cdd:TIGR01257 929 VCVKNlVKIFEPSGRpAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLP---PTSGTVLVGGKDIETNLDAVRQsL 1005
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLAlpSTLKGTARRNA---VKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKAL 155
Cdd:TIGR01257 1006 GMCPQHNILFHHLTVAEHILFY--AQLKGRSWEEAqleMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVV 1083
|
170
....*....|
gi 300840748 156 LLDEPFSRLD 165
Cdd:TIGR01257 1084 VLDEPTSGVD 1093
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-164 |
1.94e-10 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 59.56 E-value: 1.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALA-GQFSctGELWLNEQRI---DMLPTAQR 76
Cdd:PRK13549 5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPhGTYE--GEIIFEGEELqasNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGILFQDALLFDQFSVGQNLLLALPSTLKGTARRNAV----KDALDRAGLaetyHQDPAT----LSGGQRARVALLRAL 148
Cdd:PRK13549 83 GIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMylraQKLLAQLKL----DINPATpvgnLGLGQQQLVEIAKAL 158
|
170
....*....|....*.
gi 300840748 149 LAQPKALLLDEPFSRL 164
Cdd:PRK13549 159 NKQARLLILDEPTASL 174
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
17-197 |
2.00e-10 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 58.95 E-value: 2.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGEL-WlnEQRIDMLptaqRQIGILFqdallfdqfs 92
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILvptSGEVRVLGYVpF--KRRKEFA----RRIGVVF---------- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 93 vGQ--NLLLALP--STLKGTAR-----RNAVKDALDRA----GLAETYHQdPA-TLSGGQRARVALLRALLAQPKALLLD 158
Cdd:COG4586 102 -GQrsQLWWDLPaiDSFRLLKAiyripDAEYKKRLDELvellDLGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLD 179
|
170 180 190
....*....|....*....|....*....|....*....
gi 300840748 159 EPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDV 197
Cdd:COG4586 180 EPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDI 218
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-164 |
2.51e-10 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 59.41 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGA---LAGQFSCTGELWlneQRIDMLPTAQRQIGI 80
Cdd:PRK09700 8 MAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIhepTKGTITINNINY---NKLDHKLAAQLGIGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDALLFDQFSVGQNLLLALPSTLK--------GTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQP 152
Cdd:PRK09700 85 IYQELSVIDELTVLENLYIGRHLTKKvcgvniidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDA 164
|
170
....*....|..
gi 300840748 153 KALLLDEPFSRL 164
Cdd:PRK09700 165 KVIIMDEPTSSL 176
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
13-197 |
2.78e-10 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 58.64 E-value: 2.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 13 ESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRI------DMLPTAQRQIGILFQ--D 84
Cdd:PRK13646 19 EHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLK---PTTGTVTVDDITIthktkdKYIRPVRKRIGMVFQfpE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 85 ALLFDQfSVGQNLLLAlPSTLK---GTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:PRK13646 96 SQLFED-TVEREIIFG-PKNFKmnlDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 300840748 162 SRLDvalrDNFRQWVFSEVRELAI----PVVQVTHDLQDV 197
Cdd:PRK13646 174 AGLD----PQSKRQVMRLLKSLQTdenkTIILVSHDMNEV 209
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-169 |
3.47e-10 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.11 E-value: 3.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT---GE-LWLNEQRIDMLPTAQR 76
Cdd:CHL00131 7 ILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSK----VIAGHPAYKileGDiLFKGESILDLEPEERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 77 QIGIL--FQDALLFDQFSVGQNLLLALPSTLKGTARRNA--------VKDALDRAGLAETY-HQD-PATLSGGQRARVAL 144
Cdd:CHL00131 83 HLGIFlaFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELdplefleiINEKLKLVGMDPSFlSRNvNEGFSGGEKKRNEI 162
|
170 180
....*....|....*....|....*.
gi 300840748 145 LRALLAQPKALLLDEPFSRLDV-ALR 169
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIdALK 188
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
26-206 |
3.78e-10 |
|
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: 58.64 E-value: 3.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 26 KGDIVTLMGPSGCGKSTlfswMIGALAGqfsctgELWLNEQRIDMLPTAQRqigIL--FQDALLFDQFS--VGQNLLLA- 100
Cdd:COG1245 98 KGKVTGILGPNGIGKST----ALKILSG------ELKPNLGDYDEEPSWDE---VLkrFRGTELQDYFKklANGEIKVAh 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 101 -------LPSTLKGTAR--------RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:COG1245 165 kpqyvdlIPKVFKGTVRellekvdeRGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 300840748 166 VALRDNfrqwVFSEVRELA---IPVVQVTHDLqdvpadsSVLDM 206
Cdd:COG1245 245 IYQRLN----VARLIRELAeegKYVLVVEHDL-------AILDY 277
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
1-160 |
4.67e-10 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 57.99 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPES----RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGE-LWLNEqrIDML---P 72
Cdd:COG4170 3 LLDIRNLTIEIDTPqgrvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDNWHVTADrFRWNG--IDLLklsP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 73 TAQRQ-----IGILFQDAL--LFDQFSVGQNLLLALPS-TLKGT------ARRNAVKDALDRAGLAEtyHQD-----PAT 133
Cdd:COG4170 81 RERRKiigreIAMIFQEPSscLDPSAKIGDQLIEAIPSwTFKGKwwqrfkWRKKRAIELLHRVGIKD--HKDimnsyPHE 158
|
170 180
....*....|....*....|....*..
gi 300840748 134 LSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:COG4170 159 LTEGECQKVMIAMAIANQPRLLIADEP 185
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
15-194 |
6.97e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 57.44 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 15 RLLTNVNFTVDKGDIVTLMGPSGCGKStLFSWMIGAL---AGQFSCTgELWLNEQRIDMLPTAQRQ------IGILFQDA 85
Cdd:PRK11022 21 RAVDRISYSVKQGEVVGIVGESGSGKS-VSSLAIMGLidyPGRVMAE-KLEFNGQDLQRISEKERRnlvgaeVAMIFQDP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 86 L--LFDQFSVGQNLLLALPSTLKGT--ARRNAVKDALDRAGLAetyhqDPAT--------LSGGQRARVALLRALLAQPK 153
Cdd:PRK11022 99 MtsLNPCYTVGFQIMEAIKVHQGGNkkTRRQRAIDLLNQVGIP-----DPASrldvyphqLSGGMSQRVMIAMAIACRPK 173
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 300840748 154 ALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:PRK11022 174 LLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDL 214
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
17-175 |
8.05e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 57.80 E-value: 8.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELwlneqRIDMLPTAQRQI-------GILFQDALLF 88
Cdd:PRK10789 331 LENVNFTLKPGQMLGICGPTGSGKSTLLS----LIQRHFDVSeGDI-----RFHDIPLTKLQLdswrsrlAVVSQTPFLF 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 89 DQfSVGQNLLL----ALPSTLKGTARRNAVKDALDRagLAETYHQDPA----TLSGGQRARVALLRALLAQPKALLLDEP 160
Cdd:PRK10789 402 SD-TVANNIALgrpdATQQEIEHVARLASVHDDILR--LPQGYDTEVGergvMLSGGQKQRISIARALLLNAEILILDDA 478
|
170
....*....|....*....
gi 300840748 161 FSRLD----VALRDNFRQW 175
Cdd:PRK10789 479 LSAVDgrteHQILHNLRQW 497
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
15-165 |
1.30e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 55.71 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 15 RLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAG---QFSCTGELWLNEQRIDmlPTAQRQIGILFQDALLFDQF 91
Cdd:cd03232 21 QLLNNISGYVKPGTLTALMGESGAGKTTL----LDVLAGrktAGVITGEILINGRPLD--KNFQRSTGYVEQQDVHSPNL 94
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300840748 92 SVGQNLLLAlpstlkgtarrnavkdALDRAglaetyhqdpatLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:cd03232 95 TVREALRFS----------------ALLRG------------LSVEQRKRLTIGVELAAKPSILFLDEPTSGLD 140
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
19-166 |
3.09e-09 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfSCTGELWLNEQRIDMLpTAQRQI--GILF------QDALLFDq 90
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALP---RTSGYVTLDGHEVVTR-SPQDGLanGIVYisedrkRDGLVLG- 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 91 FSVGQNL-LLALPS------TLKGTARRNAVKDALdRAGLAETYHQDPAT--LSGGQRARVALLRALLAQPKALLLDEPF 161
Cdd:PRK10762 345 MSVKENMsLTALRYfsraggSLKHADEQQAVSDFI-RLFNIKTPSMEQAIglLSGGNQQKVAIARGLMTRPKVLILDEPT 423
|
....*
gi 300840748 162 SRLDV 166
Cdd:PRK10762 424 RGVDV 428
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
23-206 |
3.98e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 3.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 23 TVDKGDIVTLMGPSGCGKSTlfswMIGALAGqfsctgELWLNEQRIDMLPTAQRqigIL--FQDALLFDQFS-VGQNLLL 99
Cdd:PRK13409 95 IPKEGKVTGILGPNGIGKTT----AVKILSG------ELIPNLGDYEEEPSWDE---VLkrFRGTELQNYFKkLYNGEIK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 100 A---------LPSTLKGTAR--------RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFS 162
Cdd:PRK13409 162 VvhkpqyvdlIPKVFKGKVRellkkvdeRGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTS 241
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 163 RLDVALRDNfrqwVFSEVRELA--IPVVQVTHDLqdvpadsSVLDM 206
Cdd:PRK13409 242 YLDIRQRLN----VARLIRELAegKYVLVVEHDL-------AVLDY 276
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
16-194 |
5.58e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 54.71 E-value: 5.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL-AGQFSCTGELWLNEQRIDMLPTAQRQIGILFQDALlfDQFSVG 94
Cdd:PRK10418 18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILpAGVRQTAGRVLLDGKPVAPCALRGRKIATIMQNPR--SAFNPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 95 QNLLLALPSTLK---GTARRNAVKDALDRAGLAET---YHQDPATLSGG--QRARVALlrALLAQPKALLLDEPFSRLDV 166
Cdd:PRK10418 96 HTMHTHARETCLalgKPADDATLTAALEAVGLENAarvLKLYPFEMSGGmlQRMMIAL--ALLCEAPFIIADEPTTDLDV 173
|
170 180
....*....|....*....|....*...
gi 300840748 167 ALRDNFRQWVFSEVRELAIPVVQVTHDL 194
Cdd:PRK10418 174 VAQARILDLLESIVQKRALGMLLVTHDM 201
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-206 |
7.93e-09 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 53.91 E-value: 7.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 27 GDIVTLMGPSGCGKSTlfswMIGALAGQFSCTGELWLNEQRIDMLPTAQRqiGILFQD---ALLFDQFSVG---QNLLLa 100
Cdd:cd03236 26 GQVLGLVGPNGIGKST----ALKILAGKLKPNLGKFDDPPDWDEILDEFR--GSELQNyftKLLEGDVKVIvkpQYVDL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 101 LPSTLKGTAR--------RNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNf 172
Cdd:cd03236 99 IPKAVKGKVGellkkkdeRGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLN- 177
|
170 180 190
....*....|....*....|....*....|....*..
gi 300840748 173 rqwVFSEVRELAIP---VVQVTHDLqdvpadsSVLDM 206
Cdd:cd03236 178 ---AARLIRELAEDdnyVLVVEHDL-------AVLDY 204
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
1-199 |
8.34e-09 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 8.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSC-TGELWLNEQRIDMLPTAQRQig 79
Cdd:PRK10938 3 SLQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALAR----ALAGELPLlSGERQSQFSHITRLSFEQLQ-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ilfqdALLFDQFSVGQNLLLALPSTLKG-TAR---RNAVKDALDRAGLAETYHQDP------ATLSGGQRARVALLRALL 149
Cdd:PRK10938 77 -----KLVSDEWQRNNTDMLSPGEDDTGrTTAeiiQDEVKDPARCEQLAQQFGITAlldrrfKYLSTGETRKTLLCQALM 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 150 AQPKALLLDEPFSRLDVALRDNFRQwVFSEVRELAIPVVQVTHDLQDVPA 199
Cdd:PRK10938 152 SEPDLLILDEPFDGLDVASRQQLAE-LLASLHQSGITLVLVLNRFDEIPD 200
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
17-197 |
1.27e-08 |
|
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: 53.31 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALA---GQFSCTGEL-WLNEqridmlptaqrqIGILFQDALlfdqfS 92
Cdd:cd03220 38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPpdsGTVTVRGRVsSLLG------------LGGGFNPEL-----T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 93 VGQNL-LLALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDN 171
Cdd:cd03220 101 GRENIyLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEK 180
|
170 180
....*....|....*....|....*.
gi 300840748 172 FRQwVFSEVRELAIPVVQVTHDLQDV 197
Cdd:cd03220 181 CQR-RLRELLKQGKTVILVSHDPSSI 205
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
4-170 |
1.58e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIgalAGQfsctgelwlnEQ----RIDMLPTAqrQIG 79
Cdd:TIGR03719 325 AENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFR-MI---TGQ----------EQpdsgTIEIGETV--KLA 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQ--DAL-----LFDQFSVGQNLLL----ALPS-------TLKGTARRNAVKDaldraglaetyhqdpatLSGGQRAR 141
Cdd:TIGR03719 389 YVDQsrDALdpnktVWEEISGGLDIIKlgkrEIPSrayvgrfNFKGSDQQKKVGQ-----------------LSGGERNR 451
|
170 180 190
....*....|....*....|....*....|...
gi 300840748 142 VALLRALLAQPKALLLDEPFSRLDV----ALRD 170
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDVetlrALEE 484
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
5-167 |
2.49e-08 |
|
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: 52.26 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESR----LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGEL-WLNEQRIDMLPTAQRQIG 79
Cdd:cd03233 7 RNISFTTGKGRskipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIhYNGIPYKEFAEKYPGEII 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQFSVGQNLLLALpsTLKGtarrnavkDALDRAglaetyhqdpatLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:cd03233 87 YVSEEDVHFPTLTVRETLDFAL--RCKG--------NEFVRG------------ISGGERKRVSIAEALVSRASVLCWDN 144
|
....*...
gi 300840748 160 PFSRLDVA 167
Cdd:cd03233 145 STRGLDSS 152
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-165 |
4.78e-08 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.64 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFSCTGELWLNEQRIDMLPTAQRQiGILFQDALL--FDQF 91
Cdd:TIGR00957 654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAemdKVEGHVHMKGSVAYVPQQAWIQNDSLRE-NILFGKALNekYYQQ 732
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 92 SVGQNLLLA----LPSTlkgtarrnavkdalDRAGLAETyhqdPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:TIGR00957 733 VLEACALLPdleiLPSG--------------DRTEIGEK----GVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVD 792
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-166 |
6.38e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 52.09 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRlpESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAlagQFSCTGELWLNEQRIDM---LPTAQRQIGI 80
Cdd:PRK09700 268 VRNVTSR--DRKKVRDISFSVCRGEILGFAGLVGSGRTELMNCLFGV---DKRAGGEIRLNGKDISPrspLDAVKKGMAY 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQ---DALLFDQFSVGQNLllALPSTLKGTARRNAVK--DALDRAGLAE-----------TYHQDPATLSGGQRARVAL 144
Cdd:PRK09700 343 ITEsrrDNGFFPNFSIAQNM--AISRSLKDGGYKGAMGlfHEVDEQRTAEnqrellalkchSVNQNITELSGGNQQKVLI 420
|
170 180
....*....|....*....|..
gi 300840748 145 LRALLAQPKALLLDEPFSRLDV 166
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDV 442
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
2-167 |
1.08e-07 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 51.57 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCT-GELWLNEQRIDMLPTAQ-RQI 78
Cdd:COG3845 258 LEVENLSVRDDRGVPaLKDVSLEVRAGEILGIAGVAGNGQSELAE----ALAGLRPPAsGSIRLDGEDITGLSPRErRRL 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILF------QDALLFDqFSVGQNLLL----ALPSTLKGTARRNAVKDALDRagLAETY------HQDPA-TLSGG--QR 139
Cdd:COG3845 334 GVAYipedrlGRGLVPD-MSVAENLILgryrRPPFSRGGFLDRKAIRAFAEE--LIEEFdvrtpgPDTPArSLSGGnqQK 410
|
170 180
....*....|....*....|....*...
gi 300840748 140 ARVAllRALLAQPKALLLDEPFSRLDVA 167
Cdd:COG3845 411 VILA--RELSRDPKLLIAAQPTRGLDVG 436
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
80-165 |
1.13e-07 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 51.57 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDqFSVGQNLLLAlpstlKGTARRNAVKDALDRAGLAETYHQDP-----------ATLSGGQRARVALLRAL 148
Cdd:PTZ00265 1300 IVSQEPMLFN-MSIYENIKFG-----KEDATREDVKRACKFAAIDEFIESLPnkydtnvgpygKSLSGGQKQRIAIARAL 1373
|
90
....*....|....*..
gi 300840748 149 LAQPKALLLDEPFSRLD 165
Cdd:PTZ00265 1374 LREPKILLLDEATSSLD 1390
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
16-166 |
1.36e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 51.40 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCTGELWLNEQRIDMLPTAQRQIgilfqdallfDQFSVGQ 95
Cdd:PLN03073 524 LFKNLNFGIDLDSRIAMVGPNGIGKSTILK----LISGELQPSSGTVFRSAKVRMAVFSQHHV----------DGLDLSS 589
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300840748 96 NLLLALPSTLKGTARRNaVKDALDRAGLAETYHQDPA-TLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PLN03073 590 NPLLYMMRCFPGVPEQK-LRAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDL 660
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
15-165 |
1.69e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.26 E-value: 1.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 15 RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQRIDmlPTAQRQIGILFQDALLFDQFSVG 94
Cdd:TIGR00956 777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTGVITGGDRLVNGRPLD--SSFQRSIGYVQQQDLHLPTSTVR 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 95 QNL----LLALPSTLKGTARRNAVKDALDRAGLaETYHQDPATLSGG-----QRARVALLRALLAQPKALL-LDEPFSRL 164
Cdd:TIGR00956 855 ESLrfsaYLRQPKSVSKSEKMEYVEEVIKLLEM-ESYADAVVGVPGEglnveQRKRLTIGVELVAKPKLLLfLDEPTSGL 933
|
.
gi 300840748 165 D 165
Cdd:TIGR00956 934 D 934
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
4-165 |
1.86e-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: 51.06 E-value: 1.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPES--RLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALA--GQFSCTGELWLNEQridmLPTAQRQIG 79
Cdd:TIGR01271 1220 VQGLTAKYTEAgrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSteGEIQIDGVSWNSVT----LQTWRKAFG 1295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFdqfsvgqnlllalpstlKGTARRN----------AVKDALDRAGLAETYHQDPA-----------TLSGGQ 138
Cdd:TIGR01271 1296 VIPQKVFIF-----------------SGTFRKNldpyeqwsdeEIWKVAEEVGLKSVIEQFPDkldfvlvdggyVLSNGH 1358
|
170 180
....*....|....*....|....*..
gi 300840748 139 RARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:TIGR01271 1359 KQLMCLARSILSKAKILLLDEPSAHLD 1385
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-197 |
2.67e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 50.39 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTlfswMIGALAGQFSC-TGEL-WLNEQRIDMLPTAQRQ- 77
Cdd:PRK10762 4 LLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKST----MMKVLTGIYTRdAGSIlYLGKEVTFNGPKSSQEa 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 -IGILFQDALLFDQFSVGQNLLLAL-PSTLKGT---ARRNAVKDA-LDRAGLAETYHQDPATLSGGQRARVALLRALLAQ 151
Cdd:PRK10762 80 gIGIIHQELNLIPQLTIAENIFLGReFVNRFGRidwKKMYAEADKlLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFE 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 300840748 152 PKALLLDEPFSrldvALRDNFRQWVFSEVREL---AIPVVQVTHDLQDV 197
Cdd:PRK10762 160 SKVIIMDEPTD----ALTDTETESLFRVIRELksqGRGIVYISHRLKEI 204
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
4-166 |
4.78e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwMIgalagqfscTGELWLNEQRIDMLPTAqrQIGILFQ 83
Cdd:PRK11819 327 AENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFK-MI---------TGQEQPDSGTIKIGETV--KLAYVDQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 84 --DAL-----LFDQFSVGQNLLL----ALPS-------TLKGTarrnavkDALDRAGlaetyhqdpaTLSGGQRARVALL 145
Cdd:PRK11819 395 srDALdpnktVWEEISGGLDIIKvgnrEIPSrayvgrfNFKGG-------DQQKKVG----------VLSGGERNRLHLA 457
|
170 180
....*....|....*....|.
gi 300840748 146 RALLAQPKALLLDEPFSRLDV 166
Cdd:PRK11819 458 KTLKQGGNVLLLDEPTNDLDV 478
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
20-165 |
4.86e-07 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 48.69 E-value: 4.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 20 VNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSCTGELWLNEQRidmlptaQRQIGILFQDALLFDQFSVGQN 96
Cdd:PRK13543 30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhveSGQIQIDGKTATRGDR-------SRFMAYLGHLPGLKADLSTLEN 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300840748 97 LLLAlpSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:PRK13543 103 LHFL--CGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
4-165 |
7.23e-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: 48.70 E-value: 7.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPE--SRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAGQFSCTGELWLNEQRIDMLPTAQ--RQIG 79
Cdd:cd03289 5 VKDLTAKYTEggNAVLENISFSISPGQRVGLLGRTGSGKSTLLS----AFLRLLNTEGDIQIDGVSWNSVPLQKwrKAFG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 80 ILFQDALLFDQfSVGQNLllalpsTLKGTARRNAVKDALDRAGLAETYHQDPA-----------TLSGGQRARVALLRAL 148
Cdd:cd03289 81 VIPQKVFIFSG-TFRKNL------DPYGKWSDEEIWKVAEEVGLKSVIEQFPGqldfvlvdggcVLSHGHKQLMCLARSV 153
|
170
....*....|....*..
gi 300840748 149 LAQPKALLLDEPFSRLD 165
Cdd:cd03289 154 LSKAKILLLDEPSAHLD 170
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
4-165 |
7.28e-07 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 48.95 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRL-LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLP-TAQRQ-IGI 80
Cdd:PRK10790 343 IDNVSFAYRDDNLvLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT---EGEIRLDGRPLSSLShSVLRQgVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQD-ALLFDQFSVgqNLllalpsTLKGTARRNAVKDALDRAGLAETYHQDPA-----------TLSGGQRARVALLRAL 148
Cdd:PRK10790 420 VQQDpVVLADTFLA--NV------TLGRDISEEQVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVL 491
|
170
....*....|....*..
gi 300840748 149 LAQPKALLLDEPFSRLD 165
Cdd:PRK10790 492 VQTPQILILDEATANID 508
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
5-199 |
7.65e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 7.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIG----------ALAGQFSCTGE-LWLNEQRIDMLPT 73
Cdd:PRK10938 264 NNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgysndlTLFGRRRGSGEtIWDIKKHIGYVSS 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 74 A---QRQIGILFQDALL---FDQFSVGQnlllALPStlkgtARRNAVKDALDRAGLAETYHQDP-ATLSGGQRARVALLR 146
Cdd:PRK10938 344 SlhlDYRVSTSVRNVILsgfFDSIGIYQ----AVSD-----RQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALIVR 414
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 300840748 147 ALLAQPKALLLDEPFSRLDVALRDNFRQWVFSEVRELAIPVVQVTHDLQDVPA 199
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDAPA 467
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
16-166 |
7.70e-07 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.01 E-value: 7.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWM---IGALAGQFSCTGE---LWLNEQR-------IDMLPTAQRQIGILF 82
Cdd:PRK10636 16 LLDNATATINPGQKVGLVGKNGCGKSTLLALLkneISADGGSYTFPGNwqlAWVNQETpalpqpaLEYVIDGDREYRQLE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 QDALLFDQFSVGQ--NLLLALPSTLKGTARRNAVKDALDRAGLAETYHQDP-ATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:PRK10636 96 AQLHDANERNDGHaiATIHGKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLLDE 175
|
....*..
gi 300840748 160 PFSRLDV 166
Cdd:PRK10636 176 PTNHLDL 182
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-160 |
7.76e-07 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 49.02 E-value: 7.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLfswMiGALAGQF---SCTGELWLNEQRI---DMLPTAQRQI 78
Cdd:NF040905 5 RGITKTFPGVKALDDVNLSVREGEIHALCGENGAGKSTL---M-KVLSGVYphgSYEGEILFDGEVCrfkDIRDSEALGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLFDQFSVGQNLLLALPSTLKGTARRNAV----KDALDRAGLAEtyhqDPATLSG----GQRARVALLRALLA 150
Cdd:NF040905 81 VIIHQELALIPYLSIAENIFLGNERAKRGVIDWNETnrraRELLAKVGLDE----SPDTLVTdigvGKQQLVEIAKALSK 156
|
170
....*....|
gi 300840748 151 QPKALLLDEP 160
Cdd:NF040905 157 DVKLLILDEP 166
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
20-159 |
8.39e-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: 48.64 E-value: 8.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 20 VNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQFSCT-GELWLNEQRIDM--LPTAQRQIGILFQDALLFDQfsvgqn 96
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTL----AKLLTGLYRPEsGEILLDGQPVTAdnREAYRQLFSAVFSDFHLFDR------ 420
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300840748 97 lLLALPstlkGTARRNAVKDALDRAGLAE-TYHQDPA----TLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:COG4615 421 -LLGLD----GEADPARARELLERLELDHkVSVEDGRfsttDLSQGQRKRLALLVALLEDRPILVFDE 483
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
6-192 |
8.49e-07 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 48.98 E-value: 8.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 6 NVSLRLPESRLLTN-VNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGQFSCT------GELWLNEQRIDM-LPTAQRQ 77
Cdd:TIGR00954 456 NIPLVTPNGDVLIEsLSFEVPSGNNLLICGPNGCGKSSLFR-ILGELWPVYGGRltkpakGKLFYVPQRPYMtLGTLRDQ 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 igILFQDAlLFDQFSVG---QNL-----LLALPSTLKGTARRNAVKDALDraglaetyhqdpaTLSGGQRARVALLRALL 149
Cdd:TIGR00954 535 --IIYPDS-SEDMKRRGlsdKDLeqildNVQLTHILEREGGWSAVQDWMD-------------VLSGGEKQRIAMARLFY 598
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 300840748 150 AQPKALLLDEPFSRLDVALRDnfrqWVFSEVRELAIPVVQVTH 192
Cdd:TIGR00954 599 HKPQFAILDECTSAVSVDVEG----YMYRLCREFGITLFSVSH 637
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
121-166 |
9.20e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 48.70 E-value: 9.20e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 300840748 121 AGL---AETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PLN03073 329 AGLsftPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDL 377
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
26-196 |
9.46e-07 |
|
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: 46.98 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 26 KGDIVTLMGPSGCGKSTLfswmIGALAGQFSCTGElwlneqridmlptaqrqiGILFQDAllfdqfsvgqnlllalpstl 105
Cdd:smart00382 1 PGEVILIVGPPGSGKTTL----ARALARELGPPGG------------------GVIYIDG-------------------- 38
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 106 kgtarrNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVA-----LRDNFRQWVFSEV 180
Cdd:smart00382 39 ------EDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEqeallLLLEELRLLLLLK 112
|
170
....*....|....*.
gi 300840748 181 RELAIPVVQVTHDLQD 196
Cdd:smart00382 113 SEKNLTVILTTNDEKD 128
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-165 |
1.14e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 48.49 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 19 NVNFTVDKGDIVTLMGPSGCGKSTLFSwMIGALAGqfSCTGELWLNEQR--IDM-LPTAQRQIGILFQDALLFDQfSVGQ 95
Cdd:PTZ00265 403 DLNFTLTEGKTYAFVGESGCGKSTILK-LIERLYD--PTEGDIIINDSHnlKDInLKWWRSKIGVVSQDPLLFSN-SIKN 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 96 NLLLALPS-----------------TLKGTARRNAVK-----------DALDRAGLAETYHQ------------------ 129
Cdd:PTZ00265 479 NIKYSLYSlkdlealsnyynedgndSQENKNKRNSCRakcagdlndmsNTTDSNELIEMRKNyqtikdsevvdvskkvli 558
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 300840748 130 -----------------DPATLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:PTZ00265 559 hdfvsalpdkyetlvgsNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
12-166 |
1.37e-06 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 48.25 E-value: 1.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 12 PESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFsCTGELWLNEQRIDmLPTAQRQI--GILF------Q 83
Cdd:NF040905 271 PERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGRSYGRN-ISGTVFKDGKEVD-VSTVSDAIdaGLAYvtedrkG 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 84 DALLFDQfSVGQNLLLAlpsTLKGTARRNAVKDALDRAgLAETYH-----------QDPATLSGGQRARVALLRALLAQP 152
Cdd:NF040905 349 YGLNLID-DIKRNITLA---NLGKVSRRGVIDENEEIK-VAEEYRkkmniktpsvfQKVGNLSGGNQQKVVLSKWLFTDP 423
|
170
....*....|....
gi 300840748 153 KALLLDEPFSRLDV 166
Cdd:NF040905 424 DVLILDEPTRGIDV 437
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
4-205 |
1.42e-06 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 47.81 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCG--KSTLFSWMIGALAGQFSCTGELWLNEQRidmlpTAQRQIGIL 81
Cdd:NF000106 16 VRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGRRPWRF*TWCANRR-----ALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDAL-LFDQFSVGQNL-LLALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:NF000106 91 RPVR*gRRESFSGRENLyMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 300840748 160 PFSRLDVALRDNFRQWVFSEVRELA--IPVVQVTHDLQDVPADSSVLD 205
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGAtvLLTTQYMEEAEQLAHELTVID 218
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
5-174 |
1.42e-06 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESR--LLTNVNFTVDKGDIVTLMGPSGCGKSTLfswMIGALAGQFSCTGELwlneqRIDMLPTA-------Q 75
Cdd:TIGR00957 1288 RNYCLRYREDLdlVLRHINVTIHGGEKVGIVGRTGAGKSSL---TLGLFRINESAEGEI-----IIDGLNIAkiglhdlR 1359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 76 RQIGILFQDALLF--------DQFS--VGQNLLLALP-STLKGTArrNAVKDALDraglaetyHQ---DPATLSGGQRAR 141
Cdd:TIGR00957 1360 FKITIIPQDPVLFsgslrmnlDPFSqySDEEVWWALElAHLKTFV--SALPDKLD--------HEcaeGGENLSVGQRQL 1429
|
170 180 190
....*....|....*....|....*....|...
gi 300840748 142 VALLRALLAQPKALLLDEPFSRLDVAlRDNFRQ 174
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLE-TDNLIQ 1461
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
16-197 |
4.97e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIGAlagqfsCTGELWLNEQRIDM--LPTAQRQIGILFQDALLFDQ 90
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLlltFMRMVEV------CGGEIRVNGREIGAygLRELRRQFSMIPQDPVLFDG 1398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 91 fSVGQNL---LLALPStlkgtarrnAVKDALDRAGL-----AETYHQDPATLSG------GQRARVALLRALLAQPKA-L 155
Cdd:PTZ00243 1399 -TVRQNVdpfLEASSA---------EVWAALELVGLrervaSESEGIDSRVLEGgsnysvGQRQLMCMARALLKKGSGfI 1468
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 300840748 156 LLDEPFSRLDVALRDNFRQWVFSEVRelAIPVVQVTHDLQDV 197
Cdd:PTZ00243 1469 LMDEATANIDPALDRQIQATVMSAFS--AYTVITIAHRLHTV 1508
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
112-166 |
5.05e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.48 E-value: 5.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 300840748 112 NAVKDALDRAGLaetyhqDPAT----LSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PRK11147 137 NRINEVLAQLGL------DPDAalssLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
23-169 |
9.26e-06 |
|
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: 45.09 E-value: 9.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 23 TVDKGDIVTLMGPSGCGKSTlfswMIGALAGQFSCT-GELWLNEQRIDMLPtaqRQIGILFQ---DALLFDQfsvgqnll 98
Cdd:cd03237 21 SISESEVIGILGPNGIGKTT----FIKMLAGVLKPDeGDIEIELDTVSYKP---QYIKADYEgtvRDLLSSI-------- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 300840748 99 laLPSTLKGTARRNAVKDALdraGLAETYHQDPATLSGGQRARVALLrALLAQPKAL-LLDEPFSRLDVALR 169
Cdd:cd03237 86 --TKDFYTHPYFKTEIAKPL---QIEQILDREVPELSGGELQRVAIA-ACLSKDADIyLLDEPSAYLDVEQR 151
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
20-216 |
1.22e-05 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 45.18 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 20 VNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLNEQrIDMLPTAQRQ--------IGILFQD--ALLFD 89
Cdd:PRK15093 26 VSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDD-IDLLRLSPRErrklvghnVSMIFQEpqSCLDP 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 90 QFSVGQNLLLALPS-TLKGT-------ARRNAVkDALDRAGLAEtyHQD-----PATLSGGQRARVALLRALLAQPKALL 156
Cdd:PRK15093 105 SERVGRQLMQNIPGwTYKGRwwqrfgwRKRRAI-ELLHRVGIKD--HKDamrsfPYELTEGECQKVMIAIALANQPRLLI 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300840748 157 LDEPFSrldvALRDNFRQWVFSEVREL----AIPVVQVTHDLQdvpadssvlDMAQWSENYNKL 216
Cdd:PRK15093 182 ADEPTN----AMEPTTQAQIFRLLTRLnqnnNTTILLISHDLQ---------MLSQWADKINVL 232
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
5-164 |
1.46e-05 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTAQ---RQIGIL 81
Cdd:PRK10982 2 SNISKSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKD---SGSILFQGKEIDFKSSKEaleNGISMV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 82 FQDALLFDQFSVGQNLLLA-LPstLKG-----TARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKAL 155
Cdd:PRK10982 79 HQELNLVLQRSVMDNMWLGrYP--TKGmfvdqDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
|
....*....
gi 300840748 156 LLDEPFSRL 164
Cdd:PRK10982 157 IMDEPTSSL 165
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
1-176 |
1.73e-05 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 44.40 E-value: 1.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSwmigALAG--QFSCT-GELWLNEQRIDMLPTAQRq 77
Cdd:PRK09580 1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSA----TLAGreDYEVTgGTVEFKGKDLLELSPEDR- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 igilfqdallfdqfsVGQNLLLAL--PSTLKGTARR-------NAVK-----DALDRAGLAETYHQD------PATL--- 134
Cdd:PRK09580 76 ---------------AGEGIFMAFqyPVEIPGVSNQfflqtalNAVRsyrgqEPLDRFDFQDLMEEKiallkmPEDLltr 140
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 300840748 135 ------SGGQRARVALLRALLAQPKALLLDEPFSRLDV-----------ALRDNFRQWV 176
Cdd:PRK09580 141 svnvgfSGGEKKRNDILQMAVLEPELCILDESDSGLDIdalkivadgvnSLRDGKRSFI 199
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
17-165 |
2.02e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 44.73 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAgqfsctgelwlneQRIDMLPTAQRQIGILFQDALLFDQfSVGQN 96
Cdd:PLN03130 633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELP-------------PRSDASVVIRGTVAYVPQVSWIFNA-TVRDN 698
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 97 LLLALPSTlkgTARRNAvkdALDRAGLAETYHQDPA-----------TLSGGQRARVALLRALLAQPKALLLDEPFSRLD 165
Cdd:PLN03130 699 ILFGSPFD---PERYER---AIDVTALQHDLDLLPGgdlteigergvNISGGQKQRVSMARAVYSNSDVYIFDDPLSALD 772
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
17-162 |
2.22e-05 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 44.50 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGqfsctgelwlNEQRIDMLPTAQrQIGIlfqDALLFDQFSVGQN 96
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMP----------NKGTVDIKGSAA-LIAI---SSGLNGQLTGIEN 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300840748 97 L-LLALPSTLKGTARRNAVKDALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFS 162
Cdd:PRK13545 106 IeLKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS 172
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-173 |
3.11e-05 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 44.20 E-value: 3.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 16 LLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDM--LPTAQRQIGILFQDALLF----- 88
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELE---KGRIMIDDCDVAKfgLTDLRRVLSIIPQSPVLFsgtvr 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 89 ---DQFSVGQNlllalpSTLKGTARRNAVKDALDRA--GLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSR 163
Cdd:PLN03232 1328 fniDPFSEHND------ADLWEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATAS 1401
|
170
....*....|....*...
gi 300840748 164 LDV--------ALRDNFR 173
Cdd:PLN03232 1402 VDVrtdsliqrTIREEFK 1419
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
30-193 |
5.94e-05 |
|
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: 42.21 E-value: 5.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 30 VTLM-GPSGCGKSTLFswmigaLAGQFSCTGELWLNEQRIDMLPTAQR------QIGILFQDAllfdqfsVGQNLllalp 102
Cdd:cd03240 24 LTLIvGQNGAGKTTII------EALKYALTGELPPNSKGGAHDPKLIRegevraQVKLAFENA-------NGKKY----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 103 stlkgTARRNAvkDALDRAglaeTY-HQD---------PATLSGGQRA------RVALLRALLAQPKALLLDEPFSRLDv 166
Cdd:cd03240 86 -----TITRSL--AILENV----IFcHQGesnwplldmRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLD- 153
|
170 180 190
....*....|....*....|....*....|.
gi 300840748 167 alRDNFRQW---VFSEVRELAIP-VVQVTHD 193
Cdd:cd03240 154 --EENIEESlaeIIEERKSQKNFqLIVITHD 182
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
1-166 |
6.37e-05 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 42.96 E-value: 6.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGAL---AGQFSctgeLWLNEQridmlptaqrq 77
Cdd:PRK15064 1 MLSTANITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLepsAGNVS----LDPNER----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 78 IGILFQDALLFDQFSVgqnlllaLPSTLKGTARRNAVKDALDR------------------------------------- 120
Cdd:PRK15064 66 LGKLRQDQFAFEEFTV-------LDTVIMGHTELWEVKQERDRiyalpemseedgmkvadlevkfaemdgytaearagel 138
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 300840748 121 ---AGLAETYHQDP-ATLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PRK15064 139 llgVGIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDI 188
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
17-43 |
7.17e-05 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 42.38 E-value: 7.17e-05
10 20
....*....|....*....|....*..
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTL 43
Cdd:COG1134 42 LKDVSFEVERGESVGIIGRNGAGKSTL 68
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
17-209 |
7.99e-05 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 41.92 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLfswmigALAGqFSCTGELWLneqrIDMLPTAQRQIgILFQDALlfdqfsvgQN 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTL------VNEG-LYASGKARL----ISFLPKFSRNK-LIFIDQL--------QF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 97 LLlalpstlkgtarrnavkdaldRAGLAE-TYHQDPATLSGGQRARVALLRALLAQPKALL--LDEPFSRLDVALRDNFR 173
Cdd:cd03238 71 LI---------------------DVGLGYlTLGQKLSTLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQDINQLL 129
|
170 180 190
....*....|....*....|....*....|....*.
gi 300840748 174 QwVFSEVRELAIPVVQVTHDLqdvpadsSVLDMAQW 209
Cdd:cd03238 130 E-VIKGLIDLGNTVILIEHNL-------DVLSSADW 157
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-169 |
8.17e-05 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 42.85 E-value: 8.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 1 MLCVKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLnEQRIDMLPTAQRQIGI 80
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPV---SGEIGL-AKGIKLGYFAQHQLEF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 81 LFQDAllfdqfSVGQNLLLALPSTLKGTARrnavkDALDRAGLAETYHQDP-ATLSGGQRARVALLRALLAQPKALLLDE 159
Cdd:PRK10636 388 LRADE------SPLQHLARLAPQELEQKLR-----DYLGGFGFQGDKVTEEtRRFSGGEKARLVLALIVWQRPNLLLLDE 456
|
170
....*....|
gi 300840748 160 PFSRLDVALR 169
Cdd:PRK10636 457 PTNHLDLDMR 466
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
5-166 |
1.06e-04 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 42.80 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 5 KNVSLR----LPEsrLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELWLNEQRIDMLPTA--QRQI 78
Cdd:PLN03130 1241 EDVVLRyrpeLPP--VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELE---RGRILIDGCDISKFGLMdlRKVL 1315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 79 GILFQDALLF--------DQFSVGQN--LLLALP-STLKGTARRNAVkdaldraGLAETYHQDPATLSGGQRARVALLRA 147
Cdd:PLN03130 1316 GIIPQAPVLFsgtvrfnlDPFNEHNDadLWESLErAHLKDVIRRNSL-------GLDAEVSEAGENFSVGQRQLLSLARA 1388
|
170
....*....|....*....
gi 300840748 148 LLAQPKALLLDEPFSRLDV 166
Cdd:PLN03130 1389 LLRRSKILVLDEATAAVDV 1407
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
18-194 |
1.73e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.15 E-value: 1.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 18 TNVNFTvdkGDIVTLMGPSGCGKSTLFSWMIGALAGQFSCTGELWLN----------------------------EQRID 69
Cdd:COG0419 17 ETIDFD---DGLNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDlinvgseeasvelefehggkryrierrqGEFAE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 70 MLPTAQRQIGILFQDALLFDQFSVGQNLLLALPSTLKGTARRNAVKDALDRAGLAE-TYHQDPATLSGGQRARVALLRAL 148
Cdd:COG0419 94 FLEAKPSERKEALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILAQlSGLDPIETLSGGERLRLALADLL 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 300840748 149 laqpkALLLDepFSRLDVALRDNfrqwVFSEVRELAIpvvqVTHDL 194
Cdd:COG0419 174 -----SLILD--FGSLDEERLER----LLDALEELAI----ITHVI 204
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
24-199 |
1.74e-04 |
|
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: 41.92 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 24 VDKGDIVTLMGPSGCGKSTLFSWMIG---ALAGQFSCTGELWLNEqridmLPTAQRQIGILFQ-DALlfDQFSVGQNLLL 99
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGdttVTSGDATVAGKSILTN-----ISDVHQNMGYCPQfDAI--DDLLTGREHLY 2034
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 100 aLPSTLKGTARRNAVKDA---LDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWV 176
Cdd:TIGR01257 2035 -LYARLRGVPAEEIEKVAnwsIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTI 2113
|
170 180
....*....|....*....|...
gi 300840748 177 FSEVRElAIPVVQVTHDLQDVPA 199
Cdd:TIGR01257 2114 VSIIRE-GRAVVLTSHSMEECEA 2135
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
11-165 |
1.99e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 41.76 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 11 LPESRL--LTNVNFTVDKGDIVTLMGPSGCGKSTLfswmIGALAGQfsCTGELWLNEQRIDMLPTAQ----RQIGILFQD 84
Cdd:PLN03140 888 VTEDRLqlLREVTGAFRPGVLTALMGVSGAGKTTL----MDVLAGR--KTGGYIEGDIRISGFPKKQetfaRISGYCEQN 961
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 85 ALLFDQFSVGQNLL----LALPSTLKGTARRNAV------------KDALdrAGLAETyhqdpATLSGGQRARVALLRAL 148
Cdd:PLN03140 962 DIHSPQVTVRESLIysafLRLPKEVSKEEKMMFVdevmelveldnlKDAI--VGLPGV-----TGLSTEQRKRLTIAVEL 1034
|
170
....*....|....*..
gi 300840748 149 LAQPKALLLDEPFSRLD 165
Cdd:PLN03140 1035 VANPSIIFMDEPTSGLD 1051
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-194 |
4.45e-04 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 39.48 E-value: 4.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 24 VDKGDIVTLMGPSGCGKSTlfswMIGALAGQFSCTGElwlneqridmlptaqrqigilfqdallfdqfsvgqnlllalps 103
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTT----AVKILAGQLIPNGD------------------------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 104 tlkgtarrnavKDALDRAGLAetYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNFRQWV--FSEVR 181
Cdd:cd03222 55 -----------NDEWDGITPV--YKPQYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIrrLSEEG 121
|
170
....*....|...
gi 300840748 182 ELAIPVVQvtHDL 194
Cdd:cd03222 122 KKTALVVE--HDL 132
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
4-160 |
4.54e-04 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 40.49 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 4 VKNVSLRLPESRLLTNVNFTVDKGDIVTLMGPSGCGKSTLFSWMIGALAGQfscTGELW-LNEqriDMLPTAQRqigilf 82
Cdd:NF033858 4 LEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQ---QGRVEvLGG---DMADARHR------ 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 83 qDAL--------------LFDQFSVGQNL-----LLALpstlkGTARRNAVKDALDRA-GLAEtYHQDPA-TLSGGQRAR 141
Cdd:NF033858 72 -RAVcpriaympqglgknLYPTLSVFENLdffgrLFGQ-----DAAERRRRIDELLRAtGLAP-FADRPAgKLSGGMKQK 144
|
170
....*....|....*....
gi 300840748 142 VALLRALLAQPKALLLDEP 160
Cdd:NF033858 145 LGLCCALIHDPDLLILDEP 163
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
2-167 |
2.45e-03 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 37.97 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 2 LCVKNVSLRLPesrLLTNVNFTVDKGDIVTLMGPSGCGKSTL---FSWMIGALAGQFSCTGelwlneqrIDM----LPTA 74
Cdd:cd03288 25 LCVRYENNLKP---VLKHVKAYIKPGQKVGICGRTGSGKSSLslaFFRMVDIFDGKIVIDG--------IDIsklpLHTL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 75 QRQIGILFQDALLFDQfSVGQNLLLALPST-------LKGTARRNAVKdALDrAGLAETYHQDPATLSGGQRARVALLRA 147
Cdd:cd03288 94 RSRLSIILQDPILFSG-SIRFNLDPECKCTddrlweaLEIAQLKNMVK-SLP-GGLDAVVTEGGENFSVGQRQLFCLARA 170
|
170 180
....*....|....*....|
gi 300840748 148 LLAQPKALLLDEPFSRLDVA 167
Cdd:cd03288 171 FVRKSSILIMDEATASIDMA 190
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
133-166 |
2.51e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.17 E-value: 2.51e-03
10 20 30
....*....|....*....|....*....|....
gi 300840748 133 TLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:PRK10982 391 SLSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDV 424
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
23-166 |
9.48e-03 |
|
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: 36.69 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 23 TVDKGDIVTLMGPSGCGKSTlfswMIGALAGQFSCTGELWLNEQRIDMLPtaQRqIGILFQDallfdqfSVGQNLLLALP 102
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTT----FAKILAGVLKPDEGEVDEDLKISYKP--QY-ISPDYDG-------TVEEFLRSANT 427
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300840748 103 STLKGTARRNAVkdaLDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDV 166
Cdd:COG1245 428 DDFGSSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDV 488
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
17-197 |
9.65e-03 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 36.33 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 17 LTNVNFTVDKGDIVTLMGPSGCGKSTLfSWMIGalaGQFSCT-GELwlneqridmlpTAQRQIGILFQDALLFDQFSVGQ 95
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTL-SNIIG---GSLSPTvGKV-----------DRNGEVSVIAISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300840748 96 NLLLALpsTLKGTARRNAVK---DALDRAGLAETYHQDPATLSGGQRARVALLRALLAQPKALLLDEPFSRLDVALRDNF 172
Cdd:PRK13546 105 NIEFKM--LCMGFKRKEIKAmtpKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180
....*....|....*....|....*
gi 300840748 173 RQWVFsEVRELAIPVVQVTHDLQDV 197
Cdd:PRK13546 183 LDKIY-EFKEQNKTIFFVSHNLGQV 206
|
|
| |
