|
Name |
Accession |
Description |
Interval |
E-value |
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-254 |
5.55e-139 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 390.99 E-value: 5.55e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ 84
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 FIGRVFQDPKMGTAPRMTVAENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFL 164
Cdd:COG1101 81 YIGRVFQDPMMGTAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 165 MATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADINEQEKQNLK 244
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEEKKKLT 240
|
250
....*....|
gi 489745462 245 VSDLYKYFED 254
Cdd:COG1101 241 VEDLLELFEE 250
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
3-235 |
5.85e-57 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 181.39 E-value: 5.85e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKR 82
Cdd:COG1136 2 SPLLELRNLTKSYGTGEGE-VTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 TQF----IGRVFQDPKMgtAPRMTVAEN----LLLATKRGKRRFLKIRKLkqnlprfkkLAAVmnnGLENRLNTFVEGLS 154
Cdd:COG1136 81 ARLrrrhIGFVFQFFNL--LPELTALENvalpLLLAGVSRKERRERAREL---------LERV---GLGDRLDHRPSQLS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 155 GGQRQ------ALsflmatIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHmEDALKYGNRLLVLKD 228
Cdd:COG1136 147 GGQQQrvaiarAL------VNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHD-PELAARADRVIRLRD 219
|
....*..
gi 489745462 229 GKVKADI 235
Cdd:COG1136 220 GRIVSDE 226
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
6-231 |
1.39e-52 |
|
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: 169.98 E-value: 1.39e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTaDGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:cd03255 1 IELKNLSKTYGG-GGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 ----IGRVFQDPKMgtAPRMTVAEN----LLLATKRGKRRFLKIRKLkqnlprFKKLaavmnnGLENRLNTFVEGLSGGQ 157
Cdd:cd03255 80 rrrhIGFVFQSFNL--LPDLTALENvelpLLLAGVPKKERRERAEEL------LERV------GLGDRLNHYPSELSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489745462 158 RQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDAlKYGNRLLVLKDGKV 231
Cdd:cd03255 146 QQRVAIARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
6-231 |
4.22e-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: 168.47 E-value: 4.22e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKttvKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqf 85
Cdd:cd03259 1 LELKGLS---KTYGS--VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRKlkqnlpRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLM 165
Cdd:cd03259 74 IGMVFQDYAL--FPHLTVAENIAFGLKLRGVPKAEIRA------RVRELLELV--GLEGLLNRYPHELSGGQQQRVALAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 166 ATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03259 144 ALAREPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRI 209
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
4-231 |
5.32e-48 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 159.07 E-value: 5.32e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVkttVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT 83
Cdd:COG3638 1 PMLELRNL---SKRYPGG-TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 QF---IGRVFQDPkmGTAPRMTVAENLLLATkRGKRRFLkiRKLkqnLPRFKK---------LAAVmnnGLENRLNTFVE 151
Cdd:COG3638 77 RLrrrIGMIFQQF--NLVPRLSVLTNVLAGR-LGRTSTW--RSL---LGLFPPedreraleaLERV---GLADKAYQRAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 152 GLSGGQRQ------ALsflmatIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLV 225
Cdd:COG3638 146 QLSGGQQQrvaiarAL------VQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIG 219
|
....*.
gi 489745462 226 LKDGKV 231
Cdd:COG3638 220 LRDGRV 225
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-231 |
1.48e-46 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 158.34 E-value: 1.48e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:COG3842 1 MAMPALELENV---SKRYGD--VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRtqFIGRVFQDPkmgtA--PRMTVAENLllatkrgkrRF-LKIRKLKQN--LPRFKKLAAVMnnGLENRLNTFVEGLSG 155
Cdd:COG3842 76 KR--NVGMVFQDY----AlfPHLTVAENV---------AFgLRMRGVPKAeiRARVAELLELV--GLEGLADRYPHQLSG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 156 GQRQ--ALSFLMATieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:COG3842 139 GQQQrvALARALAP--EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRI 214
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
5-231 |
1.76e-46 |
|
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: 154.59 E-value: 1.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ 84
Cdd:cd03257 1 LLEVKNLSVSFPTGGGS-VKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 F---IGRVFQDPkmGTA--PRMTV----AENLLLATKRGKRRFLKIRKLkqnlprfkkLAAVMNNGLENRLNTFVEGLSG 155
Cdd:cd03257 80 RrkeIQMVFQDP--MSSlnPRMTIgeqiAEPLRIHGKLSKKEARKEAVL---------LLLVGVGLPEEVLNRYPHELSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 156 GQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03257 149 GQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
7-230 |
3.55e-45 |
|
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: 150.70 E-value: 3.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 7 ELKDVKTTVKTADgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFI 86
Cdd:cd03225 1 ELKNLSFSYPDGA---RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 87 GRVFQDPK---MGTAPRMTVA---ENLLLATKRGKRRflkIRKLkqnlprfkkLAAVmnnGLENRLNTFVEGLSGGQRQA 160
Cdd:cd03225 78 GLVFQNPDdqfFGPTVEEEVAfglENLGLPEEEIEER---VEEA---------LELV---GLEGLRDRSPFTLSGGQKQR 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 161 LSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDqQIKENKLTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:cd03225 143 VAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLK-KLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
6-234 |
6.35e-45 |
|
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: 150.56 E-value: 6.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:COG1122 1 IELENL--SFSYPGG--TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPK----MgtaprMTVAE-------NLLLATKRGKRRFLKIrklkqnlprfkkLAAVmnnGLENRLNTFVEGLS 154
Cdd:COG1122 77 VGLVFQNPDdqlfA-----PTVEEdvafgpeNLGLPREEIRERVEEA------------LELV---GLEHLADRPPHELS 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 155 GGQRQ--ALSFLMATieRPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVK 232
Cdd:COG1122 137 GGQKQrvAIAGVLAM--EPEVLVLDEPTAGLDPRGRRELLELL-KRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIV 213
|
..
gi 489745462 233 AD 234
Cdd:COG1122 214 AD 215
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
23-234 |
1.40e-44 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 149.83 E-value: 1.40e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQfIGRVFQDPkmGTAPRMT 102
Cdd:COG1131 13 KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR-IGYVPQEP--ALYPDLT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLAtkrgkRRFLKIRKlKQNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAA 182
Cdd:COG1131 90 VRENLRFF-----ARLYGLPR-KEARERIDELLELF--GLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTSG 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489745462 183 LDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:COG1131 162 LDPEARRELWELL-RELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-234 |
1.63e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 156.60 E-value: 1.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTkPILELKDVktTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPD---SGFLLHNGHDITKM 77
Cdd:COG1123 1 MT-PLLEVRDL--SVRYPGGD-VPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLEL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 78 SEEKRTQFIGRVFQDPKMGTAPrMTVAENLLLATKRGKRRFLKIRKLKQNLprfkkLAAVmnnGLENRLNTFVEGLSGGQ 157
Cdd:COG1123 77 SEALRGRRIGMVFQDPMTQLNP-VTVGDQIAEALENLGLSRAEARARVLEL-----LEAV---GLERRLDRYPHQLSGGQ 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 158 RQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:COG1123 148 RQRVAIAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED 224
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
6-231 |
3.38e-44 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 148.04 E-value: 3.38e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVktadgEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EEKRTQ 84
Cdd:COG4619 1 LELEGLSFRV-----GGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPpPEWRRQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 fIGRVFQDPKMGtapRMTVAENLLLAtkrgkrrfLKIRKLKQNLPRFKKLAAVMnnGLENR-LNTFVEGLSGGQRQALSF 163
Cdd:COG4619 76 -VAYVPQEPALW---GGTVRDNLPFP--------FQLRERKFDRERALELLERL--GLPPDiLDKPVERLSGGERQRLAL 141
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 164 LMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:COG4619 142 IRALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
26-234 |
7.87e-44 |
|
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: 147.97 E-value: 7.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF-IGRVFQDPKmgTAPRMTVA 104
Cdd:cd03219 16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLgIGRTFQIPR--LFPELTVL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 105 ENLLLATKRGKRRFLKIRKLKQNLPRFKK-----LAAVmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEH 179
Cdd:cd03219 94 ENVMVAAQARTGSGLLLARARREEREAREraeelLERV---GLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEP 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 180 TAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03219 171 AAGLNPEETEELAELI-RELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAE 224
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
6-234 |
1.69e-43 |
|
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: 146.81 E-value: 1.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTtvktADGEIvPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:cd03224 1 LEVENLNA----GYGKS-QILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 -IGRVFQDpkMGTAPRMTVAENLLLATKRGKRRFLKiRKLKQNLPRFKKLAAvmnnglenRLNTFVEGLSGGQRQALSFL 164
Cdd:cd03224 76 gIGYVPEG--RRIFPELTVEENLLLGAYARRRAKRK-ARLERVYELFPRLKE--------RRKQLAGTLSGGEQQMLAIA 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 165 MATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03224 145 RALMSRPKLLLLDEPSEGLAPKIVEEIFEAI-RELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLE 213
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
24-234 |
2.60e-43 |
|
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: 147.11 E-value: 2.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPkmGTAPRMTV 103
Cdd:COG1120 15 PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEP--PAPFGLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLatkrGKRRFLKIrklkqnLPRFKK---------LAAVmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDIL 174
Cdd:COG1120 93 RELVAL----GRYPHLGL------FGRPSAedreaveeaLERT---GLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 175 LLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:COG1120 160 LLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ 219
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-231 |
2.61e-43 |
|
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: 153.14 E-value: 2.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRR 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQF---IGRVFQDPkmgTA---PRMTVAENL-----LLATKRGKRRFLKIRKLkqnlprfkkLAAVmnnGL-ENRLNT 148
Cdd:COG1123 336 SLRELrrrVQMVFQDP---YSslnPRMTVGDIIaeplrLHGLLSRAERRERVAEL---------LERV---GLpPDLADR 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 149 FVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSE---NLLAvtDQQiKENKLTALMITHHMEDALKYGNRLLV 225
Cdd:COG1123 401 YPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAqilNLLR--DLQ-RELGLTYLFISHDLAVVRYIADRVAV 477
|
....*.
gi 489745462 226 LKDGKV 231
Cdd:COG1123 478 MYDGRI 483
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
26-231 |
8.40e-43 |
|
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: 145.17 E-value: 8.40e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfIGRVFQDPKMgtAPRMTVAE 105
Cdd:cd03299 15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYAL--FPHMTVYK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 NLLLATKRGKRRFLKIRKlkqnlpRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDP 185
Cdd:cd03299 91 NIAYGLKKRKVDKKEIER------KVLEIAEML--GIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDV 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 489745462 186 HTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKL 208
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-234 |
1.00e-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: 145.12 E-value: 1.00e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVktadGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:COG1127 1 MSEPMIEVRNLTKSF----GD-RVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQF---IGRVFQDPKMGTAprMTVAENLLLATkrgkRRFLKI-RKLKQNLPRFkKLAAVmnnGLENRLNTFVEGLSGG 156
Cdd:COG1127 76 ELYELrrrIGMLFQGGALFDS--LTVFENVAFPL----REHTDLsEAEIRELVLE-KLELV---GLPGAADKMPSELSGG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 157 QRQ--ALSFLMATieRPDILLLDEHTAALDPHTSenllAVTDQQI----KENKLTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:COG1127 146 MRKrvALARALAL--DPEILLYDEPTAGLDPITS----AVIDELIrelrDELGLTSVVVTHDLDSAFAIADRVAVLADGK 219
|
....
gi 489745462 231 VKAD 234
Cdd:COG1127 220 IIAE 223
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-236 |
1.49e-42 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 145.23 E-value: 1.49e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:COG1116 3 AAAPALELRGVSKRFPTGGGG-VTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 krtqfIGRVFQDPkmgtA--PRMTVAENLLLATKRGKRRFLKIRKLKQNLprfkkLAAVmnnGLENRLNTFVEGLSGGQR 158
Cdd:COG1116 82 -----RGVVFQEP----AllPWLTVLDNVALGLELRGVPKAERRERAREL-----LELV---GLAGFEDAYPHQLSGGMR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 159 QALSFLMATIERPDILLLDEHTAALDPHTSENLlavtdQQ-----IKENKLTALMITHHMEDALKYGNRLLVLKD--GKV 231
Cdd:COG1116 145 QRVAIARALANDPEVLLMDEPFGALDALTRERL-----QDellrlWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI 219
|
....*
gi 489745462 232 KADIN 236
Cdd:COG1116 220 VEEID 224
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
6-231 |
1.88e-42 |
|
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: 144.63 E-value: 1.88e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVktadGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:cd03256 1 IEVENLSKTY----PNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 ---IGRVFQDPKMgtAPRMTVAENLLLAtKRGKRRFLkiRKLKQNLPRFKK---LAAVMNNGLENRLNTFVEGLSGGQRQ 159
Cdd:cd03256 77 rrqIGMIFQQFNL--IERLSVLENVLSG-RLGRRSTW--RSLFGLFPKEEKqraLAALERVGLLDKAYQRADQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489745462 160 ALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03256 152 RVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRI 223
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
23-234 |
1.03e-41 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.11 E-value: 1.03e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF---IGRVFQDPKMgtAP 99
Cdd:COG2884 15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLrrrIGVVFQDFRL--LP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 RMTVAENLLLATK-RGKRRflkiRKLKQNLPrfkklAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:COG2884 93 DRTVYENVALPLRvTGKSR----KEIRRRVR-----EVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 179 HTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:COG2884 164 PTGNLDPETSWEIMELL-EEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRD 218
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
6-231 |
3.01e-41 |
|
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: 141.10 E-value: 3.01e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVkttVKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:cd03261 1 IELRGL---TKSFGGR--TVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 ---IGRVFQDPKMGTAprMTVAEN----LLLATKRGKRRflkIRKLKQnlprfKKLAAVmnnGLENRLNTFVEGLSGGQR 158
Cdd:cd03261 76 rrrMGMLFQSGALFDS--LTVFENvafpLREHTRLSEEE---IREIVL-----EKLEAV---GLRGAEDLYPAELSGGMK 142
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 159 QALSFLMATIERPDILLLDEHTAALDPHTSenllAVTDQQI----KENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03261 143 KRVALARALALDPELLLYDEPTAGLDPIAS----GVIDDLIrslkKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
6-235 |
5.13e-41 |
|
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: 140.30 E-value: 5.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEkrtqf 85
Cdd:cd03293 1 LEVRNVSKTYGGGGGA-VTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPD----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPkmGTAPRMTVAENLLLATKRGKRRFLKIRKLKQNLprfkkLAAVmnnGLENRLNTFVEGLSGGQRQALSFLM 165
Cdd:cd03293 75 RGYVFQQD--ALLPWLTVLDNVALGLELQGVPKAEARERAEEL-----LELV---GLSGFENAYPHQLSGGMRQRVALAR 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489745462 166 ATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVL--KDGKVKADI 235
Cdd:cd03293 145 ALAVDPDVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRIVAEV 216
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
24-231 |
1.54e-40 |
|
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: 137.53 E-value: 1.54e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRtQFIGRVFQDPkmGTAPRMTV 103
Cdd:cd03230 14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVK-RRIGYLPEEP--SLYENLTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLlatkrgkrrflkirklkqnlprfkklaavmnnglenrlntfvegLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:cd03230 91 RENLK--------------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTSGL 126
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489745462 184 DPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03230 127 DPESRREFWELLRELKKEGK-TILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
2-234 |
2.39e-40 |
|
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: 139.40 E-value: 2.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 2 TKPILELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEK 81
Cdd:COG0411 1 SDPLLEVRGL---TKRFGG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 82 RTQF-IGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRKLkqNLPRFKK------------LAAVmnnGLENRLNT 148
Cdd:COG0411 76 IARLgIARTFQNPRL--FPELTVLENVLVAAHARLGRGLLAALL--RLPRARReereareraeelLERV---GLADRADE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 149 FVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKD 228
Cdd:COG0411 149 PAGNLSYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDF 228
|
....*.
gi 489745462 229 GKVKAD 234
Cdd:COG0411 229 GRVIAE 234
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
6-230 |
1.57e-39 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 134.82 E-value: 1.57e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVkttVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:cd03228 1 IEFKNV---SFSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMgtaPRMTVAENLllatkrgkrrflkirklkqnlprfkklaavmnnglenrlntfvegLSGGQRQALSFLM 165
Cdd:cd03228 78 IAYVPQDPFL---FSGTIRENI---------------------------------------------LSGGQRQRIAIAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 166 ATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKEnkLTALMITHHMEdALKYGNRLLVLKDGK 230
Cdd:cd03228 110 ALLRDPPILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
5-231 |
4.54e-39 |
|
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: 135.40 E-value: 4.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ 84
Cdd:cd03258 1 MIELKNVSKVFGDTGGK-VTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 F---IGRVFQDPKMGTAPrmTVAEN----LLLATKRGKRRFLKIRKLkqnlprfkkLAAVmnnGLENRLNTFVEGLSGGQ 157
Cdd:cd03258 80 ArrrIGMIFQHFNLLSSR--TVFENvalpLEIAGVPKAEIEERVLEL---------LELV---GLEDKADAYPAQLSGGQ 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489745462 158 RQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03258 146 KQRVGIARALANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
6-239 |
4.86e-39 |
|
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: 136.09 E-value: 4.86e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:COG1124 2 LEVRNLSVSYGQGGRR-VPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPkMGTA-PRMTVAENLLLAtkrgkrrfLKIRKLKQNLPRFKK-LAAVmnnGLENR-LNTFVEGLSGGQRQALS 162
Cdd:COG1124 81 VQMVFQDP-YASLhPRHTVDRILAEP--------LRIHGLPDREERIAElLEQV---GLPPSfLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 163 FLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADINEQE 239
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVAD 225
|
|
| YbbA |
COG4181 |
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ... |
1-234 |
7.64e-39 |
|
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: 134.87 E-value: 7.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTADGEIVpILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:COG4181 4 SSAPIIELRGLTKTVGTGAGELT-ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDED 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQF----IGRVFQD-PKMGTaprMTVAEN----LLLATKRGKRRflKIRKLkqnlprfkkLAAVmnnGLENRLNTFVE 151
Cdd:COG4181 83 ARARLrarhVGFVFQSfQLLPT---LTALENvmlpLELAGRRDARA--RARAL---------LERV---GLGHRLDHYPA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 152 GLSGG--QRQALSflMATIERPDILLLDEHTAALDPHTSEN----LLAVTdqqiKENKLTALMITHHMEDALKYGnRLLV 225
Cdd:COG4181 146 QLSGGeqQRVALA--RAFATEPAILFADEPTGNLDAATGEQiidlLFELN----RERGTTLVLVTHDPALAARCD-RVLR 218
|
....*....
gi 489745462 226 LKDGKVKAD 234
Cdd:COG4181 219 LRAGRLVED 227
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
23-230 |
1.09e-38 |
|
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: 132.70 E-value: 1.09e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT--QFIGRVFQDPkmGTAPR 100
Cdd:cd03229 13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPlrRRIGMVFQDF--ALFPH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAENLLLatkrgkrrflkirklkqnlprfkklaavmnnglenrlntfveGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:cd03229 91 LTVLENIAL------------------------------------------GLSGGQQQRVALARALAMDPDVLLLDEPT 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 181 AALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:cd03229 129 SALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
29-235 |
1.34e-38 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 134.11 E-value: 1.34e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 29 IDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfIGRVFQDPKMgtAPRMTVAENLL 108
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP--VSMLFQENNL--FPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 109 LAtkrgkrrflkIR-KLKQNLPRFKKLAAVMNN-GLENRLNTFVEGLSGGQRQ--ALS--FLMatiERPdILLLDEHTAA 182
Cdd:COG3840 94 LG----------LRpGLKLTAEQRAQVEQALERvGLAGLLDRLPGQLSGGQRQrvALArcLVR---KRP-ILLLDEPFSA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489745462 183 LDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADI 235
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADG 212
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
23-252 |
6.85e-38 |
|
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: 132.67 E-value: 6.85e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQfIGRVFQDPkmGTAPRMT 102
Cdd:COG4555 14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQ-IGVLPDER--GLYDRLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLllatkrgkRRFLKIRKL--KQNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:COG4555 91 VRENI--------RYFAELYGLfdEELKKRIEELIELL--GLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 181 AALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADINEQE-KQNLKVSDLYKYF 252
Cdd:COG4555 161 NGLDVMARRLLREIL-RALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDElREEIGEENLEDAF 232
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
24-234 |
1.67e-37 |
|
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: 129.86 E-value: 1.67e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQdpkmgtaprmtv 103
Cdd:cd03214 13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 aenlllatkrgkrrflkirklkqnlprfkKLAAVmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:cd03214 81 -----------------------------ALELL---GLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489745462 184 DPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03214 129 DIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
24-230 |
3.18e-37 |
|
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: 128.52 E-value: 3.18e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQdpkmgtaprmtv 103
Cdd:cd00267 13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 aenlllatkrgkrrflkirklkqnlprfkklaavmnnglenrlntfvegLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:cd00267 81 -------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGL 111
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489745462 184 DPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:cd00267 112 DPASRERLLELLRELAEEGR-TVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
24-239 |
4.37e-37 |
|
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: 138.04 E-value: 4.37e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKM--Gtaprm 101
Cdd:COG2274 489 PVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLfsG----- 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLAtkrgkRRFLKIRKLKQNLprfkKLAAVMN--NGLENRLNTFV----EGLSGGQRQALSFLMATIERPDILL 175
Cdd:COG2274 564 TIRENITLG-----DPDATDEEIIEAA----RLAGLHDfiEALPMGYDTVVgeggSNLSGGQRQRLAIARALLRNPRILI 634
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 176 LDEHTAALDPHT----SENLlavtdQQIKENKlTALMITHHMEdALKYGNRLLVLKDGKVKADINEQE 239
Cdd:COG2274 635 LDEATSALDAETeaiiLENL-----RRLLKGR-TVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEE 695
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-231 |
4.58e-37 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 130.59 E-value: 4.58e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVktTVkTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:COG1121 2 MMMPAIELENL--TV-SYGGR--PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 krtqfIGRVfqdPKMGTAPR---MTVAEnLLLATKRGKRRFLKirklkqnlpRFKK---------LAAVmnnGLENRLNT 148
Cdd:COG1121 77 -----IGYV---PQRAEVDWdfpITVRD-VVLMGRYGRRGLFR---------RPSRadreavdeaLERV---GLEDLADR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 149 FVEGLSGGQRQ------ALsflmatIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNR 222
Cdd:COG1121 136 PIGELSGGQQQrvllarAL------AQDPDLLLLDEPFAGVDAATEEALYELLRELRREGK-TILVVTHDLGAVREYFDR 208
|
....*....
gi 489745462 223 LLVLKDGKV 231
Cdd:COG1121 209 VLLLNRGLV 217
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-231 |
1.18e-36 |
|
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: 129.33 E-value: 1.18e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVKTtvktADGEIvPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT 83
Cdd:COG0410 2 PMLEVENLHA----GYGGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 QF-IG------RVFqdpkmgtaPRMTVAENLLLATKRGKRRflkiRKLKQNLPR----FKKLAAvmnnglenRLNTFVEG 152
Cdd:COG0410 77 RLgIGyvpegrRIF--------PSLTVEENLLLGAYARRDR----AEVRADLERvyelFPRLKE--------RRRQRAGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 153 LSGGQRQALSF---LMAtieRPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDG 229
Cdd:COG0410 137 LSGGEQQMLAIgraLMS---RPKLLLLDEPSLGLAPLIVEEIFEII-RRLNREGVTILLVEQNARFALEIADRAYVLERG 212
|
..
gi 489745462 230 KV 231
Cdd:COG0410 213 RI 214
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
20-239 |
3.02e-36 |
|
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: 128.11 E-value: 3.02e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 20 GEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPkmgTAP 99
Cdd:cd03254 13 DEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDT---FLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 RMTVAENLLLATKRGKR-RFLKIRKLKQNLPRFKKLAavmnNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:cd03254 90 SGTIMENIRLGRPNATDeEVIEAAKEAGAHDFIMKLP----NGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDE 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 179 HTAALDPHTsENLLAVTDQQIKENKlTALMITHHMeDALKYGNRLLVLKDGKVKADINEQE 239
Cdd:cd03254 166 ATSNIDTET-EKLIQEALEKLMKGR-TSIIIAHRL-STIKNADKILVLDDGKIIEEGTHDE 223
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
6-231 |
5.77e-36 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 130.58 E-value: 5.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRtqF 85
Cdd:COG3839 4 LELENV---SKSYGG--VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--N 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPkmgtA--PRMTVAENLLLAtkrgkrrfLKIRKL-----KQnlpRFKKLAAVMnnGLENRLNTFVEGLSGGQR 158
Cdd:COG3839 77 IAMVFQSY----AlyPHMTVYENIAFP--------LKLRKVpkaeiDR---RVREAAELL--GLEDLLDRKPKQLSGGQR 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 159 Q------ALsflmatIERPDILLLDEHTAALDPHTSENLLAvtdqQIK----ENKLTALMITHHMEDALKYGNRLLVLKD 228
Cdd:COG3839 140 QrvalgrAL------VREPKVFLLDEPLSNLDAKLRVEMRA----EIKrlhrRLGTTTIYVTHDQVEAMTLADRIAVMND 209
|
...
gi 489745462 229 GKV 231
Cdd:COG3839 210 GRI 212
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
30-246 |
6.45e-36 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 127.39 E-value: 6.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 30 DLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfIGRVFQDPKMgtAPRMTVAENLLL 109
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSMLFQENNL--FSHLTVAQNIGL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 110 ATKRGkrrflkirkLKQNLPRFKKLAAVMNN-GLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTS 188
Cdd:PRK10771 95 GLNPG---------LKLNAAQREKLHAIARQmGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALR 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 189 ENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADINEQEKQNLKVS 246
Cdd:PRK10771 166 QEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKAS 223
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
30-234 |
6.60e-36 |
|
ATP-binding cassette domain of the thiamine transport system; Part of the binding-protein-dependent transport system tbpA-thiPQ for thiamine and TPP. Probably responsible for the translocation of thiamine across the membrane. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 126.84 E-value: 6.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 30 DLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfIGRVFQDPKMgtAPRMTVAENLLL 109
Cdd:cd03298 18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNL--FAHLTVEQNVGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 110 ATKRGkrrfLKIRKLKQNlpRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSE 189
Cdd:cd03298 94 GLSPG----LKLTAEDRQ--AIEVALARV--GLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489745462 190 NLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03298 166 EMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
5-231 |
6.93e-36 |
|
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: 127.80 E-value: 6.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTAdgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ 84
Cdd:TIGR02315 1 MLEVENLSKVYPNG----KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 F---IGRVFQDPKMgtAPRMTVAENLL---LATKRGkrrflkIRKLKQNLPRFKK---LAAVMNNGLENRLNTFVEGLSG 155
Cdd:TIGR02315 77 LrrrIGMIFQHYNL--IERLTVLENVLhgrLGYKPT------WRSLLGRFSEEDKeraLSALERVGLADKAYQRADQLSG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 156 GQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:TIGR02315 149 GQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEI 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
2-239 |
8.09e-36 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.83 E-value: 8.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 2 TKPILELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EE 80
Cdd:COG1129 1 AEPLLEMRGI---SKSFGG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSpRD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQFIGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRKLKQnlpRFKKLAAVMnnGLENRLNTFVEGLSGGQRQ- 159
Cdd:COG1129 76 AQAAGIAIIHQELNL--VPNLSVAENIFLGREPRRGGLIDWRAMRR---RARELLARL--GLDIDPDTPVGDLSVAQQQl 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 160 -----ALSFlmatieRPDILLLDEHTAALDPHTSENLLAVTDqQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV--- 231
Cdd:COG1129 149 veiarALSR------DARVLILDEPTASLTEREVERLFRIIR-RLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLvgt 221
|
250
....*....|
gi 489745462 232 --KADINEQE 239
Cdd:COG1129 222 gpVAELTEDE 231
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
6-231 |
5.58e-35 |
|
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: 131.03 E-value: 5.58e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:COG4988 337 IELEDV--SFSYPGGR--PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQ 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMgtaPRMTVAENLLLATKRGKRrflkiRKLKQNLprfkKLAAVMN--NGLENRLNTFVE----GLSGGQRQ 159
Cdd:COG4988 413 IAWVPQNPYL---FAGTIRENLRLGRPDASD-----EELEAAL----EAAGLDEfvAALPDGLDTPLGeggrGLSGGQAQ 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489745462 160 ALSFLMATIERPDILLLDEHTAALDPHTsENLLAVTDQQIKENKlTALMITHHMEDaLKYGNRLLVLKDGKV 231
Cdd:COG4988 481 RLALARALLRDAPLLLLDEPTAHLDAET-EAEILQALRRLAKGR-TVILITHRLAL-LAQADRILVLDDGRI 549
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
5-231 |
8.79e-35 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 127.12 E-value: 8.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ 84
Cdd:COG1135 1 MIELENLSKTFPTKGGP-VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 F---IGRVFQDPKMgtAPRMTVAEN----LLLA-TKRGKRRfLKIRKLkqnlprfkkLAAVmnnGLENRLNTFVEGLSGG 156
Cdd:COG1135 80 ArrkIGMIFQHFNL--LSSRTVAENvalpLEIAgVPKAEIR-KRVAEL---------LELV---GLSDKADAYPSQLSGG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 157 QRQ------ALsflmATieRPDILLLDEHTAALDPHTSENLLAVtdqqIKE-NK---LTALMITHHMEDALKYGNRLLVL 226
Cdd:COG1135 145 QKQrvgiarAL----AN--NPKVLLCDEATSALDPETTRSILDL----LKDiNRelgLTIVLITHEMDVVRRICDRVAVL 214
|
....*
gi 489745462 227 KDGKV 231
Cdd:COG1135 215 ENGRI 219
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
6-234 |
1.10e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 125.24 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVkttVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDItkMSEEKRT-- 83
Cdd:TIGR04520 1 IEVENV---SFSYPESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDT--LDEENLWei 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 -QFIGRVFQDPK---MGTAPRMTVA---ENLLLATKrgkrrflKIRKLKQNLprfkkLAAVmnnGLENRLNTFVEGLSGG 156
Cdd:TIGR04520 76 rKKVGMVFQNPDnqfVGATVEDDVAfglENLGVPRE-------EMRKRVDEA-----LKLV---GMEDFRDREPHLLSGG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 157 QRQ--ALSFLMATieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKyGNRLLVLKDGKVKAD 234
Cdd:TIGR04520 141 QKQrvAIAGVLAM--RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAE 217
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
6-231 |
1.61e-34 |
|
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: 123.89 E-value: 1.61e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKttvKTADGEIVpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqf 85
Cdd:cd03300 1 IELENVS---KFYGGFVA--LDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQdpKMGTAPRMTVAENLLLAtkrgkrrfLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLM 165
Cdd:cd03300 74 VNTVFQ--NYALFPHLTVFENIAFG--------LRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 166 ATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03300 144 ALVNEPKVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-239 |
2.38e-34 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 128.99 E-value: 2.38e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGhditkmsee 80
Cdd:COG3845 1 MMPPALELRGI---TKRFGG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDG--------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQF----------IGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRKLKqnlprfKKLAAVMNN-GLENRLNTF 149
Cdd:COG3845 67 KPVRIrsprdaialgIGMVHQHFML--VPNLTVAENIVLGLEPTKGGRLDRKAAR------ARIRELSERyGLDVDPDAK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 150 VEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDG 229
Cdd:COG3845 139 VEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEIL-RRLAAEGKSIIFITHKLREVMAIADRVTVLRRG 217
|
250
....*....|....*
gi 489745462 230 KV-----KADINEQE 239
Cdd:COG3845 218 KVvgtvdTAETSEEE 232
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
25-231 |
3.82e-34 |
|
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: 122.25 E-value: 3.82e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT--QFIGRVFQDPKMgtAPRMT 102
Cdd:cd03262 15 VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINElrQKVGMVFQQFNL--FPHLT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATKrgkrrflKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAA 182
Cdd:cd03262 93 VLENITLAPI-------KVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSA 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489745462 183 LDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03262 166 LDPELVGEVLDVM-KDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-226 |
2.04e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.51 E-value: 2.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVkTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKrt 83
Cdd:COG4525 2 SMLTVRHV-SVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 qfiGRVFQdpKMGTAPRMTVAENLLLAtkrgkrrfLKIRKLkqnlPRF-------KKLAAVmnnGLENRLNTFVEGLSGG 156
Cdd:COG4525 79 ---GVVFQ--KDALLPWLNVLDNVAFG--------LRLRGV----PKAerraraeELLALV---GLADFARRRIWQLSGG 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489745462 157 QRQALSFLMATIERPDILLLDEHTAALDPHTSEN----LLAVTDQQIKenklTALMITHHMEDALKYGNRLLVL 226
Cdd:COG4525 139 MRQRVGIARALAADPRFLLMDEPFGALDALTREQmqelLLDVWQRTGK----GVFLITHSVEEALFLATRLVVM 208
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
26-233 |
2.48e-33 |
|
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: 120.17 E-value: 2.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQfIGRVFQDPKMGtaPRMTVAE 105
Cdd:cd03265 16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR-IGIVFQDLSVD--DELTGWE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 NLLLatkRGKRRFLKIRKLKQnlpRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDP 185
Cdd:cd03265 93 NLYI---HARLYGVPGAERRE---RIDELLDFV--GLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDP 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489745462 186 HTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:cd03265 165 QTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIA 212
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
24-227 |
3.19e-33 |
|
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: 119.95 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEkrtqfIGRVFQDPKMGTAPRMTV 103
Cdd:cd03235 13 PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQRRSIDRDFPISV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGKRRFLKIRKlkqnlPRFKK----LAAVMNNGLENRlnTFVEgLSGGQRQALSFLMATIERPDILLLDEH 179
Cdd:cd03235 88 RDVVLMGLYGHKGLFRRLSK-----ADKAKvdeaLERVGLSELADR--QIGE-LSGGQQQRVLLARALVQDPDLLLLDEP 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489745462 180 TAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLK 227
Cdd:cd03235 160 FAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLN 206
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
26-234 |
5.54e-33 |
|
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: 121.02 E-value: 5.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF---IGRVFQDPKM---GTap 99
Cdd:TIGR04521 21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDLrkkVGLVFQFPEHqlfEE-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 rmTVAE-------NLLLATKRGKRRFlkirklkqnlprFKKLAAVmnnGLENRL---NTFveGLSGGQ--RQALSFLMAT 167
Cdd:TIGR04521 99 --TVYKdiafgpkNLGLSEEEAEERV------------KEALELV---GLDEEYlerSPF--ELSGGQmrRVAIAGVLAM 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 168 ieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:TIGR04521 160 --EPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLD 224
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
25-231 |
1.15e-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: 118.82 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAG-----SLRPDSGFLLHNGHDITKMSE---EKRTQfIGRVFQDPkmg 96
Cdd:cd03260 15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVdvlELRRR-VGMVFQKP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 97 TAPRMTVAENLLLAtkrgkrrfLKIRKLKQNlprfKKLAAVMNNGLE---------NRLNTFveGLSGGQRQALSFLMAT 167
Cdd:cd03260 91 NPFPGSIYDNVAYG--------LRLHGIKLK----EELDERVEEALRkaalwdevkDRLHAL--GLSGGQQQRLCLARAL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 168 IERPDILLLDEHTAALDPHTSENLlavtDQQIKE--NKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03260 157 ANEPEVLLLDEPTSALDPISTAKI----EELIAElkKEYTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
5-231 |
1.20e-32 |
|
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: 120.93 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRP---DSGFLLHNGHDITKMSEEK 81
Cdd:COG0444 1 LLEVRNLKVYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 82 RTQFIGR----VFQDPkMgTA--PRMTV----AENLLLATKRGKR-RFLKIRKLkqnlprfkkLAAVmnnGL---ENRLN 147
Cdd:COG0444 80 LRKIRGReiqmIFQDP-M-TSlnPVMTVgdqiAEPLRIHGGLSKAeARERAIEL---------LERV---GLpdpERRLD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 148 TFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDphtsenllaVTDQ-QI--------KENKLTALMITHHMEDALK 218
Cdd:COG0444 146 RYPHELSGGMRQRVMIARALALEPKLLIADEPTTALD---------VTIQaQIlnllkdlqRELGLAILFITHDLGVVAE 216
|
250
....*....|...
gi 489745462 219 YGNRLLVLKDGKV 231
Cdd:COG0444 217 IADRVAVMYAGRI 229
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
6-226 |
1.60e-32 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 117.97 E-value: 1.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPD---SGFLLHNGHDITKMSEEKR 82
Cdd:COG4136 2 LSLENL--TITLGG---RPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 TqfIGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRKLKQnlprfkklaAVMNNGLENRLNTFVEGLSGGQRQALS 162
Cdd:COG4136 77 R--IGILFQDDLL--FPHLSVGENLAFALPPTIGRAQRRARVEQ---------ALEEAGLAGFADRDPATLSGGQRARVA 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489745462 163 FLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGnRLLVL 226
Cdd:COG4136 144 LLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAG-RVLDL 206
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
6-234 |
2.34e-32 |
|
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: 117.69 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVkttVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:cd03245 3 IEFRNV---SFSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMGTAprmTVAENLLLATKRGK-RRFLK------IRKLKQNLPrfkklaavmnNGLENRLNTFVEGLSGGQR 158
Cdd:cd03245 80 IGYVPQDVTLFYG---TLRDNITLGAPLADdERILRaaelagVTDFVNKHP----------NGLDLQIGERGRGLSGGQR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 159 QALSFLMATIERPDILLLDEHTAALDpHTSENLLAVTDQQIKENKlTALMITHHMEdALKYGNRLLVLKDGKVKAD 234
Cdd:cd03245 147 QAVALARALLNDPPILLLDEPTSAMD-MNSEERLKERLRQLLGDK-TLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
26-181 |
2.45e-32 |
|
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: 115.44 E-value: 2.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGtaPRMTVAE 105
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLF--PRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 106 NLLL-ATKRGKRRFLKIRKLKQNLPRFKklaavMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:pfam00005 79 NLRLgLLLKGLSKREKDARAEEALEKLG-----LGDLADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
26-234 |
2.52e-32 |
|
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: 117.40 E-value: 2.52e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIK---AGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNG---HDITK---MSEEKRTqfIGRVFQDPKMg 96
Cdd:cd03297 10 LPDFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlFDSRKkinLPPQQRK--IGLVFQQYAL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 97 tAPRMTVAENLLLATKRGKRRFLKIRklkqnlprFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLL 176
Cdd:cd03297 87 -FPHLNVRENLAFGLKRKRNREDRIS--------VDELLDLL--GLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 177 DEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03297 156 DEPFSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYI 213
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
24-231 |
6.82e-32 |
|
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: 117.02 E-value: 6.82e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQdpKMGTAPRMTV 103
Cdd:cd03295 15 KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQ--QIGLFPHMTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGKRRFLKIRKlkqnlpRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:cd03295 93 EENIALVPKLLKWPKEKIRE------RADELLALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGAL 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489745462 184 DPHTSENLlavTDQQIKENKL---TALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03295 167 DPITRDQL---QEEFKRLQQElgkTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
6-231 |
1.34e-31 |
|
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: 115.43 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqf 85
Cdd:cd03301 1 VELENV---TKRFGN--VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDpkMGTAPRMTVAENLLLATKRGKRRFLKIRKlkqnlpRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLM 165
Cdd:cd03301 74 IAMVFQN--YALYPHMTVYDNIAFGLKLRKVPKDEIDE------RVREVAELL--QIEHLLDRKPKQLSGGQRQRVALGR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 166 ATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03301 144 AIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
26-229 |
1.40e-31 |
|
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: 116.03 E-value: 1.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfigrVFQDPKMgtAPRMTVAE 105
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRMV-----VFQNYSL--LPWLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 NLLLATKRGKRrflkirklkqNLPRFKKLAAVMNN----GLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:TIGR01184 74 NIALAVDRVLP----------DLSKSERRAIVEEHialvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFG 143
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489745462 182 ALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDG 229
Cdd:TIGR01184 144 ALDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
24-230 |
1.67e-31 |
|
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: 115.27 E-value: 1.67e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQfIGRVFQDPkmGTAPRMTV 103
Cdd:COG4133 16 LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR-LAYLGHAD--GLKPELTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLatkrgkrrFLKIRKLKQNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:COG4133 93 RENLRF--------WAALYGLRADREAIDEALEAV--GLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489745462 184 DPHTSENLLAVTDQQiKENKLTALMITHHMEDALkyGNRLLVLKDGK 230
Cdd:COG4133 163 DAAGVALLAELIAAH-LARGGAVLLTTHQPLELA--AARVLDLGDFK 206
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
6-233 |
1.76e-31 |
|
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: 115.29 E-value: 1.76e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVkttVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRtQF 85
Cdd:cd03263 1 LQIRNL---TKTYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR-QS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPkmGTAPRMTVAENLLLATK-RGKRRfLKIRKLKQNLprFKKLaavmnnGLENRLNTFVEGLSGGQRQALSFL 164
Cdd:cd03263 77 LGYCPQFD--ALFDELTVREHLRFYARlKGLPK-SEIKEEVELL--LRVL------GLTDKANKRARTLSGGMKRKLSLA 145
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 165 MATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:cd03263 146 IALIGGPSVLLLDEPTSGLDPASRRAIWDLI-LEVRKGR-SIILTTHSMDEAEALCDRIAIMSDGKLRC 212
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
1-234 |
1.93e-31 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 118.90 E-value: 1.93e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKttvKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:PRK09452 10 SLSPLVELRGIS---KSFDGK--EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRtqFIGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRklkqnlPR-FKKLAAVMnngLENRLNTFVEGLSGGQRQ 159
Cdd:PRK09452 85 NR--HVNTVFQSYAL--FPHMTVFENVAFGLRMQKTPAAEIT------PRvMEALRMVQ---LEEFAQRKPHQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 160 ALSFLMATIERPDILLLDEHTAALDphtsENLLAVTDQQIK--ENKL--TALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:PRK09452 152 RVAIARAVVNKPKVLLLDESLSALD----YKLRKQMQNELKalQRKLgiTFVFVTHDQEEALTMSDRIVVMRDGRIEQD 226
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
23-239 |
3.35e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 115.19 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT--QFIGRVFQdpKMGTAPR 100
Cdd:PRK09493 14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLirQEAGMVFQ--QFYLFPH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAENLLLatkrGKRRflkIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PRK09493 92 LTALENVMF----GPLR---VRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPT 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 181 AALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADINEQE 239
Cdd:PRK09493 165 SALDPELRHEVLKVM-QDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQV 222
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
26-231 |
4.77e-31 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 117.56 E-value: 4.77e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDI-TKMSEEKRTqfIGRVFQDPkmgtA--PRMT 102
Cdd:COG1118 18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERR--VGFVFQHY----AlfPHMT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENL---LLATKRGKRRflkIRKLKQNLprfkkLAAVMNNGLENRlntFVEGLSGGQRQ--ALSFLMATieRPDILLLD 177
Cdd:COG1118 92 VAENIafgLRVRPPSKAE---IRARVEEL-----LELVQLEGLADR---YPSQLSGGQRQrvALARALAV--EPEVLLLD 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 178 EHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:COG1118 159 EPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
24-231 |
6.04e-31 |
|
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: 114.74 E-value: 6.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfIGRVFQDPKMgtAPRMTV 103
Cdd:cd03296 16 VALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN--VGFVFQHYAL--FRHMTV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLAtkrgkrrfLKIRKLKQNLPRFKKLAAVMN-------NGLENRlntFVEGLSGGQRQALSFLMATIERPDILLL 176
Cdd:cd03296 92 FDNVAFG--------LRVKPRSERPPEAEIRAKVHEllklvqlDWLADR---YPAQLSGGQRQRVALARALAVEPKVLLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 177 DEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03296 161 DEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
1-233 |
1.04e-30 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 115.11 E-value: 1.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTADGeivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGhdiTKMSEE 80
Cdd:PRK13635 1 MKEEIIRVEHISFRYPDAAT---YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGG---MVLSEE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 K----RTQfIGRVFQDPK---MGTAPRMTVA---ENlllatkRGKRRFLKIRKLKQnlprfkklaAVMNNGLENRLNTFV 150
Cdd:PRK13635 75 TvwdvRRQ-VGMVFQNPDnqfVGATVQDDVAfglEN------IGVPREEMVERVDQ---------ALRQVGMEDFLNREP 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 151 EGLSGGQRQ--ALSFLMATieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKyGNRLLVLKD 228
Cdd:PRK13635 139 HRLSGGQKQrvAIAGVLAL--QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNK 215
|
....*
gi 489745462 229 GKVKA 233
Cdd:PRK13635 216 GEILE 220
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
23-231 |
1.60e-30 |
|
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: 111.37 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EEKRTQFIGRVFQdpkmgtaprm 101
Cdd:cd03216 13 VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASpRDARRAGIAMVYQ---------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 tvaenlllatkrgkrrflkirklkqnlprfkklaavmnnglenrlntfvegLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:cd03216 83 ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEPTA 111
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 182 ALDPHTSENLLAVTDqQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03216 112 ALTPAEVERLFKVIR-RLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
25-234 |
2.43e-30 |
|
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: 112.29 E-value: 2.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGdFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRtQFIGRVFQDPkmGTAPRMTVA 104
Cdd:cd03264 15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLR-RRIGYLPQEF--GVYPNFTVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 105 ENL-LLATKRGkrrfLKIRKLKQNLPRFkkLAAVmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:cd03264 91 EFLdYIAWLKG----IPSKEVKARVDEV--LELV---NLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 184 DP---HTSENLLavtdQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03264 162 DPeerIRFRNLL----SELGEDR-IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
4-231 |
2.85e-30 |
|
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: 113.51 E-value: 2.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVKTTVKTADGeIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSE---- 79
Cdd:cd03294 19 KLLAKGKSKEEILKKTG-QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRkelr 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 80 EKRTQFIGRVFQdpKMGTAPRMTVAENLLLAtkrgkrrfLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQ 159
Cdd:cd03294 98 ELRRKKISMVFQ--SFALLPHRTVLENVAFG--------LEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQ 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 160 ALSFLMATIERPDILLLDEHTAALDP----HTSENLLAVTdqqiKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03294 168 RVGLARALAVDPDILLMDEAFSALDPlirrEMQDELLRLQ----AELQKTIVFITHDLDEALRLGDRIAIMKDGRL 239
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
23-231 |
6.31e-30 |
|
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: 111.35 E-value: 6.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT---QFIGRVFQDPKMgtAP 99
Cdd:cd03292 14 TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPylrRKIGVVFQDFRL--LP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 RMTVAENLLLAtkrgkrrfLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEH 179
Cdd:cd03292 92 DRNVYENVAFA--------LEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEP 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489745462 180 TAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03292 164 TGNLDPDTTWEIMNLL-KKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
24-231 |
1.60e-29 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.03 E-value: 1.60e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EEKRTQfIGRVFQDPKMGTaprMT 102
Cdd:COG1132 354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTlESLRRQ-IGVVPQDTFLFS---GT 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLAtkrgkrrflkirklKQNLPRFK-----KLAAVMN--NGLENRLNTFV-EG---LSGGQRQALSFLMATIERP 171
Cdd:COG1132 430 IRENIRYG--------------RPDATDEEveeaaKAAQAHEfiEALPDGYDTVVgERgvnLSGGQRQRIAIARALLKDP 495
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 172 DILLLDEHTAALDPHT----SENLLAVTdqqikENKlTALMITHHM---EDAlkygNRLLVLKDGKV 231
Cdd:COG1132 496 PILILDEATSALDTETealiQEALERLM-----KGR-TTIVIAHRLstiRNA----DRILVLDDGRI 552
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
23-231 |
3.14e-29 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 110.08 E-value: 3.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT--QFIGRVFQD----Pkmg 96
Cdd:COG1126 14 LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDINKlrRKVGMVFQQfnlfP--- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 97 tapRMTVAENLLLA-TKRGKRRFLKIRKLKQNLprfkkLAAVmnnGLENRLNTFVEGLSGGQRQ------ALSflMatie 169
Cdd:COG1126 91 ---HLTVLENVTLApIKVKKMSKAEAEERAMEL-----LERV---GLADKADAYPAQLSGGQQQrvaiarALA--M---- 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489745462 170 RPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:COG1126 154 EPKVMLFDEPTSALDPELVGEVLDVM-RDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRI 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
6-231 |
6.42e-29 |
|
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: 107.30 E-value: 6.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:cd03246 1 LEVENV--SFRYPGAE-PPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMGTAprmTVAENLllatkrgkrrflkirklkqnlprfkklaavmnnglenrlntfvegLSGGQRQALSFLM 165
Cdd:cd03246 78 VGYLPQDDELFSG---SIAENI---------------------------------------------LSGGQRQRLGLAR 109
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 166 ATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEdALKYGNRLLVLKDGKV 231
Cdd:cd03246 110 ALYGNPRILVLDEPNSHLDVEGERALNQAI-AALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
26-234 |
7.21e-29 |
|
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: 108.61 E-value: 7.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRtQFIGRVFQdpKMGTAPRMTVAE 105
Cdd:cd03266 21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEAR-RRLGFVSD--STGLYDRLTARE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 NLLLAtkrGKRRFLKIRKLKQnlpRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDP 185
Cdd:cd03266 98 NLEYF---AGLYGLKGDELTA---RLEELADRL--GMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDV 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489745462 186 HTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03266 170 MATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYE 217
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
29-233 |
1.01e-28 |
|
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 443319 [Multi-domain] Cd Length: 358 Bit Score: 111.35 E-value: 1.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 29 IDLKIKAGDF------------IT-IIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGH---DITK---MSEEKRTqfIGRV 89
Cdd:COG4148 5 VDFRLRRGGFtldvdftlpgrgVTaLFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgifLPPHRRR--IGYV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 90 FQDPKMgtAPRMTVAENLLLATKRGKRRflkirklkQNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQRQ------ALsf 163
Cdd:COG4148 83 FQEARL--FPHLSVRGNLLYGRKRAPRA--------ERRISFDEVVELL--GIGHLLDRRPATLSGGERQrvaigrAL-- 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 164 lmATieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:COG4148 149 --LS--SPRLLLMDEPLAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVA 214
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
7-231 |
1.97e-28 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 110.28 E-value: 1.97e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 7 ELKDVKTTVKTADGEIVPiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF- 85
Cdd:PRK11153 3 ELKNISKVFPQGGRTIHA-LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKAr 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 --IGRVFQDPKMgTAPRmTVAENLLLATKRGKRRFLKIRKLKQNLprfkkLAAVmnnGLENRLNTFVEGLSGGQRQALSF 163
Cdd:PRK11153 82 rqIGMIFQHFNL-LSSR-TVFDNVALPLELAGTPKAEIKARVTEL-----LELV---GLSDKADRYPAQLSGGQKQRVAI 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 164 LMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK11153 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRL 219
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
25-235 |
2.36e-28 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 108.23 E-value: 2.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfigrVFQDPKMgtAPRMTVA 104
Cdd:PRK11247 27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTRL-----MFQDARL--LPWKKVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 105 ENLLLATKrGKRRflkirklkqnlPR-FKKLAAVmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:PRK11247 100 DNVGLGLK-GQWR-----------DAaLQALAAV---GLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGAL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489745462 184 DPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADI 235
Cdd:PRK11247 165 DALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLDL 216
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
8-234 |
6.92e-28 |
|
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: 106.08 E-value: 6.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 8 LKDVKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfllhnghDITKMseekrtqfiG 87
Cdd:cd03220 20 LKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSG-------TVTVR---------G 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 88 RV--FQDPKMGTAPRMTVAENL-LLATKRGKRRflkirklkqnlprfKKLAAVMN-----NGLENRLNTFVEGLSGGQRQ 159
Cdd:cd03220 84 RVssLLGLGGGFNPELTGRENIyLNGRLLGLSR--------------KEIDEKIDeiiefSELGDFIDLPVKTYSSGMKA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 160 ALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03220 150 RLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
25-232 |
1.28e-27 |
|
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: 105.03 E-value: 1.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDItkmSEEKRTQFIGRVFQDP--KMGTAprmT 102
Cdd:cd03226 15 ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVMQDVdyQLFTD---S 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATKRGKRRFLKIRKLkqnlprFKKLAavmnnglenrLNTFVE----GLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:cd03226 89 VREELLLGLKELDAGNEQAETV------LKDLD----------LYALKErhplSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 179 HTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVK 232
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
3-211 |
2.38e-27 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 104.80 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKTTVKTAdgeivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKR 82
Cdd:PRK10247 5 SPLLQLQNVGYLAGDA-----KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 TQFIGRVFQDPKM-GTaprmTVAENLLLAtkrgkrrfLKIRKLKqnlPRFKKLAA-VMNNGL-ENRLNTFVEGLSGGQRQ 159
Cdd:PRK10247 80 RQQVSYCAQTPTLfGD----TVYDNLIFP--------WQIRNQQ---PDPAIFLDdLERFALpDTILTKNIAELSGGEKQ 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489745462 160 ALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITH 211
Cdd:PRK10247 145 RISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTH 196
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
23-234 |
4.46e-27 |
|
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.
Pssm-ID: 213234 [Multi-domain] Cd Length: 236 Bit Score: 104.34 E-value: 4.46e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQfIGRVFqdpkmgtAPRMT 102
Cdd:cd03267 34 VEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVF-------GQKTQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENL-LLATKRGKRRFLKI--RKLKQNLprfKKLAAVMNngLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEH 179
Cdd:cd03267 106 LWWDLpVIDSFYLLAAIYDLppARFKKRL---DELSELLD--LEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEP 180
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 180 TAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:cd03267 181 TIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
6-233 |
5.14e-27 |
|
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: 103.51 E-value: 5.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTadgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHditKMSEEKRTQF 85
Cdd:cd03269 1 LEVENVTKRFGR-----VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGK---PLDIAARNRI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 iGRVFQDpkMGTAPRMTVAENLL-LATKRGkrrfLKIRKLKQNLPR-FKKLaavmnnGLENRLNTFVEGLSGGQRQALSF 163
Cdd:cd03269 73 -GYLPEE--RGLYPKMKVIDQLVyLAQLKG----LKKEEARRRIDEwLERL------ELSEYANKRVEELSKGNQQKVQF 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 164 LMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:cd03269 140 IAAVIHDPELLILDEPFSGLDPVNVELLKDVIRELARAGK-TVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
8-234 |
5.42e-27 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 104.39 E-value: 5.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 8 LKDVKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGhditkmseeKRTQFIG 87
Cdd:COG1134 24 LKELLLRRRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG---------RVSALLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 88 rvfqdpkMGTA--PRMTVAENLLLatkRGkrRFLKIRKlkqnlprfKKLAAVMNN-----GLENRLNTFVEGLSGGQRQA 160
Cdd:COG1134 95 -------LGAGfhPELTGRENIYL---NG--RLLGLSR--------KEIDEKFDEivefaELGDFIDQPVKTYSSGMRAR 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 161 LSFLMATIERPDILLLDEhtaaldphtsenLLAVTD-----------QQIKENKLTALMITHHMEDALKYGNRLLVLKDG 229
Cdd:COG1134 155 LAFAVATAVDPDILLVDE------------VLAVGDaafqkkclariRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKG 222
|
....*
gi 489745462 230 KVKAD 234
Cdd:COG1134 223 RLVMD 227
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-212 |
1.98e-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: 107.06 E-value: 1.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 2 TKPILELKDVktTVKTADGEIVpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEK 81
Cdd:TIGR02868 331 GKPTLELRDL--SAGYPGAPPV--LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDE 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 82 RTQFIGRVFQDPKMGTAprmTVAENLLLATKRGKRRFLkIRKLKQnlPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQAL 161
Cdd:TIGR02868 407 VRRRVSVCAQDAHLFDT---TVRENLRLARPDATDEEL-WAALER--VGLADWLRALPDGLDTVLGEGGARLSGGERQRL 480
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 162 SFLMATIERPDILLLDEHTAALDPHTS----ENLLAVTDQqikenkLTALMITHH 212
Cdd:TIGR02868 481 ALARALLADAPILLLDEPTEHLDAETAdellEDLLAALSG------RTVVLITHH 529
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
1-244 |
2.23e-26 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 107.12 E-value: 2.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTkPILELKDVKTTVKTADgEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNtIAGSL-RPDSGFLLHNGHDITKMSE 79
Cdd:PRK10535 1 MT-ALLELKDIRRSYPSGE-EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLdKPTSGTYRVAGQDVATLDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 80 EK----RTQFIGRVFQdpKMGTAPRMTVAENL----LLATKRGKRRFLKIRKLKQNLprfkklaavmnnGLENRLNTFVE 151
Cdd:PRK10535 78 DAlaqlRREHFGFIFQ--RYHLLSHLTAAQNVevpaVYAGLERKQRLLRAQELLQRL------------GLEDRVEYQPS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 152 GLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKyGNRLLVLKDGKV 231
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAIL-HQLRDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEI 221
|
250
....*....|...
gi 489745462 232 KADINEQEKQNLK 244
Cdd:PRK10535 222 VRNPPAQEKVNVA 234
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
6-230 |
2.38e-26 |
|
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: 101.78 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHditkmseekrtqf 85
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMgtaPRMTVAENLLLATKRGKRRFLKIRKLKQNLPRFKKlaavmnngLENRLNTFV-EG---LSGGQRQAL 161
Cdd:cd03250 68 IAYVSQEPWI---QNGTIRENILFGKPFDEERYEKVIKACALEPDLEI--------LPDGDLTEIgEKginLSGGQKQRI 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 162 SFLMATIERPDILLLDEHTAALDPHTSENLLavtDQQI----KENKlTALMITHHMEdALKYGNRLLVLKDGK 230
Cdd:cd03250 137 SLARAVYSDADIYLLDDPLSAVDAHVGRHIF---ENCIlgllLNNK-TRILVTHQLQ-LLPHADQIVVLDNGR 204
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
25-233 |
1.40e-25 |
|
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: 100.29 E-value: 1.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfigrvfqdpKMGTA------ 98
Cdd:TIGR03410 15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERA----------RAGIAyvpqgr 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 ---PRMTVAENLLLATKRGKRRFLKIRK--------LKQNLPRfkklaavmNNGLenrlntfvegLSGGQRQALSFLMAT 167
Cdd:TIGR03410 85 eifPRLTVEENLLTGLAALPRRSRKIPDeiyelfpvLKEMLGR--------RGGD----------LSGGQQQQLAIARAL 146
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 168 IERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:TIGR03410 147 VTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVA 212
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
24-217 |
2.71e-25 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 98.46 E-value: 2.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDitkmseekrtqfigRVFQDPKMGTAPR--- 100
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA--------------RVAYVPQRSEVPDslp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAEnlLLATKRGKRRFLkIRKLKQNLPRF--KKLAAVMNNGLENRLntfVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:NF040873 72 LTVRD--LVAMGRWARRGL-WRRLTRDDRAAvdDALERVGLADLAGRQ---LGELSGGQRQRALLAQGLAQEADLLLLDE 145
|
170 180 190
....*....|....*....|....*....|....*....
gi 489745462 179 HTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDAL 217
Cdd:NF040873 146 PTTGLDAESRERIIALL-AEEHARGATVVVVTHDLELVR 183
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
24-234 |
3.34e-25 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 99.85 E-value: 3.34e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMgTAPrMTV 103
Cdd:PRK13548 16 TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSL-SFP-FTV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AEnlLLATKRGKRRFLKIRklKQNLPRfKKLAAVMNNGLENRlntFVEGLSGGQRQ------ALSFLMATIERPDILLLD 177
Cdd:PRK13548 94 EE--VVAMGRAPHGLSRAE--DDALVA-AALAQVDLAHLAGR---DYPQLSGGEQQrvqlarVLAQLWEPDGPPRWLLLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 178 EHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:PRK13548 166 EPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVAD 222
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
4-234 |
3.64e-25 |
|
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: 99.77 E-value: 3.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVktTVKTADgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLH------NGHDItkm 77
Cdd:COG1119 2 PLLELRNV--TVRRGG---KTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDVRlfgerrGGEDV--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 78 sEEKRTQfIGRVFQDPKMGTAPRMTVAENLL--------LATKRGKRRFLKIRKLkqnlprfkkLAAVmnnGLENRLNTF 149
Cdd:COG1119 74 -WELRKR-IGLVSPALQLRFPRDETVLDVVLsgffdsigLYREPTDEQRERAREL---------LELL---GLAHLADRP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 150 VEGLSGGQRQ------ALsflmatIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRL 223
Cdd:COG1119 140 FGTLSQGEQRrvliarAL------VKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHV 213
|
250
....*....|.
gi 489745462 224 LVLKDGKVKAD 234
Cdd:COG1119 214 LLLKDGRVVAA 224
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
24-216 |
5.81e-25 |
|
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: 102.75 E-value: 5.81e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAprmTV 103
Cdd:TIGR02857 336 PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG---TI 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGKRrflkiRKLKQNLPR--FKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:TIGR02857 413 AENIRLARPDASD-----AEIREALERagLDEFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTA 487
|
170 180 190
....*....|....*....|....*....|....*...
gi 489745462 182 ALDPHTsENLLAVTDQQIKENKlTALMITH---HMEDA 216
Cdd:TIGR02857 488 HLDAET-EAEVLEALRALAQGR-TVLLVTHrlaLAALA 523
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
6-234 |
9.46e-25 |
|
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: 96.61 E-value: 9.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVktaDGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMsEEKRTQF 85
Cdd:cd03247 1 LSINNVSFSY---PEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL-EKALSSL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMGTAprmTVAENLllatkrGKRrflkirklkqnlprfkklaavmnnglenrlntfvegLSGGQRQALSFLM 165
Cdd:cd03247 77 ISVLNQRPYLFDT---TLRNNL------GRR------------------------------------FSGGERQRLALAR 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 166 ATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENklTALMITHHMEdALKYGNRLLVLKDGKVKAD 234
Cdd:cd03247 112 ILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK--TLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
24-249 |
1.29e-24 |
|
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.
Pssm-ID: 213185 [Multi-domain] Cd Length: 232 Bit Score: 97.61 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF-IGRVFQDPKMGTapRMT 102
Cdd:cd03218 14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYLPQEASIFR--KLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATK-RGKRRFLKIRKLKQNLPRFkklaavmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:cd03218 92 VEENILAVLEiRGLSKKEREEKLEELLEEF---------HITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFA 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489745462 182 ALDPhtsenlLAVTD-----QQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADIN-EQEKQNLKVSDLY 249
Cdd:cd03218 163 GVDP------IAVQDiqkiiKILKDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTpEEIAANELVRKVY 230
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
24-248 |
1.70e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.52 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSE-EKRTQFIGRVFQDPKMGTAPRmT 102
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVGIVFQNPETQFVGR-T 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATKRGKRRFLKIRKLKQNlprfkklaAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAA 182
Cdd:PRK13644 95 VEEDLAFGPENLCLPPIEIRKRVDR--------ALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSM 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 183 LDPHTSENLLAVTdQQIKENKLTALMITHHMEDaLKYGNRLLVLKDGKVKAdinEQEKQNLkVSDL 248
Cdd:PRK13644 167 LDPDSGIAVLERI-KKLHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVL---EGEPENV-LSDV 226
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
23-231 |
1.85e-24 |
|
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: 97.61 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIagsLR---PDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTap 99
Cdd:cd03249 16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLL---ERfydPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFD-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 rMTVAENLLLatkrGKRRflkiRKLKQnLPRFKKLAAVMN--NGLENRLNTFVeG-----LSGGQRQALSFLMATIERPD 172
Cdd:cd03249 91 -GTIAENIRY----GKPD----ATDEE-VEEAAKKANIHDfiMSLPDGYDTLV-GergsqLSGGQKQRIAIARALLRNPK 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 173 ILLLDEHTAALDPHtSENLLAVTDQQIKENKlTALMITHHMEdALKYGNRLLVLKDGKV 231
Cdd:cd03249 160 ILLLDEATSALDAE-SEKLVQEALDRAMKGR-TTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
26-231 |
2.30e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 98.20 E-value: 2.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDIT----KMSEEKRTqfIGRVFQDPKMGTAPRm 101
Cdd:PRK13637 23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkkvKLSDIRKK--VGLVFQYPEYQLFEE- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLATKRgkrRFLKIRKLKQNLPRFKKLAAVMNNGLENRlNTFveGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:PRK13637 100 TIEKDIAFGPIN---LGLSEEEIENRVKRAMNIVGLDYEDYKDK-SPF--ELSGGQKRRVAIAGVVAMEPKILILDEPTA 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 182 ALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK13637 174 GLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKC 223
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
10-231 |
2.67e-24 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 97.51 E-value: 2.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 10 DVKTTVKTADGEIVpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLlhNGHDIT-----KMSEEKRT- 83
Cdd:PRK11264 5 EVKNLVKKFHGQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTI--RVGDITidtarSLSQQKGLi 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 ----QFIGRVFQDpkMGTAPRMTVAENLL---LATKRGKRrflkirklKQNLPRFKKLAAVMnnGLENRLNTFVEGLSGG 156
Cdd:PRK11264 81 rqlrQHVGFVFQN--FNLFPHRTVLENIIegpVIVKGEPK--------EEATARARELLAKV--GLAGKETSYPRRLSGG 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 157 QRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAvTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK11264 149 QQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLN-TIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRI 222
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
25-232 |
4.03e-24 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 96.96 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDIT---------KMSEEKRTQF----IGRVFQ 91
Cdd:PRK10619 20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlKVADKNQLRLlrtrLTMVFQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 92 DPKMGTapRMTVAENLLLATkrgkrrfLKIRKLKQNLPRFKKLAAVMNNGLENRLN-TFVEGLSGGQRQALSFLMATIER 170
Cdd:PRK10619 100 HFNLWS--HMTVLENVMEAP-------IQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAME 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489745462 171 PDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVK 232
Cdd:PRK10619 171 PEVLLFDEPTSALDPELVGEVLRIM-QQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIE 231
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
1-229 |
4.34e-24 |
|
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: 96.35 E-value: 4.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTkPILELKDV-KT-TVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSG--FLLHNGH--DI 74
Cdd:COG4778 1 MT-TLLEVENLsKTfTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGsiLVRHDGGwvDL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 75 TKMSEE------KRT-----QFIgRVFqdpkmgtaPRMT----VAENLLlatKRGKRRFLKIRKLKQNLPRFkklaavmn 139
Cdd:COG4778 80 AQASPReilalrRRTigyvsQFL-RVI--------PRVSaldvVAEPLL---ERGVDREEARARARELLARL-------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 140 nGLENRL-----NTFveglSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSEnllAVTD--QQIKENKLTALMITHH 212
Cdd:COG4778 140 -NLPERLwdlppATF----SGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA---VVVEliEEAKARGTAIIGIFHD 211
|
250
....*....|....*..
gi 489745462 213 MEDALKYGNRLLVLKDG 229
Cdd:COG4778 212 EEVREAVADRVVDVTPF 228
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
19-239 |
5.58e-24 |
|
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: 96.15 E-value: 5.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 19 DGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTA 98
Cdd:cd03251 11 PGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLFND 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 prmTVAENLLLAtKRGKRRFLKIRKLKQ-NLPRFkklaaVMNngLENRLNTFVE----GLSGGQRQALSFLMATIERPDI 173
Cdd:cd03251 91 ---TVAENIAYG-RPGATREEVEEAARAaNAHEF-----IME--LPEGYDTVIGergvKLSGGQRQRIAIARALLKDPPI 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 174 LLLDEHTAALDpHTSENLLAVTDQQIKENKlTALMITHHM---EDAlkygNRLLVLKDGKVKADINEQE 239
Cdd:cd03251 160 LILDEATSALD-TESERLVQAALERLMKNR-TTFVIAHRLstiENA----DRIVVLEDGKIVERGTHEE 222
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
23-233 |
8.37e-24 |
|
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: 99.82 E-value: 8.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKM--Gtapr 100
Cdd:COG4618 345 RPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELfdG---- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 mTVAENllLAtkrgkrrflkirklkqnlpRFK-----------KLAAV--MNNGLENRLNTFVE----GLSGGQRQALSF 163
Cdd:COG4618 421 -TIAEN--IA-------------------RFGdadpekvvaaaKLAGVheMILRLPDGYDTRIGeggaRLSGGQRQRIGL 478
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 164 LMATIERPDILLLDEHTAALDpHTSENLLAVTDQQIKENKLTALMITHHMEdALKYGNRLLVLKDGKVKA 233
Cdd:COG4618 479 ARALYGDPRLVVLDEPNSNLD-DEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQA 546
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
6-231 |
1.23e-23 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 99.15 E-value: 1.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLrPDSGFLLHNGHDITKMSEEKRTQF 85
Cdd:PRK11174 350 IEAEDL--EILSPDGK--TLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKH 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMgtaPRMTVAENLLLATKRgkrrfLKIRKLKQNLPRFKklAAVMNNGLENRLNTFVE----GLSGGQRQAL 161
Cdd:PRK11174 425 LSWVGQNPQL---PHGTLRDNVLLGNPD-----ASDEQLQQALENAW--VSEFLPLLPQGLDTPIGdqaaGLSVGQAQRL 494
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 162 SFLMATIERPDILLLDEHTAALDPHtSENLLAVTDQQIKENKlTALMITHHMEDaLKYGNRLLVLKDGKV 231
Cdd:PRK11174 495 ALARALLQPCQLLLLDEPTASLDAH-SEQLVMQALNAASRRQ-TTLMVTHQLED-LAQWDQIWVMQDGQI 561
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
24-231 |
1.27e-23 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 95.46 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGH--DITKMSEEKRTQF----IGRVFQDPKMGt 97
Cdd:COG4161 16 QALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHqfDFSQKPSEKAIRLlrqkVGMVFQQYNLW- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 98 aPRMTVAENLLLATKRgkrrFLKIRKlKQNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLD 177
Cdd:COG4161 95 -PHLTVMENLIEAPCK----VLGLSK-EQAREKAMKLLARL--RLTDKADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 178 EHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:COG4161 167 EPTAALDPEITAQVVEII-RELSQTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
25-239 |
2.72e-23 |
|
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: 94.48 E-value: 2.72e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDpkmGTAPRMTVA 104
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQE---NVLFNRSIR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 105 ENLLLA-TKRGKRRFLKIRKLKQNLPRFKKLAavmnNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:cd03252 94 DNIALAdPGMSMERVIEAAKLAGAHDFISELP----EGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSAL 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 184 DpHTSENLLAVTDQQIKENKlTALMITHHMEdALKYGNRLLVLKDGKVKADINEQE 239
Cdd:cd03252 170 D-YESEHAIMRNMHDICAGR-TVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDE 222
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
1-231 |
3.00e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 94.18 E-value: 3.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVktadGEIvPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITK---- 76
Cdd:PRK11614 1 MEKVMLSFDKVSAHY----GKI-QALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqta 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 77 --MSE------EKRtqfigRVFQdpkmgtapRMTVAENLLLATKRGKRRFL--KIRKLKQNLPRfkklaavmnngLENRL 146
Cdd:PRK11614 76 kiMREavaivpEGR-----RVFS--------RMTVEENLAMGGFFAERDQFqeRIKWVYELFPR-----------LHERR 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 147 NTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAvTDQQIKENKLTALMITHHMEDALKYGNRLLVL 226
Cdd:PRK11614 132 IQRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFD-TIEQLREQGMTIFLVEQNANQALKLADRGYVL 210
|
....*
gi 489745462 227 KDGKV 231
Cdd:PRK11614 211 ENGHV 215
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
39-233 |
4.15e-23 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 96.10 E-value: 4.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 39 IT-IIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGH---DITK---MSEEKRTqfIGRVFQDPKMgtAPRMTVAENLLLAT 111
Cdd:PRK11144 26 ITaIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfDAEKgicLPPEKRR--IGYVFQDARL--FPHYKVRGNLRYGM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 112 KrgkrrflkirklKQNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALD-PHTSEn 190
Cdd:PRK11144 102 A------------KSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDlPRKRE- 166
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489745462 191 LLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:PRK11144 167 LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKA 209
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
4.65e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 94.43 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKtadGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:PRK13648 3 DKNSIIVFKNVSFQYQ---SDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQFIGRVFQDPK---MGTAPRMTVA---ENLLLATKRGKRRFLKirklkqnlprfkklaAVMNNGLENRLNTFVEGLS 154
Cdd:PRK13648 80 KLRKHIGIVFQNPDnqfVGSIVKYDVAfglENHAVPYDEMHRRVSE---------------ALKQVDMLERADYEPNALS 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 155 GGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKyGNRLLVLKDGKV 231
Cdd:PRK13648 145 GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
25-231 |
5.07e-23 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 95.92 E-value: 5.07e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfIGRVFQDPKMGTapRMTVA 104
Cdd:PRK10851 17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRK--VGFVFQHYALFR--HMTVF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 105 ENL---LLATKRGKRRFLKIrkLKQNLPRFkkLAAVMNNGLENRlntFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:PRK10851 93 DNIafgLTVLPRRERPNAAA--IKAKVTQL--LEMVQLAHLADR---YPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 182 ALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK10851 166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
2-233 |
5.44e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 94.41 E-value: 5.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 2 TKPILELKDVKTTVKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEK 81
Cdd:PRK13650 1 MSNIIEVKNLTFKYKEDQEK--YTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 82 RTQFIGRVFQDPK---MGTAPRMTVA---ENLLLATKRGKRRFLKirklkqnlprfkKLAAVmnnGLENRLNTFVEGLSG 155
Cdd:PRK13650 79 IRHKIGMVFQNPDnqfVGATVEDDVAfglENKGIPHEEMKERVNE------------ALELV---GMQDFKEREPARLSG 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 156 GQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAvTDQQIKE-NKLTALMITHHMeDALKYGNRLLVLKDGKVKA 233
Cdd:PRK13650 144 GQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIK-TIKGIRDdYQMTVISITHDL-DEVALSDRVLVMKNGQVES 220
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
5-232 |
6.96e-23 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 93.30 E-value: 6.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEIvPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ 84
Cdd:PRK10584 6 IVEVHHLKKSVGQGEHEL-SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 F----IGRVFQDPKMgtAPRMTVAENLLL-ATKRGKRRflkirklKQNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQRQ 159
Cdd:PRK10584 85 LrakhVGFVFQSFML--IPTLNALENVELpALLRGESS-------RQSRNGAKALLEQL--GLGKRLDHLPAQLSGGEQQ 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 160 ALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLvLKDGKVK 232
Cdd:PRK10584 154 RVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLR-LVNGQLQ 225
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-232 |
9.42e-23 |
|
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: 92.56 E-value: 9.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAprmTV 103
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQDPVLFSG---TI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENL-----------LLATKRgkrrfLKIRKLKQNLPrfKKLAAVMNNGLENrlntfvegLSGGQRQALSFLMATIERPD 172
Cdd:cd03244 95 RSNLdpfgeysdeelWQALER-----VGLKEFVESLP--GGLDTVVEEGGEN--------LSVGQRQLLCLARALLRKSK 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 173 ILLLDEHTAALDPHTSENLLAVTDQQIKENklTALMITHHMEDALKYgNRLLVLKDGKVK 232
Cdd:cd03244 160 ILVLDEATASVDPETDALIQKTIREAFKDC--TVLTIAHRLDTIIDS-DRILVLDKGRVV 216
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
2-231 |
9.89e-23 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 96.27 E-value: 9.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 2 TKPILELKDVKttvKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEK 81
Cdd:PRK15439 8 APPLLCARSIS---KQYSG--VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 82 RTQF-IGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRKLKQNLPRFKKLAavMNNG-LENRLNTFVEGLSGGQRQ 159
Cdd:PRK15439 83 AHQLgIYLVPQEPLL--FPNLSVKENILFGLPKRQASMQKMKQLLAALGCQLDLD--SSAGsLEVADRQIVEILRGLMRD 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 160 AlsflmatierpDILLLDEHTAALDPHTSENLLavtdQQIKEnkLTAL-----MITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK15439 159 S-----------RILILDEPTASLTPAETERLF----SRIRE--LLAQgvgivFISHKLPEIRQLADRISVMRDGTI 218
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
24-234 |
1.08e-22 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 93.26 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAprMTV 103
Cdd:COG4559 15 TLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLPQHSSLAFP--FTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLatkrGKRRFLKIRKLKQNLPRfKKLAAVMNNGLENRlntFVEGLSGGQRQ--ALSFLMATIERPD-----ILLL 176
Cdd:COG4559 93 EEVVAL----GRAPHGSSAAQDRQIVR-EALALVGLAHLAGR---SYQTLSGGEQQrvQLARVLAQLWEPVdggprWLFL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 177 DEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:COG4559 165 DEPTSALDLAHQHAVLRLA-RQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQ 221
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
25-216 |
1.13e-22 |
|
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 130234 [Multi-domain] Cd Length: 190 Bit Score: 91.72 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGH--DITKMSEEKRTQFIGRVFQDPK-------- 94
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGLVFQDPDdqlfaadv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 95 ---MGTAPRmtvaeNLLLATKRGKRRflkIRKlkqnlprfkKLAAVMNNGLENRLntfVEGLSGGQRQALSFLMATIERP 171
Cdd:TIGR01166 87 dqdVAFGPL-----NLGLSEAEVERR---VRE---------ALTAVGASGLRERP---THCLSGGEKKRVAIAGAVAMRP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489745462 172 DILLLDEHTAALDPHTSENLLAVTDqQIKENKLTALMITHHMEDA 216
Cdd:TIGR01166 147 DVLLLDEPTAGLDPAGREQMLAILR-RLRAEGMTVVISTHDVDLA 190
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
4-233 |
1.87e-22 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 94.91 E-value: 1.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVktTVKTADgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT 83
Cdd:PRK09536 2 PMIDVSDL--SVEFGD---TTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 QFIGRVFQDP------------KMGTAPRMTVAENLLLATKRGKRRflkirklkqnlprfkklaAVMNNGLENRLNTFVE 151
Cdd:PRK09536 77 RRVASVPQDTslsfefdvrqvvEMGRTPHRSRFDTWTETDRAAVER------------------AMERTGVAQFADRPVT 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 152 GLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK09536 139 SLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRV 217
|
..
gi 489745462 232 KA 233
Cdd:PRK09536 218 RA 219
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
1-230 |
2.29e-22 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 92.36 E-value: 2.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVktadGEIVPIlKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:PRK11300 1 MSQPLLSVSGLMMRF----GGLLAV-NNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGH 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQF-IGRVFQDPKMgtAPRMTVAENLLLATKRgkrrflkirKLKQNL-------PRFKK-------LAAVMNN--GLE 143
Cdd:PRK11300 76 QIARMgVVRTFQHVRL--FREMTVIENLLVAQHQ---------QLKTGLfsgllktPAFRRaesealdRAATWLErvGLL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 144 NRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRL 223
Cdd:PRK11300 145 EHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRI 224
|
....*..
gi 489745462 224 LVLKDGK 230
Cdd:PRK11300 225 YVVNQGT 231
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-230 |
2.31e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 93.33 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKttvKTADGEIVpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:PRK13537 3 MSVAPIDFRNVE---KRYGDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRtQFIGRVFQDPKMGtaPRMTVAENLLLATKRGKRRFLKIRKLKQNLPRFKKLaavmnnglENRLNTFVEGLSGGQRQA 160
Cdd:PRK13537 78 AR-QRVGVVPQFDNLD--PDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKL--------ENKADAKVGELSGGMKRR 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 161 LSFLMATIERPDILLLDEHTAALDPHtSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:PRK13537 147 LTLARALVNDPDVLVLDEPTTGLDPQ-ARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
5-231 |
2.31e-22 |
|
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: 91.56 E-value: 2.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPD---SGFLLHNGhditkmSEEK 81
Cdd:cd03234 3 VLPWWDVGLKAKNWNKY-ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNG------QPRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 82 RTQF---IGRVFQDPKmgTAPRMTVAENLL-LATKRGKRRFLKIRKlkqnlprfKKLAAVMnngLENRL------NTFVE 151
Cdd:cd03234 76 PDQFqkcVAYVRQDDI--LLPGLTVRETLTyTAILRLPRKSSDAIR--------KKRVEDV---LLRDLaltrigGNLVK 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 152 GLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03234 143 GISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
1-231 |
3.00e-22 |
|
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: 95.14 E-value: 3.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKS----TLLNTIAGSLRPDSGFLLHNGHDITK 76
Cdd:COG4172 2 MSMPLLSVEDLSVAFGQGGGT-VEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 77 MSEEK----RTQFIGRVFQDPkMgTA--PRMTV----AENLLL---ATKRGKRRflKIRKLkqnlprfkkLAAVmnnGL- 142
Cdd:COG4172 81 LSERElrriRGNRIAMIFQEP-M-TSlnPLHTIgkqiAEVLRLhrgLSGAAARA--RALEL---------LERV---GIp 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 143 --ENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDphtsenllaVTDQ-QI--------KENKLTALMITH 211
Cdd:COG4172 145 dpERRLDAYPHQLSGGQRQRVMIAMALANEPDLLIADEPTTALD---------VTVQaQIldllkdlqRELGMALLLITH 215
|
250 260
....*....|....*....|....*.
gi 489745462 212 ------HMEDalkygnRLLVLKDGKV 231
Cdd:COG4172 216 dlgvvrRFAD------RVAVMRQGEI 235
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
26-238 |
4.24e-22 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 91.09 E-value: 4.24e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEK----RTQfIGRVFQDPK--MGTAP 99
Cdd:PRK10908 18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflRRQ-IGMIFQDHHllMDRTV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 RMTVAENLLLATKRGKrrflKIRKlkqnlprfKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEH 179
Cdd:PRK10908 97 YDNVAIPLIIAGASGD----DIRR--------RVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEP 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 180 TAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADINEQ 238
Cdd:PRK10908 165 TGNLDDALSEGILRLF-EEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHGGVGGE 222
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
24-231 |
5.02e-22 |
|
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: 94.81 E-value: 5.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAprmTV 103
Cdd:TIGR01193 488 NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYLPQEPYIFSG---SI 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGkrrfLKIRKLKQ--NLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:TIGR01193 565 LENLLLGAKEN----VSQDEIWAacEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTS 640
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 182 ALDPHTS----ENLLAVTDQQIkenkltaLMITHHMEDAlKYGNRLLVLKDGKV 231
Cdd:TIGR01193 641 NLDTITEkkivNNLLNLQDKTI-------IFVAHRLSVA-KQSDKIIVLDHGKI 686
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
24-238 |
5.92e-22 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 92.97 E-value: 5.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQfIGRVFQDPKMGtaPRMTV 103
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVPQFDNLD--LEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLAtkrGKRRFLKIRKLKQNLPRFKKLAAvmnngLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:PRK13536 132 RENLLVF---GRYFGMSTREIEAVIPSLLEFAR-----LESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGL 203
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 184 DPHtSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLK------DGKVKADINEQ 238
Cdd:PRK13536 204 DPH-ARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEagrkiaEGRPHALIDEH 263
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
25-231 |
6.28e-22 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 90.84 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGH--DITKMSEEKRT----QFIGRVFQDPKMGta 98
Cdd:PRK11124 17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSDKAIrelrRNVGMVFQQYNLW-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 PRMTVAENLLLATKRgkrrFLKIRKlKQNLPRFKKLAAVMnnglenRLNTFVEG----LSGGQRQALSFLMATIERPDIL 174
Cdd:PRK11124 95 PHLTVQQNLIEAPCR----VLGLSK-DQALARAEKLLERL------RLKPYADRfplhLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 175 LLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSII-RELAETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
1-211 |
6.46e-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: 6.46e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVK--------------TTVKTADGeivpilkgIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGF 66
Cdd:COG4608 3 MAEPLLEVRDLKkhfpvrgglfgrtvGVVKAVDG--------VSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 67 LLHNGHDITKMSEEKRTQFigR-----VFQDPKMGTAPRMTV----AENLL---LATKRGKRRflKIRKLkqnlprfkkL 134
Cdd:COG4608 75 ILFDGQDITGLSGRELRPL--RrrmqmVFQDPYASLNPRMTVgdiiAEPLRihgLASKAERRE--RVAEL---------L 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 135 AAVmnnGL-ENRLNTFVEGLSGGQRQ------ALSFlmatieRPDILLLDEHTAALDphTS-----ENLLAvtDQQiKEN 202
Cdd:COG4608 142 ELV---GLrPEHADRYPHEFSGGQRQrigiarALAL------NPKLIVCDEPVSALD--VSiqaqvLNLLE--DLQ-DEL 207
|
....*....
gi 489745462 203 KLTALMITH 211
Cdd:COG4608 208 GLTYLFISH 216
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
1-231 |
7.33e-22 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 92.48 E-value: 7.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDV-----KTTVktadgeivpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDIT 75
Cdd:PRK11432 2 TQKNFVVLKNItkrfgSNTV----------IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 76 KMSEEKRTqfIGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRKlkqnlpRFKK-LAAVMNNGLENRlntFVEGLS 154
Cdd:PRK11432 72 HRSIQQRD--ICMVFQSYAL--FPHMSLGENVGYGLKMLGVPKEERKQ------RVKEaLELVDLAGFEDR---YVDQIS 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 155 GGQRQALSFLMATIERPDILLLDEHTAALDPhtseNLLAVTDQQIKENK----LTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:PRK11432 139 GGQQQRVALARALILKPKVLLFDEPLSNLDA----NLRRSMREKIRELQqqfnITSLYVTHDQSEAFAVSDTVIVMNKGK 214
|
.
gi 489745462 231 V 231
Cdd:PRK11432 215 I 215
|
|
| type_I_sec_PrtD |
TIGR01842 |
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ... |
24-233 |
7.53e-22 |
|
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: 93.95 E-value: 7.53e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAprmTV 103
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPG---TV 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENlllatkrgkrrflkIRKLKQNLPRFK-----KLAAV--MNNGLENRLNTFV----EGLSGGQRQALSFLMATIERPD 172
Cdd:TIGR01842 409 AEN--------------IARFGENADPEKiieaaKLAGVheLILRLPDGYDTVIgpggATLSGGQRQRIALARALYGDPK 474
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 173 ILLLDEHTAALDpHTSENLLAVTDQQIKENKLTALMITHHMEdALKYGNRLLVLKDGKVKA 233
Cdd:TIGR01842 475 LVVLDEPNSNLD-EEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIAR 533
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
6-231 |
9.03e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 89.15 E-value: 9.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTADGEIV-PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRP--DSGFLLHNGHDITKMSEEKR 82
Cdd:cd03213 4 LSFRNLTVTVKSSPSKSGkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKRSFRKI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 tqfIGRVFQDPKmgTAPRMTVAENLLLAtkrgkrrfLKIRklkqnlprfkklaavmnnglenrlntfveGLSGGQRQALS 162
Cdd:cd03213 84 ---IGYVPQDDI--LHPTLTVRETLMFA--------AKLR-----------------------------GLSGGERKRVS 121
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 163 FLMATIERPDILLLDEHTAALDPHTSENLLaVTDQQIKENKLTALMITH-------HMEDalkygnRLLVLKDGKV 231
Cdd:cd03213 122 IALELVSNPSLLFLDEPTSGLDSSSALQVM-SLLRRLADTGRTIICSIHqpsseifELFD------KLLLLSQGRV 190
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
25-234 |
1.46e-21 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 90.43 E-value: 1.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDpkmGTAP-RMTV 103
Cdd:PRK10253 22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQN---ATTPgDITV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AEnlLLATKRGKRRFLKIRKLKQNLPRFKKlaAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:PRK10253 99 QE--LVARGRYPHQPLFTRWRKEDEEAVTK--AMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489745462 184 DPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:PRK10253 175 DISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQ 225
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-232 |
1.66e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 1.66e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKttvKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHnGHDITkmseekr 82
Cdd:COG0488 313 KKVLELEGLS---KSYGDK--TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK------- 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 tqfIGRVFQDPKmGTAPRMTVAENLLLATKRGKRRFlkIRKLkqnlprfkkLAAVMNNGleNRLNTFVEGLSGGQRQALS 162
Cdd:COG0488 380 ---IGYFDQHQE-ELDPDKTVLDELRDGAPGGTEQE--VRGY---------LGRFLFSG--DDAFKPVGVLSGGEKARLA 442
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 163 FLMATIERPDILLLDEHTAALDPHTSENLlavtdqqikENKL-----TALMITHHME--DALkyGNRLLVLKDGKVK 232
Cdd:COG0488 443 LAKLLLSPPNVLLLDEPTNHLDIETLEAL---------EEALddfpgTVLLVSHDRYflDRV--ATRILEFEDGGVR 508
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
6-231 |
1.92e-21 |
|
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: 88.74 E-value: 1.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADGEIvpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAG--SLRPDSGFLLHNGHDITKMSEEKRT 83
Cdd:cd03217 1 LEIKDL--HVSVGGKEI---LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 QF-IGRVFQDPKmgTAPRMTVAENLllatkrgkrRFLKirklkqnlprfkklaavmnnglenrlntfvEGLSGGQRQALS 162
Cdd:cd03217 76 RLgIFLAFQYPP--EIPGVKNADFL---------RYVN------------------------------EGFSGGEKKRNE 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 163 FLMATIERPDILLLDEHTAALDphtSENLLAVTDQ--QIKENKLTALMITHHmEDALKY--GNRLLVLKDGKV 231
Cdd:cd03217 115 ILQLLLLEPDLAILDEPDSGLD---IDALRLVAEVinKLREEGKSVLIITHY-QRLLDYikPDRVHVLYDGRI 183
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-231 |
3.98e-21 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 91.95 E-value: 3.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPkmGTAPRmTV 103
Cdd:PRK13657 349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA--GLFNR-SI 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLL----ATKRGKRRFLKirklkqnlpRFKKLAAVMNNglENRLNTFV----EGLSGGQRQALSFLMATIERPDILL 175
Cdd:PRK13657 426 EDNIRVgrpdATDEEMRAAAE---------RAQAHDFIERK--PDGYDTVVgergRQLSGGERQRLAIARALLKDPPILI 494
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 176 LDEHTAALDPHTSENLLAVTDqQIKENKlTALMITHHMEdALKYGNRLLVLKDGKV 231
Cdd:PRK13657 495 LDEATSALDVETEAKVKAALD-ELMKGR-TTFIIAHRLS-TVRNADRILVFDNGRV 547
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
24-233 |
5.12e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.89 E-value: 5.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPK---MGTapr 100
Cdd:PRK13632 23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQNPDnqfIGA--- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 mTVAENLL--LATKRGKRRflKIRKLkqnlprFKKLAAVMnnGLENRLNTFVEGLSGGQRQ--ALSFLMATieRPDILLL 176
Cdd:PRK13632 100 -TVEDDIAfgLENKKVPPK--KMKDI------IDDLAKKV--GMEDYLDKEPQNLSGGQKQrvAIASVLAL--NPEIIIF 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 177 DEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKyGNRLLVLKDGKVKA 233
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLIA 222
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
24-231 |
5.90e-21 |
|
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: 88.71 E-value: 5.90e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF---IGRVFQDPKMGTAPR 100
Cdd:TIGR02769 25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrrdVQLVFQDSPSAVNPR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAENLllatKRGKRRFLKIRKLKQnLPRFKKLAAVMnnGLENR-LNTFVEGLSGGQRQALSFLMATIERPDILLLDEH 179
Cdd:TIGR02769 105 MTVRQII----GEPLRHLTSLDESEQ-KARIAELLDMV--GLRSEdADKLPRQLSGGQLQRINIARALAVKPKLIVLDEA 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489745462 180 TAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:TIGR02769 178 VSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
23-231 |
6.23e-21 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 88.43 E-value: 6.23e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAG--SLRPD---SGFLLHNGHDITKMSEEKRTQFIGRVFQDPKmgT 97
Cdd:PRK14247 16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEarvSGEVYLDGQDIFKMDVIELRRRVQMVFQIPN--P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 98 APRMTVAENLLLATKRGkrRFLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLD 177
Cdd:PRK14247 94 IPNLSIFENVALGLKLN--RLVKSKKELQERVRWALEKAQLWDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 178 EHTAALDPHTSENLLAVTDQQIKEnkLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
26-231 |
6.50e-21 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 90.48 E-value: 6.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSE----EKRTQFIGRVFQdpKMGTAPRM 101
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrEVRRKKIAMVFQ--SFALMPHM 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLAtkrgkrrfLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:PRK10070 122 TVLDNTAFG--------MELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFS 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 182 ALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK10070 194 ALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-239 |
6.51e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 88.99 E-value: 6.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 15 VKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDitkMSEEKRTQFI----GRVF 90
Cdd:PRK13633 15 ESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD---TSDEENLWDIrnkaGMVF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 91 QDPK---MGTAPRMTVA---ENLLLATKRGKRRFLKIRKlKQNLPRFKKLAAVMnnglenrlntfvegLSGGQRQALSFL 164
Cdd:PRK13633 92 QNPDnqiVATIVEEDVAfgpENLGIPPEEIRERVDESLK-KVGMYEYRRHAPHL--------------LSGGQKQRVAIA 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 165 MATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKyGNRLLVLKDGKVKADINEQE 239
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKE 230
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
1-240 |
9.69e-21 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 89.89 E-value: 9.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVkttVKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:PRK11607 15 ALTPLLEIRNL---TKSFDGQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPY 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTqfIGRVFQDPKMgtAPRMTVAENLLLATKRGKRRFLKIRKLKQNLprfkkLAAVMNNGLENRLNtfvEGLSGGQRQA 160
Cdd:PRK11607 90 QRP--INMMFQSYAL--FPHMTVEQNIAFGLKQDKLPKAEIASRVNEM-----LGLVHMQEFAKRKP---HQLSGGQRQR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 161 LSFLMATIERPDILLLDEHTAALDPHTSENL-LAVTDqqIKEN-KLTALMITHHMEDALKYGNRLLVLKDGKVkADINEQ 238
Cdd:PRK11607 158 VALARSLAKRPKLLLLDEPMGALDKKLRDRMqLEVVD--ILERvGVTCVMVTHDQEEAMTMAGRIAIMNRGKF-VQIGEP 234
|
..
gi 489745462 239 EK 240
Cdd:PRK11607 235 EE 236
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
1-231 |
1.31e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 88.37 E-value: 1.31e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVktTVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGH--DITKMS 78
Cdd:PRK13636 1 MEDYILKVEEL--NYNYSDG--THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 79 EEKRTQFIGRVFQDP--KMGTAprmTVAENLLLATKRGKRRFLKIRKLKQNlprfkklaAVMNNGLENRLNTFVEGLSGG 156
Cdd:PRK13636 77 LMKLRESVGMVFQDPdnQLFSA---SVYQDVSFGAVNLKLPEDEVRKRVDN--------ALKRTGIEHLKDKPTHCLSFG 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 157 QRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK13636 146 QKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRV 220
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
24-229 |
1.52e-20 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 87.45 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKrtqfiGRVFQDPkmGTAPRMTV 103
Cdd:PRK11248 15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER-----GVVFQNE--GLLPWRNV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENL-----LLATKRGKRRFLKIRKLKQnlprfkklaavmnNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:PRK11248 88 QDNVafglqLAGVEKMQRLEIAHQMLKK-------------VGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489745462 179 HTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDG 229
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
1-229 |
4.15e-20 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 86.37 E-value: 4.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKD--VKTTVKTAdgeivpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTI--AGSLRPD---SGFLLHNGHD 73
Cdd:PRK14239 1 MTEPILQVSDlsVYYNKKKA-------LNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEvtiTGSIVYNGHN 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 74 I---TKMSEEKRTQfIGRVFQDPKmgTAPrMTVAEN----LLLATKRGKRRflkirkLKQNLPRFKKLAAVMNNgLENRL 146
Cdd:PRK14239 74 IyspRTDTVDLRKE-IGMVFQQPN--PFP-MSIYENvvygLRLKGIKDKQV------LDEAVEKSLKGASIWDE-VKDRL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 147 NTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTS----ENLLAVTDqqikenKLTALMITHHMEDALKYGNR 222
Cdd:PRK14239 143 HDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDPISAgkieETLLGLKD------DYTMLLVTRSMQQASRISDR 216
|
....*..
gi 489745462 223 LLVLKDG 229
Cdd:PRK14239 217 TGFFLDG 223
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
5-253 |
4.66e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 86.67 E-value: 4.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKtaDGEIVpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDIT--KMSEEKR 82
Cdd:PRK13639 1 ILETRDLKYSYP--DGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKydKKSLLEV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 TQFIGRVFQDPKMGT-APrmTVAE-------NLLLATKRGKRRFLkirklkqnlprfKKLAAVMNNGLENRLNtfvEGLS 154
Cdd:PRK13639 77 RKTVGIVFQNPDDQLfAP--TVEEdvafgplNLGLSKEEVEKRVK------------EALKAVGMEGFENKPP---HHLS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 155 GGQ--RQALSFLMATieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENkLTALMITHHMEDALKYGNRLLVLKDGK-- 230
Cdd:PRK13639 140 GGQkkRVAIAGILAM--KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKii 216
|
250 260 270
....*....|....*....|....*....|
gi 489745462 231 -------VKADINEQEKQNLKVSDLYKYFE 253
Cdd:PRK13639 217 kegtpkeVFSDIETIRKANLRLPRVAHLIE 246
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
24-231 |
4.71e-20 |
|
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: 85.74 E-value: 4.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAprmTV 103
Cdd:cd03253 15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQDTVLFND---TI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENL----LLATKRGKRRFLKIRKLK---QNLPrFKKLAAVMNNGLEnrlntfvegLSGGQRQALSFLMATIERPDILLL 176
Cdd:cd03253 92 GYNIrygrPDATDEEVIEAAKAAQIHdkiMRFP-DGYDTIVGERGLK---------LSGGEKQRVAIARAILKNPPILLL 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 177 DEHTAALDPHTSENLLAVTDQQIKeNKlTALMITHHME---DALKygnrLLVLKDGKV 231
Cdd:cd03253 162 DEATSALDTHTEREIQAALRDVSK-GR-TTIVIAHRLStivNADK----IIVLKDGRI 213
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
26-250 |
4.91e-20 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 86.22 E-value: 4.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHN---GHDITKMSE-----EKRTQFIGRVFQdpKMGT 97
Cdd:PRK09984 20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIellGRTVQREGRlardiRKSRANTGYIFQ--QFNL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 98 APRMTVAENLLLATkRGKRRFLKI------RKLKQnlprfKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERP 171
Cdd:PRK09984 98 VNRLSVLENVLIGA-LGSTPFWRTcfswftREQKQ-----RALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 172 DILLLDEHTAALDPHtSENLLAVTDQQIKENK-LTALMITHHMEDALKYGNRLLVLKDGKVKADINEQEKQNLKVSDLYK 250
Cdd:PRK09984 172 KVILADEPIASLDPE-SARIVMDTLRDINQNDgITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQFDNERFDHLYR 250
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
1-233 |
8.08e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 86.01 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTADgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDS---GFLLHNGHDITKM 77
Cdd:PRK13640 1 MKDNIVEFKHVSFTYPDSK---KPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 78 SEEKRTQFIGRVFQDPK---MGTAPRMTVAENLllaTKRGKRRfLKIRKLKQNLprfkkLAAVmnnGLENRLNTFVEGLS 154
Cdd:PRK13640 78 TVWDIREKVGIVFQNPDnqfVGATVGDDVAFGL---ENRAVPR-PEMIKIVRDV-----LADV---GMLDYIDSEPANLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 155 GGQRQ--ALSFLMATieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDAlKYGNRLLVLKDGKVK 232
Cdd:PRK13640 146 GGQKQrvAIAGILAV--EPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
|
.
gi 489745462 233 A 233
Cdd:PRK13640 223 A 223
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
24-212 |
8.89e-20 |
|
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: 83.95 E-value: 8.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEkRTQFIGRVFQDPkmGTAPRMTV 103
Cdd:TIGR01189 14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLGHLP--GLKPELSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLllatkrgkrRFL-KIRKLKQNLPrFKKLAAVMNNGLENRLntfVEGLSGGQRQALSFLMATIERPDILLLDEHTAA 182
Cdd:TIGR01189 91 LENL---------HFWaAIHGGAQRTI-EDALAAVGLTGFEDLP---AAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180 190
....*....|....*....|....*....|
gi 489745462 183 LDPHTSENLLAVTDQQIKENKLtALMITHH 212
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGI-VLLTTHQ 186
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-231 |
8.92e-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: 87.94 E-value: 8.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFL-LHNGHDITKMSEE- 80
Cdd:TIGR03269 277 EPIIKVRNVSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnVRVGDEWVDMTKPg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 -----KRTQFIGRVFQDpkMGTAPRMTVAENLLLATKRGKRRFLKIRKLKQNLprfkKLAAVMNNGLENRLNTFVEGLSG 155
Cdd:TIGR03269 357 pdgrgRAKRYIGILHQE--YDLYPHRTVLDNLTEAIGLELPDELARMKAVITL----KMVGFDEEKAEEILDKYPDELSE 430
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 156 GQRQALSFLMATIERPDILLLDEHTAALDPHTSenlLAVTDQQIK---ENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITK---VDVTHSILKareEMEQTFIIVSHDMDFVLDVCDRAALMRDGKI 506
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
24-231 |
9.21e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.95 E-value: 9.21e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFI----GRVFQDPKmgtap 99
Cdd:PRK13649 21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKDIKQIrkkvGLVFQFPE----- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 RMTVAENLLLATKRGKRRFLKIRKLKQNLPRfKKLAAVmnnGLENRL---NTFveGLSGGQ--RQALSFLMATieRPDIL 174
Cdd:PRK13649 96 SQLFEETVLKDVAFGPQNFGVSQEEAEALAR-EKLALV---GISESLfekNPF--ELSGGQmrRVAIAGILAM--EPKIL 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 175 LLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK13649 168 VLDEPTAGLDPKGRKELMTLF-KKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKL 223
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
23-231 |
1.08e-19 |
|
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: 87.85 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAprmT 102
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVALVSQDVVLFND---T 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATKRGKRRfLKIRKLKQ--NLPRFKklaavmnNGLENRLNTFV----EGLSGGQRQALSFLMATIERPDILLL 176
Cdd:TIGR02203 422 IANNIAYGRTEQADR-AEIERALAaaYAQDFV-------DKLPLGLDTPIgengVLLSGGQRQRLAIARALLKDAPILIL 493
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 177 DEHTAALDpHTSENLLAVTDQQIKENKlTALMITHHMEdALKYGNRLLVLKDGKV 231
Cdd:TIGR02203 494 DEATSALD-NESERLVQAALERLMQGR-TTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
3-226 |
1.47e-19 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 85.91 E-value: 1.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKTTVKTADGEIVP-----ILK---GIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDI 74
Cdd:PRK15079 6 KVLLEVADLKVHFDIKDGKQWFwqppkTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 75 TKMSEEKRTQF---IGRVFQDPKMGTAPRMTVAEnlLLATKrgkrrfLKIR--KLKQNLPRFKKLAAVMNNGL-ENRLNT 148
Cdd:PRK15079 86 LGMKDDEWRAVrsdIQMIFQDPLASLNPRMTIGE--IIAEP------LRTYhpKLSRQEVKDRVKAMMLKVGLlPNLINR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 149 FVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSE---NLLavtdQQI-KENKLTALMITH------HMEDalk 218
Cdd:PRK15079 158 YPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAqvvNLL----QQLqREMGLSLIFIAHdlavvkHISD--- 230
|
....*...
gi 489745462 219 ygnRLLVL 226
Cdd:PRK15079 231 ---RVLVM 235
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
25-231 |
1.49e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.85 E-value: 1.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDIT--------------KMSEEKRTQfIGRVF 90
Cdd:COG4598 23 VLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelvpadrRQLQRIRTR-LGMVF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 91 QDpkMGTAPRMTVAENLLLAtkrgKRRFLKIRKlKQNLPRFKK-LAAVmnnGLENRLNTFVEGLSGGQRQalsflMATIE 169
Cdd:COG4598 102 QS--FNLWSHMTVLENVIEA----PVHVLGRPK-AEAIERAEAlLAKV---GLADKRDAYPAHLSGGQQQ-----RAAIA 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 170 R-----PDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:COG4598 167 RalamePEVMLFDEPTSALDPELVGEVLKVM-RDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-229 |
1.65e-19 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.15 E-value: 1.65e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKttvKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:PRK09700 1 MATPYISMAGIG---KSFGP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQF-IGRVFQDpkMGTAPRMTVAENLLLAtKRGKRRFLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQ 159
Cdd:PRK09700 76 LAAQLgIGIIYQE--LSVIDELTVLENLYIG-RHLTKKVCGVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 160 ALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDG 229
Cdd:PRK09700 153 MLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDG 221
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-232 |
1.72e-19 |
|
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: 83.62 E-value: 1.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPK--MGTaprm 101
Cdd:cd03369 22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTlfSGT---- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 tvaenlllatkrgkrrflkirkLKQNLPRFKKL-------AAVMNNGLENrlntfvegLSGGQRQALSFLMATIERPDIL 174
Cdd:cd03369 98 ----------------------IRSNLDPFDEYsdeeiygALRVSEGGLN--------LSQGQRQLLCLARALLKRPRVL 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 175 LLDEHTAALDPHTSenllAVTDQQIKE--NKLTALMITHHMEDALKYgNRLLVLKDGKVK 232
Cdd:cd03369 148 VLDEATASIDYATD----ALIQKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEVK 202
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
3-231 |
2.12e-19 |
|
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: 86.66 E-value: 2.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKTTVKTADG------EIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGsLRPDSGFLLHNGHDITK 76
Cdd:COG4172 273 PPLLEARDLKVWFPIKRGlfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDG 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 77 MSEEKRTQFigR-----VFQDPkMGT-APRMTV----AENLLL----ATKRGKRRflKIRKLkqnlprfkkLAAVmnnGL 142
Cdd:COG4172 352 LSRRALRPL--RrrmqvVFQDP-FGSlSPRMTVgqiiAEGLRVhgpgLSAAERRA--RVAEA---------LEEV---GL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 143 -ENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDphtsenllaVTDQ-QI--------KENKLTALMITHH 212
Cdd:COG4172 415 dPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD---------VSVQaQIldllrdlqREHGLAYLFISHD 485
|
250 260
....*....|....*....|.
gi 489745462 213 ME--DALkyGNRLLVLKDGKV 231
Cdd:COG4172 486 LAvvRAL--AHRVMVMKDGKV 504
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
1-211 |
2.20e-19 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 85.55 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTADGeIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPD---SGFLLHNGHDITKM 77
Cdd:PRK09473 8 QADALLDVKDLRVTFSTPDG-DVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANgriGGSATFNGREILNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 78 SEEK----RTQFIGRVFQDPKMGTAPRMTVAENLLLATKRGKRrflkIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGL 153
Cdd:PRK09473 87 PEKElnklRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKG----MSKAEAFEESVRMLDAVKMPEARKRMKMYPHEF 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 154 SGGQRQALSFLMATIERPDILLLDEHTAALDphtsenllaVTDQ-QIKE--NKL-----TA-LMITH 211
Cdd:PRK09473 163 SGGMRQRVMIAMALLCRPKLLIADEPTTALD---------VTVQaQIMTllNELkrefnTAiIMITH 220
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
26-231 |
3.11e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 84.45 E-value: 3.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT----QFIGRVFQDPkmgtaprm 101
Cdd:PRK13646 23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYIrpvrKRIGMVFQFP-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 tvaENLLLATKRGKRRFLKIRKLKQNLPRFKKLA--AVMNNGLE-NRLNTFVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:PRK13646 95 ---ESQLFEDTVEREIIFGPKNFKMNLDEVKNYAhrLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDE 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 179 HTAALDPHTSENLLAVTDQ-QIKENKlTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK13646 172 PTAGLDPQSKRQVMRLLKSlQTDENK-TIILVSHDMNEVARYADEVIVMKEGSI 224
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
21-234 |
3.80e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 84.75 E-value: 3.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 21 EIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKmseeKRTQF---IGRVF------- 90
Cdd:COG4586 33 REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFK----RRKEFarrIGVVFgqrsqlw 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 91 QDpkmgtaprMTVAENLLLatkrgKRRFLKI--RKLKQNLprfKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATI 168
Cdd:COG4586 109 WD--------LPAIDSFRL-----LKAIYRIpdAEYKKRL---DELVELL--DLGELLDTPVRQLSLGQRMRCELAAALL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 169 ERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:COG4586 171 HRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYD 236
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
26-233 |
4.02e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 84.30 E-value: 4.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKR----TQFIGRVFQDPKMGTAPRm 101
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKNKKlkplRKKVGIVFQFPEHQLFEE- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLatkrGKRRF-LKIRKLKQnlpRFKKLAAVMnnGLENRLNT---FveGLSGGQ--RQALSFLMATieRPDILL 175
Cdd:PRK13634 102 TVEKDICF----GPMNFgVSEEDAKQ---KAREMIELV--GLPEELLArspF--ELSGGQmrRVAIAGVLAM--EPEVLV 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 176 LDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:PRK13634 169 LDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFL 226
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
24-234 |
5.18e-19 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 83.14 E-value: 5.18e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVfqdPKMGTAPR-MT 102
Cdd:PRK11231 16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALL---PQHHLTPEgIT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAEnlLLATKRGKRrflkirklkqnLPRFKKLA---------AVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDI 173
Cdd:PRK11231 93 VRE--LVAYGRSPW-----------LSLWGRLSaednarvnqAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 174 LLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:PRK11231 160 VLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQ 219
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
2-231 |
7.21e-19 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 85.26 E-value: 7.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 2 TKPILELKDVKTTVktaDGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEK 81
Cdd:PRK11160 335 DQVSLTLNNVSFTY---PDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAA 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 82 RTQFIGRVFQDPKMGTAprmTVAENLLLAtkrgkrrflkirklkQNLPRFKKLAAVMNN-GLEN------RLNTFV-EG- 152
Cdd:PRK11160 412 LRQAISVVSQRVHLFSA---TLRDNLLLA---------------APNASDEALIEVLQQvGLEKlleddkGLNAWLgEGg 473
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 153 --LSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKlTALMITHHMEdALKYGNRLLVLKDGK 230
Cdd:PRK11160 474 rqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL-AEHAQNK-TVLMITHRLT-GLEQFDRICVMDNGQ 550
|
.
gi 489745462 231 V 231
Cdd:PRK11160 551 I 551
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
5-234 |
8.37e-19 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 83.23 E-value: 8.37e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITK-------- 76
Cdd:COG4152 1 MLELKGL---TKRFGD--KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPedrrrigy 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 77 MSEEKrtqfigrvfqdpkmGTAPRMTVAENLL-LATKRGkrrfLKIRKLKQNLPR-FKKLaavmnnGLENRLNTFVEGLS 154
Cdd:COG4152 76 LPEER--------------GLYPKMKVGEQLVyLARLKG----LSKAEAKRRADEwLERL------GLGDRANKKVEELS 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 155 GGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:COG4152 132 KGNQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAKGT-TVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
24-233 |
1.32e-18 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 82.00 E-value: 1.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF-IG------RVFQdpkmg 96
Cdd:COG1137 17 TVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARLgIGylpqeaSIFR----- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 97 tapRMTVAENLLLatkrgkrrFLKIRKL--KQnlpRFKKLAAVMNN-GLENRLNTFVEGLSGGQRQALSFLMATIERPDI 173
Cdd:COG1137 92 ---KLTVEDNILA--------VLELRKLskKE---REERLEELLEEfGITHLRKSKAYSLSGGERRRVEIARALATNPKF 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 174 LLLDEHTAALDPhtsenlLAVTD-QQI----KENKLTALmIT-HHMEDALKYGNRLLVLKDGKVKA 233
Cdd:COG1137 158 ILLDEPFAGVDP------IAVADiQKIirhlKERGIGVL-ITdHNVRETLGICDRAYIISEGKVLA 216
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
26-234 |
1.73e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.83 E-value: 1.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSG---FLLHNGHDITKMSEE---------KRTQF-------- 85
Cdd:PRK13651 23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGtieWIFKDEKNKKKTKEKekvleklviQKTRFkkikkike 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 ----IGRVFQdpkmgtaprmtVAENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAVMNN--GL-ENRLNTFVEGLSGGQ- 157
Cdd:PRK13651 103 irrrVGVVFQ-----------FAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIElvGLdESYLQRSPFELSGGQk 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 158 -RQALSFLMATieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:PRK13651 172 rRVALAGILAM--EPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKD 246
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
25-235 |
3.13e-18 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 80.63 E-value: 3.13e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSE----EKRTQFIGRVFQDPKMgtAPR 100
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSaakaELRNQKLGFIYQFHHL--LPD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAENLLLATKRGKRRFLKIRKLKQNLprfkkLAAVmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEINSRALEM-----LAAV---GLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPT 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 181 AALDPHTSENLLAVTDQQIKENKLTALMITHHMEDAlKYGNRLLVLKDGKVKADI 235
Cdd:PRK11629 174 GNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA-KRMSRQLEMRDGRLTAEL 227
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
24-211 |
9.59e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 9.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfllhnghDITKMSEEKrtqfIGRVFQDPKMGtaPRMTV 103
Cdd:COG0488 12 PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSG-------EVSIPKGLR----IGYLPQEPPLD--DDLTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGKRRFLKIRKLKQNLP-------RFKKLAAVMN--NG--LENRLNTFVEGL--------------SGGQR 158
Cdd:COG0488 79 LDTVLDGDAELRALEAELEELEAKLAepdedleRLAELQEEFEalGGweAEARAEEILSGLgfpeedldrpvselSGGWR 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489745462 159 ------QALsflmatIERPDILLLDEHTAALDPHTS---ENLLavtdqqiKENKLTALMITH 211
Cdd:COG0488 159 rrvalaRAL------LSEPDLLLLDEPTNHLDLESIewlEEFL-------KNYPGTVLVVSH 207
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
24-194 |
1.91e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 77.99 E-value: 1.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGrvfqdPKMGTAPRMTV 103
Cdd:PRK13539 16 VLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG-----HRNAMKPALTV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLL-ATKRGKRRfLKIRklkqnlprfKKLAAVmnnGLENRLNTFVEGLSGGQ--RQALSFLMATiERPdILLLDEHT 180
Cdd:PRK13539 91 AENLEFwAAFLGGEE-LDIA---------AALEAV---GLAPLAHLPFGYLSAGQkrRVALARLLVS-NRP-IWILDEPT 155
|
170
....*....|....
gi 489745462 181 AALDPHTSENLLAV 194
Cdd:PRK13539 156 AALDAAAVALFAEL 169
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
11-231 |
2.03e-17 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 81.60 E-value: 2.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 11 VKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQfigrvf 90
Cdd:TIGR01257 931 VKNLVKIFEPSGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQS------ 1004
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 91 qdpkMGTAPR-------MTVAENLLLatkrgkrrFLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSF 163
Cdd:TIGR01257 1005 ----LGMCPQhnilfhhLTVAEHILF--------YAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSV 1072
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 164 LMATIERPDILLLDEHTAALDPHTSEnllAVTDQQIK-ENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:TIGR01257 1073 AIAFVGDAKVVVLDEPTSGVDPYSRR---SIWDLLLKyRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
1-231 |
2.15e-17 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 78.92 E-value: 2.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTadgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAG--SLRPDSGFLLHNGHDITKMS 78
Cdd:CHL00131 3 KNKPILEIKNLHASVNE-----NEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 79 EEKRTQ---FIGrvFQDPKmgTAPRMTVAENLLLATKrGKRRFlkirklkQNLPRF----------KKLAAV-MNNGLEN 144
Cdd:CHL00131 78 PEERAHlgiFLA--FQYPI--EIPGVSNADFLRLAYN-SKRKF-------QGLPELdplefleiinEKLKLVgMDPSFLS 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 145 R-LNtfvEGLSGGQRQALSFLMATIERPDILLLDEHTAALD------PHTSENLLAVTDQQIkenkltaLMITHHmedal 217
Cdd:CHL00131 146 RnVN---EGFSGGEKKRNEILQMALLDSELAILDETDSGLDidalkiIAEGINKLMTSENSI-------ILITHY----- 210
|
250 260
....*....|....*....|...
gi 489745462 218 kygNRLL---------VLKDGKV 231
Cdd:CHL00131 211 ---QRLLdyikpdyvhVMQNGKI 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
6-231 |
2.36e-17 |
|
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.
Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 77.64 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTadgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqf 85
Cdd:cd03268 1 LKTNDLTKTYGK-----KRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRR-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPkmGTAPRMTVAENLLLatkrgKRRFLKIRKLKQNlprfKKLAAVmnnGLENRLNTFVEGLSGGQRQALSFLM 165
Cdd:cd03268 74 IGALIEAP--GFYPNLTARENLRL-----LARLLGIRKKRID----EVLDVV---GLKDSAKKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 166 ATIERPDILLLDEHTAALDP---HTSENLLavtdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDPdgiKELRELI----LSLRDQGITVLISSHLLSEIQKVADRIGIINKGKL 204
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
23-231 |
2.89e-17 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 80.07 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqfIGRVFQDPKMgtAPRMT 102
Cdd:PRK11000 16 VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG--VGMVFQSYAL--YPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAVmnngLENRlntfVEGLSGGQRQALSFLMATIERPDILLLDEHTAA 182
Cdd:PRK11000 92 VAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHL----LDRK----PKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489745462 183 LDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK11000 164 LDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
25-231 |
4.05e-17 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 80.09 E-value: 4.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPD---SGFLLHNGHDITKMSEEKRTQFigrVFQDPKMgtAPRM 101
Cdd:TIGR00955 40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAY---VQQDDLF--IPTL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLL-ATKRGKRRFLKirklKQNLPRFKKLAAVMnnGLENRLNT------FVEGLSGGQRQALSFLMATIERPDIL 174
Cdd:TIGR00955 115 TVREHLMFqAHLRMPRRVTK----KEKRERVDEVLQAL--GLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 175 LLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALkYG--NRLLVLKDGKV 231
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVL-KGLAQKGKTIICTIHQPSSEL-FElfDKIILMAEGRV 245
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
23-231 |
4.58e-17 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 80.15 E-value: 4.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGtapRMT 102
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLF---SGS 570
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATKRgkrrflkirKLKQNLPRFKKLAAVMN--NGLENRLNTFVEG----LSGGQRQALSFLMATIERPDILLL 176
Cdd:TIGR00958 571 VRENIAYGLTD---------TPDEEIMAAAKAANAHDfiMEFPNGYDTEVGEkgsqLSGGQKQRIAIARALVRKPRVLIL 641
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 177 DEHTAALDPHtSENLLavtdQQIKENK-LTALMITHHMEDALKyGNRLLVLKDGKV 231
Cdd:TIGR00958 642 DEATSALDAE-CEQLL----QESRSRAsRTVLLIAHRLSTVER-ADQILVLKKGSV 691
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
6-231 |
5.36e-17 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 79.12 E-value: 5.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKttvKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMseEKRTQF 85
Cdd:PRK11650 4 LKLQAVR---KSYDGK-TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNEL--EPADRD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDpkmgTA--PRMTVAENLLLAtkrgkrrfLKIRKL-KQNLPRFKKLAAVMnngLEnrLNTFVE----GLSGGQR 158
Cdd:PRK11650 78 IAMVFQN----YAlyPHMSVRENMAYG--------LKIRGMpKAEIEERVAEAARI---LE--LEPLLDrkprELSGGQR 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 159 QALSFLMATIERPDILLLDEHTAALDPHtsenlLAVtdQ---QIKenKL------TALMITHHMEDALKYGNRLLVLKDG 229
Cdd:PRK11650 141 QRVAMGRAIVREPAVFLFDEPLSNLDAK-----LRV--QmrlEIQ--RLhrrlktTSLYVTHDQVEAMTLADRVVVMNGG 211
|
..
gi 489745462 230 KV 231
Cdd:PRK11650 212 VA 213
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
25-192 |
5.51e-17 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 79.92 E-value: 5.51e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDS--GFLLHNGHDITKMSeEKRTQFigrVFQDPKMgtAPRMT 102
Cdd:PLN03211 83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTKQI-LKRTGF---VTQDDIL--YPHLT 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLlatkrgkrrFLKIRKLKQNLPRFKKLAA----VMNNGL---ENRL--NTFVEGLSGGQRQALSFLMATIERPDI 173
Cdd:PLN03211 157 VRETLV---------FCSLLRLPKSLTKQEKILVaesvISELGLtkcENTIigNSFIRGISGGERKRVSIAHEMLINPSL 227
|
170
....*....|....*....
gi 489745462 174 LLLDEHTAALDPHTSENLL 192
Cdd:PLN03211 228 LILDEPTSGLDATAAYRLV 246
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
28-231 |
6.70e-17 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 77.66 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 28 GIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNG-----HDITKMSEEKRtQFIGR-----VFQDPKMGT 97
Cdd:PRK11701 24 DVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAER-RRLLRtewgfVHQHPRDGL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 98 apRMTVAE--NL---LLATkrGKRRFLKIRKLKQNLPRFKKLAAvmnNGLENRLNTFveglSGGQRQALSFLMATIERPD 172
Cdd:PRK11701 103 --RMQVSAggNIgerLMAV--GARHYGDIRATAGDWLERVEIDA---ARIDDLPTTF----SGGMQQRLQIARNLVTHPR 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 173 ILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK11701 172 LVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
24-234 |
6.97e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 77.43 E-value: 6.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPkmGTAPRMTV 103
Cdd:COG4604 15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQEN--HINSRLTV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AEnlLLATKR---GKRRFLKI--RKLKQNLpRFKKLAAvmnngLENRlntFVEGLSGGQRQaLSFL-MATIERPDILLLD 177
Cdd:COG4604 93 RE--LVAFGRfpySKGRLTAEdrEIIDEAI-AYLDLED-----LADR---YLDELSGGQRQ-RAFIaMVLAQDTDYVLLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 178 EHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:COG4604 161 EPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQ 217
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
23-230 |
8.89e-17 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 79.18 E-value: 8.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EEKRTQFIGRVFQDpkMGTAPRM 101
Cdd:PRK11288 17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFAStTAALAAGVAIIYQE--LHLVPEM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLA---TKRG--KRRFLKIRKLKQnlprFKKLaavmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLL 176
Cdd:PRK11288 95 TVAENLYLGqlpHKGGivNRRLLNYEAREQ----LEHL------GVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAF 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 177 DEHTAALDPHTSENLLAVTDQQIKENKLTaLMITHHMEDALKYGNRLLVLKDGK 230
Cdd:PRK11288 165 DEPTSSLSAREIEQLFRVIRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDGR 217
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
1-231 |
9.84e-17 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 78.98 E-value: 9.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKTTVKTAdGEIVPILKGIDLKIKAGDFITIIGTNGAGKS-TLLNTIagSLRPD------SGFLLHNGHD 73
Cdd:PRK15134 1 MTQPLLAIENLSVAFRQQ-QTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSIL--RLLPSppvvypSGDIRFHGES 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 74 ITKMSEEK----RTQFIGRVFQDPKMGTAPRMTVAENL--LLATKRGKRRFLKIRKLKQNLPRFKKLAAvmnnglENRLN 147
Cdd:PRK15134 78 LLHASEQTlrgvRGNKIAMIFQEPMVSLNPLHTLEKQLyeVLSLHRGMRREAARGEILNCLDRVGIRQA------AKRLT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 148 TFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLK 227
Cdd:PRK15134 152 DYPHQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQ 231
|
....
gi 489745462 228 DGKV 231
Cdd:PRK15134 232 NGRC 235
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
26-231 |
1.22e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 77.18 E-value: 1.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFI----GRVFQdpkmgtAPRM 101
Cdd:PRK13641 23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKNLKKLrkkvSLVFQ------FPEA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLA-TKRGKRRFlkirKLKQNLPRFKKLAAVMNNGL-ENRLNTFVEGLSGGQ--RQALSFLMAtiERPDILLLD 177
Cdd:PRK13641 97 QLFENTVLKdVEFGPKNF----GFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQmrRVAIAGVMA--YEPEILCLD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 178 EHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK13641 171 EPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKL 223
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
5-239 |
1.29e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 77.15 E-value: 1.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTAdgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ 84
Cdd:PRK13652 3 LIETRDLCYSYSGS----KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 FIGRVFQDPK---MGTAPRMTVA---ENLLLATKRGKRRFLKIRKLKqnlprfkklaavmnnGLENRLNTFVEGLSGGQR 158
Cdd:PRK13652 79 FVGLVFQNPDdqiFSPTVEQDIAfgpINLGLDEETVAHRVSSALHML---------------GLEELRDRVPHHLSGGEK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 159 QALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADINEQ 238
Cdd:PRK13652 144 KRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
.
gi 489745462 239 E 239
Cdd:PRK13652 224 E 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
5-231 |
1.57e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 77.58 E-value: 1.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFL----LHNGHDIT----- 75
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNnheli 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 76 ------KMSEEKR-TQFIGRVFQDPkmgtaprmtvaENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAVMNNGLENRlNT 148
Cdd:PRK13631 101 tnpyskKIKNFKElRRRVSMVFQFP-----------EYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLD-DS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 149 FVE----GLSGGQ--RQALSFLMAtIErPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNR 222
Cdd:PRK13631 169 YLErspfGLSGGQkrRVAIAGILA-IQ-PEILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADE 245
|
....*....
gi 489745462 223 LLVLKDGKV 231
Cdd:PRK13631 246 VIVMDKGKI 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
3-231 |
1.63e-16 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 78.14 E-value: 1.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVktTVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKR 82
Cdd:COG3845 255 EVVLEVENL--SVRDDRG--VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRER 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 TQF-IGRVFQDP-KMGTAPRMTVAENLLLATKR----GKRRFLKIRKLKQNLPRFKKLAAVMNNGLEnrlnTFVEGLSGG 156
Cdd:COG3845 331 RRLgVAYIPEDRlGRGLVPDMSVAENLILGRYRrppfSRGGFLDRKAIRAFAEELIEEFDVRTPGPD----TPARSLSGG 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 157 --QRqalsFLMA-TIER-PDILLLDEHTAALDPHTSENLLavtdQQIKE--NKLTA-LMITHHMEDALKYGNRLLVLKDG 229
Cdd:COG3845 407 nqQK----VILArELSRdPKLLIAAQPTRGLDVGAIEFIH----QRLLElrDAGAAvLLISEDLDEILALSDRIAVMYEG 478
|
..
gi 489745462 230 KV 231
Cdd:COG3845 479 RI 480
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
5-233 |
1.98e-16 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 76.70 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKtaDGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ 84
Cdd:PRK13647 4 IIEVEDLHFRYK--DG--TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 FIGRVFQDPKmGTAPRMTVAE-------NLLLATKRGKRRFLKirklkqnlprfkKLAAVmnnGLENRLNTFVEGLSGGQ 157
Cdd:PRK13647 80 KVGLVFQDPD-DQVFSSTVWDdvafgpvNMGLDKDEVERRVEE------------ALKAV---RMWDFRDKPPYHLSYGQ 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 158 --RQALSFLMATieRPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:PRK13647 144 kkRVAIAGVLAM--DPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLA 218
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
25-231 |
2.08e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 76.26 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF---IGRVFQDPKMGTAPRM 101
Cdd:PRK10419 27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFrrdIQMVFQDSISAVNPRK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLllatKRGKRRFLKIRKLKQNLPRFKKLAAV-MNNGLENRLNtfvEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PRK10419 107 TVREII----REPLRHLLSLDKAERLARASEMLRAVdLDDSVLDKRP---PQLSGGQLQRVCLARALAVEPKLLILDEAV 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489745462 181 AALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK10419 180 SNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
6-232 |
4.42e-16 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 77.37 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTADgeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EEKRTQ 84
Cdd:PRK11176 342 IEFRNVTFTYPGKE---VPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDYTlASLRNQ 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 FI-----GRVFQDpkmgtaprmTVAENLLLATKRGKRRflkirklkQNLPRFKKLAAVMN--NGLENRLNTFV--EG--L 153
Cdd:PRK11176 419 VAlvsqnVHLFND---------TIANNIAYARTEQYSR--------EQIEEAARMAYAMDfiNKMDNGLDTVIgeNGvlL 481
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 154 SGGQRQALSFLMATIERPDILLLDEHTAALDPHtSENLLAVTDQQIKENKlTALMITHHMEdALKYGNRLLVLKDGKVK 232
Cdd:PRK11176 482 SGGQRQRIAIARALLRDSPILILDEATSALDTE-SERAIQAALDELQKNR-TSLVIAHRLS-TIEKADEILVVEDGEIV 557
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-231 |
4.45e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 75.26 E-value: 4.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAG--SLRPDS---GFLLHNGHDI--TKMSEEKRTQFIGRVFQDPKmgT 97
Cdd:PRK14267 19 VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEArveGEVRLFGRNIysPDVDPIEVRREVGMVFQYPN--P 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 98 APRMTVAENLLLATKrgkrrFLKIRKLKQNLPRFKKLA---AVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDIL 174
Cdd:PRK14267 97 FPHLTIYDNVAIGVK-----LNGLVKSKKELDERVEWAlkkAALWDEVKDRLNDYPSNLSGGQRQRLVIARALAMKPKIL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 175 LLDEHTAALDPhtsenllaVTDQQIKE------NKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK14267 172 LMDEPTANIDP--------VGTAKIEEllfelkKEYTIVLVTHSPAQAARVSDYVAFLYLGKL 226
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
24-229 |
6.32e-16 |
|
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: 75.28 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNghditkmseekrtqfiGRVFQDPKMGTAPRMTV 103
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHS----------------GRISFSSQFSWIMPGTI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGKRRFLKIRK---LKQNLPRF-KKLAAVMNNGLENrlntfvegLSGGQRQALSFLMATIERPDILLLDEH 179
Cdd:cd03291 115 KENIIFGVSYDEYRYKSVVKacqLEEDITKFpEKDNTVLGEGGIT--------LSGGQRARISLARAVYKDADLYLLDSP 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 180 TAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDaLKYGNRLLVLKDG 229
Cdd:cd03291 187 FGYLDVFTEKEIFESCVCKLMANK-TRILVTSKMEH-LKKADKILILHEG 234
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-231 |
8.07e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.13 E-value: 8.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKmGTAPRMTVAE 105
Cdd:PRK13642 23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPD-NQFVGATVED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 NLLLATKrgkrrflkirklKQNLPRFKKLAAVMNNGLENRLNTFV----EGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:PRK13642 102 DVAFGME------------NQGIPREEMIKRVDEALLAVNMLDFKtrepARLSGGQKQRVAVAGIIALRPEIIILDESTS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 182 ALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKyGNRLLVLKDGKV 231
Cdd:PRK13642 170 MLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEI 218
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
21-231 |
1.63e-15 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 75.93 E-value: 1.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 21 EIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTApr 100
Cdd:PLN03130 1250 ELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSG-- 1327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 mTVAENLLLATKRGKRrflkirKLKQNLPRFKKLAAVMNN--GLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:PLN03130 1328 -TVRFNLDPFNEHNDA------DLWESLERAHLKDVIRRNslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 179 HTAALDPHTSenllAVTDQQIKE--NKLTALMITHHMEDALKyGNRLLVLKDGKV 231
Cdd:PLN03130 1401 ATAAVDVRTD----ALIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRV 1450
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
29-231 |
1.85e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 74.00 E-value: 1.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 29 IDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ----FIGRVFQDPKmgtapRMTVA 104
Cdd:PRK13643 25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKEIKpvrkKVGVVFQFPE-----SQLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 105 ENLLLATKRGKRRFlKIRKLKQNLPRFKKLAAVmnnGLENRlntFVEG----LSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PRK13643 100 ETVLKDVAFGPQNF-GIPKEKAEKIAAEKLEMV---GLADE---FWEKspfeLSGGQMRRVAIAGILAMEPEVLVLDEPT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489745462 181 AALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK13643 173 AGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHI 222
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
6-229 |
2.78e-15 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 74.84 E-value: 2.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGsLRPD-SGfllhnghDITkMSEEKRTQ 84
Cdd:COG4178 363 LALEDL--TLRTPDGR--PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAG-LWPYgSG-------RIA-RPAGARVL 429
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 FIGrvfQDPKMgtaPRMTVAENLL---LATKRGKRRFLKIrkLKQ-NLPRfkklaavmnngLENRLNTFV---EGLSGGQ 157
Cdd:COG4178 430 FLP---QRPYL---PLGTLREALLypaTAEAFSDAELREA--LEAvGLGH-----------LAERLDEEAdwdQVLSLGE 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489745462 158 RQALSFLMATIERPDILLLDEHTAALDPHTSENLLavtdQQIKEN--KLTALMITHHmEDALKYGNRLLVLKDG 229
Cdd:COG4178 491 QQRLAFARLLLHKPDWLFLDEATSALDEENEAALY----QLLREElpGTTVISVGHR-STLAAFHDRVLELTGD 559
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
25-230 |
3.48e-15 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 74.76 E-value: 3.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIA----GSLRPDSGFLLHNGHDitkmSEEKRTQFIGRVFQDPKMGT-AP 99
Cdd:TIGR00956 76 ILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGIT----PEEIKKHYRGDVVYNAETDVhFP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 RMTVAENLLLATK-RG-KRRFLKIRKLKqnlpRFKKLAAVMNN--GLENRLNT-----FVEGLSGGQRQALSFLMATIER 170
Cdd:TIGR00956 152 HLTVGETLDFAARcKTpQNRPDGVSREE----YAKHIADVYMAtyGLSHTRNTkvgndFVRGVSGGERKRVSIAEASLGG 227
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 171 PDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALM-ITHHMEDALKYGNRLLVLKDGK 230
Cdd:TIGR00956 228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGY 288
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
28-212 |
3.56e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 71.76 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 28 GIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQ--FIGRvfqdpKMGTAPRMTVAE 105
Cdd:PRK13538 19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDllYLGH-----QPGIKTELTALE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 NLllatkrgkRRFLKIRKLKQNLPRFKKLAAVmnnGLENRLNTFVEGLSGGQ--RQALSFLMatIERPDILLLDEHTAAL 183
Cdd:PRK13538 94 NL--------RFYQRLHGPGDDEALWEALAQV---GLAGFEDVPVRQLSAGQqrRVALARLW--LTRAPLWILDEPFTAI 160
|
170 180
....*....|....*....|....*....
gi 489745462 184 DPHTSENLLAVTDQQIkENKLTALMITHH 212
Cdd:PRK13538 161 DKQGVARLEALLAQHA-EQGGMVILTTHQ 188
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
25-216 |
4.80e-15 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 72.38 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAG--SLRPD---SGFLLHNGHDI--TKMS-EEKRTQfIGRVFQDPkmg 96
Cdd:COG1117 26 ALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRmnDLIPGarvEGEILLDGEDIydPDVDvVELRRR-VGMVFQKP--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 97 tAP-RMTVAEN----LLLATKRGKRRFLKI--RKLKQnlprfkklAAVMNNgLENRLNTFVEGLSGGQRQALsflmaTIE 169
Cdd:COG1117 102 -NPfPKSIYDNvaygLRLHGIKSKSELDEIveESLRK--------AALWDE-VKDRLKKSALGLSGGQQQRL-----CIA 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 170 R-----PDILLLDEHTAALDPHTS---ENLLavtdQQIKENkLTALMITHHMEDA 216
Cdd:COG1117 167 RalavePEVLLMDEPTSALDPISTakiEELI----LELKKD-YTIVIVTHNMQQA 216
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
5-231 |
7.63e-15 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 72.13 E-value: 7.63e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADG----EIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE 80
Cdd:PRK15112 4 LLEVRNLSKTFRYRTGwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 81 KRTQFIGRVFQDPKMGTAPRMTVAENL---------LLATKRGKRRFLKIRKLKQnlprfkklaavmnngLENRLNTFVE 151
Cdd:PRK15112 84 YRSQRIRMIFQDPSTSLNPRQRISQILdfplrlntdLEPEQREKQIIETLRQVGL---------------LPDHASYYPH 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 152 GLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK15112 149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-231 |
1.01e-14 |
|
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.
Pssm-ID: 213215 [Multi-domain] Cd Length: 226 Bit Score: 70.96 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAprmT 102
Cdd:cd03248 27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFAR---S 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENllLATKRGKRRFLKIRKLKQnlprfKKLAAVMNNGLENRLNTFV--EG--LSGGQRQALSFLMATIERPDILLLDE 178
Cdd:cd03248 104 LQDN--IAYGLQSCSFECVKEAAQ-----KAHAHSFISELASGYDTEVgeKGsqLSGGQKQRVAIARALIRNPQVLILDE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489745462 179 HTAALDPHtSENLLAVTDQQIKENKlTALMITHHMEdALKYGNRLLVLKDGKV 231
Cdd:cd03248 177 ATSALDAE-SEQQVQQALYDWPERR-TVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
4-226 |
1.07e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 72.25 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVKTTVKTADGEIVpILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRP------DSGFLlhNGHDITKM 77
Cdd:COG4170 2 PLLDIRNLTIEIDTPQGRVK-AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvtaDRFRW--NGIDLLKL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 78 SEEKRTQFIGR----VFQDPKMGTAPRMTVAENLLLA----TKRGK---RRFLKIRKLKQNLPR--FKKLAAVMNNglen 144
Cdd:COG4170 79 SPRERRKIIGReiamIFQEPSSCLDPSAKIGDQLIEAipswTFKGKwwqRFKWRKKRAIELLHRvgIKDHKDIMNS---- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 145 rlntFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLL 224
Cdd:COG4170 155 ----YPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTIT 230
|
..
gi 489745462 225 VL 226
Cdd:COG4170 231 VL 232
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
24-231 |
1.56e-14 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 72.83 E-value: 1.56e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPkmgtaprMTV 103
Cdd:PRK10790 355 LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDP-------VVL 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGkrRFLKIRKLKQNLP--RFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:PRK10790 428 ADTFLANVTLG--RDISEEQVWQALEtvQLAELARSLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILILDEATA 505
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 182 ALDPHTsENLLAVTDQQIKENklTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK10790 506 NIDSGT-EQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQA 552
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-231 |
1.88e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 70.85 E-value: 1.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNT------IAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKmgTA 98
Cdd:PRK14246 25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVlnrlieIYDSKIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPN--PF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 PRMTVAENLLLATK-RGKRRFLKIRKLKQNLPRFKKLAavmnNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLD 177
Cdd:PRK14246 103 PHLSIYDNIAYPLKsHGIKEKREIKKIVEECLRKVGLW----KEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 178 EHTAALDPHTSENLLAVTDQQikENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK14246 179 EPTSMIDIVNSQAIEKLITEL--KNEIAIVIVSHNPQQVARVADYVAFLYNGEL 230
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
29-231 |
2.43e-14 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 71.31 E-value: 2.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 29 IDLKIKAGDFITIIGTNGAGKSTLLNTIAGSL----RPDSGFLLHNGHDITKMSEEKRTQFIGR----VFQDPKMGTAPR 100
Cdd:PRK11022 26 ISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdypgRVMAEKLEFNGQDLQRISEKERRNLVGAevamIFQDPMTSLNPC 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAENLLLATKR---GKRRFLKIRKLKQnlprfkkLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLD 177
Cdd:PRK11022 106 YTVGFQIMEAIKVhqgGNKKTRRQRAIDL-------LNQVGIPDPASRLDVYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 178 EHTAALD----PHTSENLLavtDQQIKENkLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK11022 179 EPTTALDvtiqAQIIELLL---ELQQKEN-MALVLITHDLALVAEAAHKIIVMYAGQV 232
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-230 |
2.51e-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: 2.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 8 LKDVKTTVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGsLRPD---SGFLLHNGHDItKMSEEKRTQ 84
Cdd:TIGR02633 1 LLEMKGIVKTFGG--VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSG-VYPHgtwDGEIYWSGSPL-KASNIRDTE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 FIGRVFQDPKMGTAPRMTVAENLLLA---TKRGKRRFLKIRKLK-QNLPRFKKLAAvMNNGLEnrlntfVEGLSGGQRQA 160
Cdd:TIGR02633 77 RAGIVIIHQELTLVPELSVAENIFLGneiTLPGGRMAYNAMYLRaKNLLRELQLDA-DNVTRP------VGDYGGGQQQL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 161 LSFLMATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:TIGR02633 150 VEIAKALNKQARLLILDEPSSSLTEKETEILLDII-RDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQ 218
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
22-229 |
3.12e-14 |
|
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: 71.87 E-value: 3.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 22 IVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNghditkmseekrtqfiGRVFQDPKMGTAPRM 101
Cdd:TIGR01271 438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHS----------------GRISFSPQTSWIMPG 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLATKRGKRRFLKIRK---LKQNLPRF--KKLAAVMNNGLEnrlntfvegLSGGQRQALSFLMATIERPDILLL 176
Cdd:TIGR01271 502 TIKDNIIFGLSYDEYRYTSVIKacqLEEDIALFpeKDKTVLGEGGIT---------LSGGQRARISLARAVYKDADLYLL 572
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489745462 177 DEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDaLKYGNRLLVLKDG 229
Cdd:TIGR01271 573 DSPFTHLDVVTEKEIFESCLCKLMSNK-TRILVTSKLEH-LKKADKILLLHEG 623
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
6-241 |
3.99e-14 |
|
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: 71.37 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EEKRTQ 84
Cdd:COG4615 328 LELRGVTYRYPGEDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNrEAYRQL 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 FiGRVFQD-------PKMGTAPRMTVAENLLlatkrgkrRFLKI-RKLKqnlprfkklaaVMNNGLENRlntfveGLSGG 156
Cdd:COG4615 408 F-SAVFSDfhlfdrlLGLDGEADPARARELL--------ERLELdHKVS-----------VEDGRFSTT------DLSQG 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 157 QRQALSFLMATIERPDILLLDEHTAALDPH-----TSEnLLavtdQQIKENKLTALMITH-----HMEDalkygnRLLVL 226
Cdd:COG4615 462 QRKRLALLVALLEDRPILVFDEWAADQDPEfrrvfYTE-LL----PELKARGKTVIAISHddryfDLAD------RVLKM 530
|
250
....*....|....*
gi 489745462 227 KDGKVKADINEQEKQ 241
Cdd:COG4615 531 DYGKLVELTGPAALA 545
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
24-231 |
4.17e-14 |
|
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: 68.83 E-value: 4.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPD---SGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMgtaPR 100
Cdd:cd03233 21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF---PT 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAENLllatkrgkrrflkirklkqnlprfkKLAAVMNNglenrlNTFVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:cd03233 98 LTVRETL-------------------------DFALRCKG------NEFVRGISGGERKRVSIAEALVSRASVLCWDNST 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489745462 181 AALDPHTSENLLAVTDQQIKENKLTALM-ITHHMEDALKYGNRLLVLKDGKV 231
Cdd:cd03233 147 RGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
20-229 |
4.83e-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: 68.90 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 20 GEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEE---KRTQF-IGRVFQDPKM 95
Cdd:cd03290 11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEatrSRNRYsVAYAAQKPWL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 96 GTAprmTVAENLLLATKRGKRRFLKIRKLKQNLPRFKklaaVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILL 175
Cdd:cd03290 91 LNA---TVEENITFGSPFNKQRYKAVTDACSLQPDID----LLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 176 LDEHTAALDPHTSENLL-AVTDQQIKENKLTALMITHHMEdALKYGNRLLVLKDG 229
Cdd:cd03290 164 LDDPFSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQ-YLPHADWIIAMKDG 217
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
24-227 |
4.92e-14 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 69.11 E-value: 4.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKmseEKRTQFIGRVFQDPkmGTAPRMTV 103
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATR---GDRSRFMAYLGHLP--GLKADLST 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENL-LLATKRGKRrflkirklKQNLPRfKKLAAVmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAA 182
Cdd:PRK13543 100 LENLhFLCGLHGRR--------AKQMPG-SALAIV---GLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYAN 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489745462 183 LDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLK 227
Cdd:PRK13543 168 LDLEGITLVNRMISAHLRGGG-AALVTTHGAYAAPPVRTRMLTLE 211
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-230 |
5.86e-14 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 70.77 E-value: 5.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGT---APRMT 102
Cdd:PRK10522 339 VGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTDFHLFDqllGPEGK 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATkrgkrrFLKIRKLKQNLpRFKklaavmnnglENRLNTFveGLSGGQRQALSFLMATIERPDILLLDEHTAA 182
Cdd:PRK10522 419 PANPALVEK------WLERLKMAHKL-ELE----------DGRISNL--KLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489745462 183 LDPHTSENLLAVTDQQIKENKLTALMITHhmEDA-LKYGNRLLVLKDGK 230
Cdd:PRK10522 480 QDPHFRREFYQVLLPLLQEMGKTIFAISH--DDHyFIHADRLLEMRNGQ 526
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
19-212 |
1.22e-13 |
|
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: 67.52 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 19 DGEIVpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDpkmGTA 98
Cdd:cd03231 11 DGRAL--FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP---GIK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 PRMTVAENLllatkrgkrRFLkiRKLKQNLPRFKKLAAVMNNGLENRLntfVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:cd03231 86 TTLSVLENL---------RFW--HADHSDEQVEEALARVGLNGFEDRP---VAQLSAGQQRRVALARLLLSGRPLWILDE 151
|
170 180 190
....*....|....*....|....*....|....
gi 489745462 179 HTAALDPhTSENLLAVTDQQIKENKLTALMITHH 212
Cdd:cd03231 152 PTTALDK-AGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
26-216 |
1.51e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 68.27 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLL------NTIAGSLRPDSGFLLH----NGHDITKMSEEKRtqfIGRVFQDPKm 95
Cdd:PRK14243 26 VKNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIPGFRVEGKVTFHgknlYAPDVDPVEVRRR---IGMVFQKPN- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 96 gTAPRmTVAENLLLATK----RGKRRFLKIRKLKQnlprfkklaAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERP 171
Cdd:PRK14243 102 -PFPK-SIYDNIAYGARingyKGDMDELVERSLRQ---------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQP 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 489745462 172 DILLLDEHTAALDPHTS---ENLLavtdQQIKEnKLTALMITHHMEDA 216
Cdd:PRK14243 171 EVILMDEPCSALDPISTlriEELM----HELKE-QYTIIIVTHNMQQA 213
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-231 |
1.55e-13 |
|
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: 69.85 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKST---LLntiagsLR---PDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGT 97
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTlarLL------FRfydVTSGRILIDGQDIRDVTQASLRAAIGIVPQDTVLFN 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 98 AprmTVAENLLL----ATKRgkrrflKIRklkqnlpRFKKLAAVMN--NGLENRLNTFVeG-----LSGGQRQALSFLMA 166
Cdd:COG5265 446 D---TIAYNIAYgrpdASEE------EVE-------AAARAAQIHDfiESLPDGYDTRV-GerglkLSGGEKQRVAIART 508
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 167 TIERPDILLLDEHTAALDPHTSENLLAvTDQQIKENKlTALMITHHME---DAlkygNRLLVLKDGKV 231
Cdd:COG5265 509 LLKNPPILIFDEATSALDSRTERAIQA-ALREVARGR-TTLVIAHRLStivDA----DEILVLEAGRI 570
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-231 |
1.56e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 1.56e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGF-----LLHNGHDITKMSE--EKRTQfIGRVFQDPKmgT 97
Cdd:PRK14271 36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYrysgdVLLGGRSIFNYRDvlEFRRR-VGMLFQRPN--P 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 98 APrMTVAENLLLATKRGKrrfLKIRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLD 177
Cdd:PRK14271 113 FP-MSIMDNVLAGVRAHK---LVPRKEFRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 178 EHTAALDPHTSENLlavtDQQIKE--NKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK14271 189 EPTSALDPTTTEKI----EEFIRSlaDRLTVIIVTHNLAQAARISDRAALFFDGRL 240
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
1-230 |
1.79e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 1.79e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGsLRPD---SGFLLHNGHDItKM 77
Cdd:PRK13549 1 MMEYLLEMKNI---TKTFGG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSG-VYPHgtyEGEIIFEGEEL-QA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 78 SEEKRTQFIGRVFQDPKMGTAPRMTVAENLLLATKRGKRRFLKIRKLKQnlpRFKKLAAVMNngLENRLNTFVEGLSGGQ 157
Cdd:PRK13549 74 SNIRDTERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDYDAMYL---RAQKLLAQLK--LDINPATPVGNLGLGQ 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 158 RQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:PRK13549 149 QQLVEIAKALNKQARLLILDEPTASLTESETAVLLDII-RDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
25-233 |
1.81e-13 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 68.28 E-value: 1.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKrtqFIGRVFQDPK-MGTAPRMTV 103
Cdd:PRK10575 26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKA---FARKVAYLPQqLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AEnlLLATKR-------GKRRFLKIRKLKQnlprfkklaAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLL 176
Cdd:PRK10575 103 RE--LVAIGRypwhgalGRFGAADREKVEE---------AISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 177 DEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:PRK10575 172 DEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIA 228
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
24-217 |
3.43e-13 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 66.51 E-value: 3.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITK--MSEEKRTQFIGRvfqdpKMGTAPRM 101
Cdd:PRK13540 15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdlCTYQKQLCFVGH-----RSGINPYL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLL--LATKRGKRRFLKIRKLkqnlprFKklaavmnngLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEH 179
Cdd:PRK13540 90 TLRENCLydIHFSPGAVGITELCRL------FS---------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEP 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 489745462 180 TAALDPHTSENLlaVTDQQIKENKLTALMITHHMEDAL 217
Cdd:PRK13540 155 LVALDELSLLTI--ITKIQEHRAKGGAVLLTSHQDLPL 190
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
24-233 |
3.45e-13 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 67.34 E-value: 3.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGH--DITKMSEEKRTQFIGRVFQDPKMG---TA 98
Cdd:PRK13638 15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVATVFQDPEQQifyTD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 PRMTVA---ENLLLATKRGKRRFLKIRKLkQNLPRFKKLAavmnnglenrlntfVEGLSGGQRQALSFLMATIERPDILL 175
Cdd:PRK13638 95 IDSDIAfslRNLGVPEAEITRRVDEALTL-VDAQHFRHQP--------------IQCLSHGQKKRVAIAGALVLQARYLL 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 176 LDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:PRK13638 160 LDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILT 216
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
21-231 |
3.93e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 68.85 E-value: 3.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 21 EIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTApr 100
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSG-- 1324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 mTVAENLLLATKRGKRrflkirKLKQNLPRFKKLAAVMNN--GLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:PLN03232 1325 -TVRFNIDPFSEHNDA------DLWEALERAHIKDVIDRNpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDE 1397
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 489745462 179 HTAALDPHTSenllAVTDQQIKE--NKLTALMITHHMEDALKYgNRLLVLKDGKV 231
Cdd:PLN03232 1398 ATASVDVRTD----SLIQRTIREefKSCTMLVIAHRLNTIIDC-DKILVLSSGQV 1447
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
19-230 |
4.25e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 68.34 E-value: 4.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 19 DGEIVPILKGIDLKIKAGDFITIIGTNGAGKST-------LLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQF------ 85
Cdd:PRK10261 25 EQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVtalalmrLLEQAGGLVQCDKMLLRRRSRQVIELSEQSAAQMrhvrga 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 -IGRVFQDPKMGTAPRMTV----AENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAVmnnglenrLNTFVEGLSGGQRQA 160
Cdd:PRK10261 105 dMAMIFQEPMTSLNPVFTVgeqiAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTI--------LSRYPHQLSGGMRQR 176
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 161 LSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:PRK10261 177 VMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGE 246
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
1-211 |
4.88e-13 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 67.68 E-value: 4.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 1 MTKPILELKDVKT--TVKT---ADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTL---LNTIAgslRPDSGFLLHNGH 72
Cdd:PRK11308 1 SQQPLLQAIDLKKhyPVKRglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLarlLTMIE---TPTGGELYYQGQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 73 DITKMSEEKRTQF---IGRVFQDPKMGTAPRMTV----AENLLLATKRGKRRflkirklkqnlpRFKKLAAVMNN-GLE- 143
Cdd:PRK11308 78 DLLKADPEAQKLLrqkIQIVFQNPYGSLNPRKKVgqilEEPLLINTSLSAAE------------RREKALAMMAKvGLRp 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489745462 144 ---NRlntFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSE---NLLAvtDQQiKENKLTALMITH 211
Cdd:PRK11308 146 ehyDR---YPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAqvlNLMM--DLQ-QELGLSYVFISH 213
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
24-242 |
9.84e-13 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 65.94 E-value: 9.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSE----EKRTQfIGRVFQDPKMGTap 99
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrlyTVRKR-MSMLFQSGALFT-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 100 RMTVAENLLLATKRGKRrflkirkLKQNLPR---FKKLAAVmnnGLENRLNTFVEGLSGG--QRQALSFLMATieRPDIL 174
Cdd:PRK11831 98 DMNVFDNVAYPLREHTQ-------LPAPLLHstvMMKLEAV---GLRGAAKLMPSELSGGmaRRAALARAIAL--EPDLI 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 175 LLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADINEQEKQN 242
Cdd:PRK11831 166 MFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQA 233
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
25-234 |
1.03e-12 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 66.00 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSL----RPD----SGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMG 96
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLtgggAPRgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 97 TAprMTVAENLLLAtkrgkrRFLKIRKLKQNLPRFKKLA--AVMNNGLENRLNTFVEGLSGGQRQALSFLMA-------- 166
Cdd:PRK13547 96 FA--FSAREIVLLG------RYPHARRAGALTHRDGEIAwqALALAGATALVGRDVTTLSGGELARVQFARVlaqlwpph 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 167 -TIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKAD 234
Cdd:PRK13547 168 dAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
7-239 |
1.56e-12 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 66.58 E-value: 1.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 7 ELKDVKTTVKTADGEIV---------PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKM 77
Cdd:COG1129 240 ELEDLFPKRAAAPGEVVleveglsvgGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIR 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 78 S-------------EEKRTQfigrvfqdpkmGTAPRMTVAENLLLAT--KRGKRRFLKIRKLKQNLPRF-KKLAAVMNNg 141
Cdd:COG1129 320 SprdairagiayvpEDRKGE-----------GLVLDLSIRENITLASldRLSRGGLLDRRRERALAEEYiKRLRIKTPS- 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 142 lenrLNTFVEGLSGG--QRQALSFLMATieRPDILLLDEHTAALDPHT-SE--NLLavtdQQIKENKLTALMITHHMEDA 216
Cdd:COG1129 388 ----PEQPVGNLSGGnqQKVVLAKWLAT--DPKVLILDEPTRGIDVGAkAEiyRLI----RELAAEGKAVIVISSELPEL 457
|
250 260
....*....|....*....|...
gi 489745462 217 LKYGNRLLVLKDGKVKADINEQE 239
Cdd:COG1129 458 LGLSDRILVMREGRIVGELDREE 480
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
31-230 |
1.93e-12 |
|
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: 65.12 E-value: 1.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 31 LKIKAGDF-----ITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVfqdpkmgtaprmtvae 105
Cdd:cd03237 15 LEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTV---------------- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 nlllatkrgkRRFL-KIRKLKQNLPRFKklAAVMNN-GLENRLNTFVEGLSGGQRQALSfLMATIERP-DILLLDEHTAA 182
Cdd:cd03237 79 ----------RDLLsSITKDFYTHPYFK--TEIAKPlQIEQILDREVPELSGGELQRVA-IAACLSKDaDIYLLDEPSAY 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489745462 183 LDphtSENLLAVT---DQQIKENKLTALMITH--HMEDALkyGNRLLVLkDGK 230
Cdd:cd03237 146 LD---VEQRLMASkviRRFAENNEKTAFVVEHdiIMIDYL--ADRLIVF-EGE 192
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
11-239 |
2.28e-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: 65.98 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 11 VKTTVKTADGEIVpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAG--SLRPDSGFLLHNGHDITKMSEEKRTQFIGR 88
Cdd:TIGR03269 3 VKNLTKKFDGKEV--LKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALCEKCGYVERPSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 89 vfQDPKMGTAPRMTVAENLLLAtKRGKRRFLK----------------------IRKL-------KQNLPRFKKLAAVMN 139
Cdd:TIGR03269 81 --PCPVCGGTLEPEEVDFWNLS-DKLRRRIRKriaimlqrtfalygddtvldnvLEALeeigyegKEAVGRAVDLIEMVQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 140 ngLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKY 219
Cdd:TIGR03269 158 --LSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDL 235
|
250 260
....*....|....*....|
gi 489745462 220 GNRLLVLKDGKVKADINEQE 239
Cdd:TIGR03269 236 SDKAIWLENGEIKEEGTPDE 255
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
26-231 |
2.28e-12 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 65.41 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGH----DITKMSEEKRTQF-IGRVFQDPKMGTAPR 100
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYaipaNLKKIKEVKRLRKeIGLVFQFPEYQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAENLLLATKRGKRRflkiRKLKQNLPRFKKLAAVMnnglENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PRK13645 107 TIEKDIAFGPVNLGENK----QEAYKKVPELLKLVQLP----EDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPT 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 489745462 181 AALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK13645 179 GGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKV 229
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
6-228 |
3.33e-12 |
|
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: 62.94 E-value: 3.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADGEIvpILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGsLRPdsgflLHNGHDItkMSEEKRTQF 85
Cdd:cd03223 1 IELENL--SLATPDGRV--LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAG-LWP-----WGSGRIG--MPEGEDLLF 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGrvfQDPKMgtaPRMTVAENLLLatkrgkrrflkirklkqnlPRFKKLaavmnnglenrlntfveglSGGQRQALSFLM 165
Cdd:cd03223 69 LP---QRPYL---PLGTLREQLIY-------------------PWDDVL-------------------SGGEQQRLAFAR 104
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 166 ATIERPDILLLDEHTAALDPhTSENLLAvtdQQIKENKLTALMITHHmEDALKYGNRLLVLKD 228
Cdd:cd03223 105 LLLHKPKFVFLDEATSALDE-ESEDRLY---QLLKELGITVISVGHR-PSLWKFHDRVLDLDG 162
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
24-230 |
3.49e-12 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 62.08 E-value: 3.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHditkmseekrtqfigrvfqdpkmgtaprmtv 103
Cdd:cd03221 14 LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------------------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 aenlllatkrgkrrfLKIRKLKQnlprfkklaavmnnglenrlntfvegLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:cd03221 63 ---------------VKIGYFEQ--------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHL 101
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 489745462 184 DPHTSENLLavtdQQIKENKLTALMITH--HMEDALkyGNRLLVLKDGK 230
Cdd:cd03221 102 DLESIEALE----EALKEYPGTVILVSHdrYFLDQV--ATKIIELEDGK 144
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
25-233 |
4.55e-12 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 63.76 E-value: 4.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRT-QFIGRVFQDPKMGTapRMTV 103
Cdd:PRK10895 18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYLPQEASIFR--RLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLAtkrgkrrfLKIRK---LKQNLPRFKKLAAVMNngLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PRK10895 96 YDNLMAV--------LQIRDdlsAEQREDRANELMEEFH--IEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPF 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 489745462 181 AALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:PRK10895 166 AGVDPISVIDIKRII-EHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIA 217
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
25-211 |
7.06e-12 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 63.59 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHnghditkmSEEKRtqfIGRVFQDPKMGTAPRMTVa 104
Cdd:PRK09544 19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKR--------NGKLR---IGYVPQKLYLDTTLPLTV- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 105 enlllatkrgkRRFLKIR---KLKQNLPRFKKLAAvmnnglENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:PRK09544 87 -----------NRFLRLRpgtKKEDILPALKRVQA------GHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190
....*....|....*....|....*....|
gi 489745462 182 ALDPHTSENLLAVTDQQIKENKLTALMITH 211
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRELDCAVLMVSH 179
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
5-230 |
7.83e-12 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 64.43 E-value: 7.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVkttVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTI-----AGSLrpdSGFLLHNG-----HDI 74
Cdd:NF040905 1 ILEMRGI---TKTFPG--VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLsgvypHGSY---EGEILFDGevcrfKDI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 75 tKMSEEKrtqfiGRVFQDPKMGTAPRMTVAENLLLATKRGKR-------RFLKIRKLkqnlprfkkLAAVmnnGLENRLN 147
Cdd:NF040905 73 -RDSEAL-----GIVIIHQELALIPYLSIAENIFLGNERAKRgvidwneTNRRAREL---------LAKV---GLDESPD 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 148 TFVEGLSGGQRQ------ALSflmatiERPDILLLDEHTAALDPHTSENLLAVTDqQIKENKLTALMITHHMEDALKYGN 221
Cdd:NF040905 135 TLVTDIGVGKQQlveiakALS------KDVKLLILDEPTAALNEEDSAALLDLLL-ELKAQGITSIIISHKLNEIRRVAD 207
|
....*....
gi 489745462 222 RLLVLKDGK 230
Cdd:NF040905 208 SITVLRDGR 216
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
26-233 |
9.20e-12 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 62.94 E-value: 9.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGsLRPDSGFLLHNGHDITKMS------------EEKRTQFIGRVFQDP 93
Cdd:COG4138 12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSaaelarhraylsQQQSPPFAMPVFQYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 94 KMGtAPRMTVAENLLLAtkrgkrrflkIRKLKQNLprfkklaavmnnGLENRLNTFVEGLSGGQRQALSfLMATIER--P 171
Cdd:COG4138 91 ALH-QPAGASSEAVEQL----------LAQLAEAL------------GLEDKLSRPLTQLSGGEWQRVR-LAAVLLQvwP 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 172 DI------LLLDEHTAALDPHTsenlLAVTDQQIKE---NKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:COG4138 147 TInpegqlLLLDEPMNSLDVAQ----QAALDRLLRElcqQGITVVMSSHDLNHTLRHADRVWLLKQGKLVA 213
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
2-248 |
1.08e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.25 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 2 TKPILELKDVKttvKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDIT----KM 77
Cdd:PRK10762 1 MQALLQLKGID---KAFPG--VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngpKS 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 78 SEEkrtQFIGRVFQDpkMGTAPRMTVAENLLLAtKRGKRRFLKIrKLKQNLPRFKKLAAVMNngLENRLNTFVEGLSGGQ 157
Cdd:PRK10762 76 SQE---AGIGIIHQE--LNLIPQLTIAENIFLG-REFVNRFGRI-DWKKMYAEADKLLARLN--LRFSSDKLVGELSIGE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 158 RQ------ALSFlmatieRPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK10762 147 QQmveiakVLSF------ESKVIIMDEPTDALTDTETESLFRVI-RELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQF 219
|
250
....*....|....*..
gi 489745462 232 kadINEQEkqnlkVSDL 248
Cdd:PRK10762 220 ---IAERE-----VADL 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
20-211 |
1.20e-11 |
|
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: 64.19 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 20 GEIVP----ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfllhnghditkmseEKRTQ---FIGRVFQD 92
Cdd:TIGR03719 11 SKVVPpkkeILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG--------------EARPQpgiKVGYLPQE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 93 PKMGtaPRMTVAENLLLA---TKRGKRRFLKIR-KLKQNLPRFKKLAAVM---------NNG--LENRL----------- 146
Cdd:TIGR03719 77 PQLD--PTKTVRENVEEGvaeIKDALDRFNEISaKYAEPDADFDKLAAEQaelqeiidaADAwdLDSQLeiamdalrcpp 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 147 -NTFVEGLSGGQRQ--ALSFLMatIERPDILLLDEHTAALDPHTSENLlavtDQQIKENKLTALMITH 211
Cdd:TIGR03719 155 wDADVTKLSGGERRrvALCRLL--LSKPDMLLLDEPTNHLDAESVAWL----ERHLQEYPGTVVAVTH 216
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
25-231 |
1.52e-11 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 63.57 E-value: 1.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKST----LLNTIAGSlrpdsGFLLHNGHDITKMSEEKRTQFIGR---VFQDPKMGT 97
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINSQ-----GEIWFDGQPLHNLNRRQLLPVRHRiqvVFQDPNSSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 98 APRMTV----AENLllatkRGKRRFLKIRKLKQNLprfkkLAAVMNNGL--ENRLNTFVEgLSGGQRQALSFLMATIERP 171
Cdd:PRK15134 376 NPRLNVlqiiEEGL-----RVHQPTLSAAQREQQV-----IAVMEEVGLdpETRHRYPAE-FSGGQRQRIAIARALILKP 444
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 172 DILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK15134 445 SLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEV 504
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
25-213 |
6.94e-11 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 60.82 E-value: 6.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLL------NTIAGSLRPDSG--FLLHNGHDITKMSEEKRTQfIGRVFqdPKMG 96
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLkclnrmNELESEVRVEGRveFFNQNIYERRVNLNRLRRQ-VSMVH--PKPN 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 97 TAPrMTVAENLLLATKR-GKRRFLKIRKLKQNLPRfkklAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILL 175
Cdd:PRK14258 99 LFP-MSVYDNVAYGVKIvGWRPKLEIDDIVESALK----DADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLL 173
|
170 180 190
....*....|....*....|....*....|....*...
gi 489745462 176 LDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHM 213
Cdd:PRK14258 174 MDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
25-232 |
9.32e-11 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 61.89 E-value: 9.32e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTAP-RMTV 103
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSlRMNL 1380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 -------AENLLLATKrgkrrflkirklkqnLPRFKKLAAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLL 176
Cdd:TIGR00957 1381 dpfsqysDEEVWWALE---------------LAHLKTFVSALPDKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVL 1445
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 177 DEHTAALDPHTsENLLAVTDQQIKENkLTALMITHHMEDALKYgNRLLVLKDGKVK 232
Cdd:TIGR00957 1446 DEATAAVDLET-DNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEVA 1498
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-250 |
9.37e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 61.53 E-value: 9.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPdsgfllhnghditkmSEEKRTQFIGRVFQDPKMGTAPRMTV 103
Cdd:PLN03232 631 PTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSH---------------AETSSVVIRGSVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGKRRFLK---IRKLKQNLPRF--KKLAAVMNNGLEnrlntfvegLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:PLN03232 696 RENILFGSDFESERYWRaidVTALQHDLDLLpgRDLTEIGERGVN---------ISGGQKQRVSMARAVYSNSDIYIFDD 766
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489745462 179 HTAALDPHTSENllaVTDQQIKE--NKLTALMITHHMEdALKYGNRLLVLKDGKVKADINEQEKQnlKVSDLYK 250
Cdd:PLN03232 767 PLSALDAHVAHQ---VFDSCMKDelKGKTRVLVTNQLH-FLPLMDRIILVSEGMIKEEGTFAELS--KSGSLFK 834
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
6-191 |
1.36e-10 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 60.68 E-value: 1.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKttvKTADGEivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfllhnghdITKMSEEKRtqf 85
Cdd:PRK15064 320 LEVENLT---KGFDNG--PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG--------TVKWSENAN--- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMGTAPRMTVAENLLLATKRGKRRfLKIRklkqnlprfkklaAVMNNGL--ENRLNTFVEGLSGGQRQALSF 163
Cdd:PRK15064 384 IGYYAQDHAYDFENDLTLFDWMSQWRQEGDDE-QAVR-------------GTLGRLLfsQDDIKKSVKVLSGGEKGRMLF 449
|
170 180
....*....|....*....|....*...
gi 489745462 164 LMATIERPDILLLDEHTAALDPHTSENL 191
Cdd:PRK15064 450 GKLMMQKPNVLVMDEPTNHMDMESIESL 477
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
5-229 |
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: 61.18 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVkttVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDI-TKMSEekrt 83
Cdd:TIGR01257 1937 ILRLNEL---TKVYSGTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISD---- 2009
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 qfigrVFQDpkMGTAPRMTVAENLLLAtkrgkRRFLKIRKLKQNLPRfKKLAAVMNNGLENR-LNTFVEGL----SGGQR 158
Cdd:TIGR01257 2010 -----VHQN--MGYCPQFDAIDDLLTG-----REHLYLYARLRGVPA-EEIEKVANWSIQSLgLSLYADRLagtySGGNK 2076
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 159 QALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDG 229
Cdd:TIGR01257 2077 RKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-225 |
1.59e-10 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 60.59 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 33 IKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLhnghditkmSEEK---RTQFIGrvfqdpkmgTAPRMTVAENLLL 109
Cdd:PRK13409 362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVD---------PELKisyKPQYIK---------PDYDGTVEDLLRS 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 110 ATKRGKRRFLK---IRKLkqnlprfkklaavmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDph 186
Cdd:PRK13409 424 ITDDLGSSYYKseiIKPL----------------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD-- 485
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 489745462 187 tSENLLAVTD---QQIKENKLTALMITH--HMEDALkyGNRLLV 225
Cdd:PRK13409 486 -VEQRLAVAKairRIAEEREATALVVDHdiYMIDYI--SDRLMV 526
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
24-251 |
1.75e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 60.50 E-value: 1.75e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EEKRTQFiGRVFQDPKMGTAprmT 102
Cdd:PRK10789 329 PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQlDSWRSRL-AVVSQTPFLFSD---T 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLL----ATKrgkrrflkirklkQNLPRFKKLAAVMNNGLenRL----NTFV--EG--LSGGQRQALSFLMATIER 170
Cdd:PRK10789 405 VANNIALgrpdATQ-------------QEIEHVARLASVHDDIL--RLpqgyDTEVgeRGvmLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 171 PDILLLDEHTAALDPHTSENLLAVTDQQIKENkltALMITHHMEDALKYGNRLLVLKDGKV--KADINEQEKQNLKVSDL 248
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGR---TVIISAHRLSALTEASEILVMQHGHIaqRGNHDQLAQQSGWYRDM 546
|
...
gi 489745462 249 YKY 251
Cdd:PRK10789 547 YRY 549
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
24-231 |
1.76e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.76e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGslrpdsgfllhnghDITKMseEKRTQFIGRVFQDPKMGTAPRMTV 103
Cdd:TIGR00957 652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLA--------------EMDKV--EGHVHMKGSVAYVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAvmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:TIGR00957 716 RENILFGKALNEKYYQQVLEACALLPDLEILPS----GDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 184 DPHTSENLL--AVTDQQIKENKlTALMITHHMEdALKYGNRLLVLKDGKV 231
Cdd:TIGR00957 792 DAHVGKHIFehVIGPEGVLKNK-TRILVTHGIS-YLPQVDVIIVMSGGKI 839
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-184 |
1.78e-10 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 59.42 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVktadgEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGS--LRPDSGFLLHNGHDITKMSEEKR 82
Cdd:PRK09580 1 MLSIKDLHVSV-----EDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 T-QFIGRVFQDPkmgtAPRMTVAENLLLATKRGkrrflKIRKLKQNLP--RFK---------KLAAVMNNGLENRLNtfv 150
Cdd:PRK09580 76 AgEGIFMAFQYP----VEIPGVSNQFFLQTALN-----AVRSYRGQEPldRFDfqdlmeekiALLKMPEDLLTRSVN--- 143
|
170 180 190
....*....|....*....|....*....|....*
gi 489745462 151 EGLSGGQRQALSFL-MATIErPDILLLDEHTAALD 184
Cdd:PRK09580 144 VGFSGGEKKRNDILqMAVLE-PELCILDESDSGLD 177
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
4-230 |
4.06e-10 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 59.05 E-value: 4.06e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVKTTVKTADGEiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAG----SLRPDSGFLLHNGHDITKMSE 79
Cdd:PRK15093 2 PLLDIRNLTIEFKTSDGW-VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDIDLLRLSP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 80 EKRTQFIGR----VFQDPKMGTAPRMTVAENLLLA----TKRGK--RRF-LKIRKLKQNLPR--FKKLAAVMNNglenrl 146
Cdd:PRK15093 81 RERRKLVGHnvsmIFQEPQSCLDPSERVGRQLMQNipgwTYKGRwwQRFgWRKRRAIELLHRvgIKDHKDAMRS------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 147 ntFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVL 226
Cdd:PRK15093 155 --FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVL 232
|
....
gi 489745462 227 KDGK 230
Cdd:PRK15093 233 YCGQ 236
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
33-233 |
8.42e-10 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 57.64 E-value: 8.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 33 IKAGDFITIIGTNGAGKSTLLNTIAGSLrPDSGFLLHNGHDITKM------------SEEKRTQFIGRVFQ--DPKMGTA 98
Cdd:PRK03695 19 VRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWsaaelarhraylSQQQTPPFAMPVFQylTLHQPDK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 PRMTVAENLLlatkrgkrrflkiRKLKQNLprfkklaavmnnGLENRLNTFVEGLSGGQ----RQALSFLMATierPDI- 173
Cdd:PRK03695 98 TRTEAVASAL-------------NEVAEAL------------GLDDKLGRSVNQLSGGEwqrvRLAAVVLQVW---PDIn 149
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 174 -----LLLDEHTAALDPhTSENLLavtDQQIKE---NKLTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:PRK03695 150 pagqlLLLDEPMNSLDV-AQQAAL---DRLLSElcqQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLA 213
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
6-228 |
1.40e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 58.12 E-value: 1.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVKTTVKTADGeiVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSG-FLLHNGHDITKMSEEKRTQ 84
Cdd:PTZ00265 383 IQFKNVRFHYDTRKD--VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGdIIINDSHNLKDINLKWWRS 460
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 85 FIGRVFQDPKM---------------------------------------GTAPRMTVAENL-LLATKRGKRRFLKIRKL 124
Cdd:PTZ00265 461 KIGVVSQDPLLfsnsiknnikyslyslkdlealsnyynedgndsqenknkRNSCRAKCAGDLnDMSNTTDSNELIEMRKN 540
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 125 KQNLP-------RFKKLAAVMNNGLENRLNTFV----EGLSGGQRQALSFLMATIERPDILLLDEHTAALDpHTSENLLA 193
Cdd:PTZ00265 541 YQTIKdsevvdvSKKVLIHDFVSALPDKYETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLD-NKSEYLVQ 619
|
250 260 270
....*....|....*....|....*....|....*
gi 489745462 194 VTDQQIKENKLTALMITHHMEDALKYGNRLLVLKD 228
Cdd:PTZ00265 620 KTINNLKGNENRITIIIAHRLSTIRYANTIFVLSN 654
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
3-237 |
2.20e-09 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 57.21 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVktTVKTADGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLlhnghDItkmseEKR 82
Cdd:PRK13545 19 KPFDKLKDL--FFRSKDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTV-----DI-----KGS 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 TQFIGrvfqdPKMGTAPRMTVAENLLLatkRGKRRFLKIRKLKQNLPRFKKLAAVmnnglENRLNTFVEGLSGGQRQALS 162
Cdd:PRK13545 87 AALIA-----ISSGLNGQLTGIENIEL---KGLMMGLTKEKIKEIIPEIIEFADI-----GKFIYQPVKTYSSGMKSRLG 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 163 FLMATIERPDILLLDEHTAALDPHTSENLLAVTDqQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVK--ADINE 237
Cdd:PRK13545 154 FAISVHINPDILVIDEALSVGDQTFTKKCLDKMN-EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKeyGDIKE 229
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
24-191 |
3.01e-09 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 3.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGhDITkmseekrtqfIGRVFQDPkmgtaPRMT- 102
Cdd:PRK11147 17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQ-DLI----------VARLQQDP-----PRNVe 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 ------VAENLLLATKRGKR-----RFLKIRKLKQNLPRFKKLAAVM--NNG--LENRLNTFVE-----------GLSGG 156
Cdd:PRK11147 81 gtvydfVAEGIEEQAEYLKRyhdisHLVETDPSEKNLNELAKLQEQLdhHNLwqLENRINEVLAqlgldpdaalsSLSGG 160
|
170 180 190
....*....|....*....|....*....|....*.
gi 489745462 157 -QRQAlSFLMATIERPDILLLDEHTAALDPHTSENL 191
Cdd:PRK11147 161 wLRKA-ALGRALVSNPDVLLLDEPTNHLDIETIEWL 195
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
5-229 |
3.82e-09 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 56.66 E-value: 3.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 5 ILELKDVKTTVKTADGEIVpILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGslRPDSGFL-----LHNGHDITKmSE 79
Cdd:TIGR00956 759 IFHWRNLTYEVKIKKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVItggdrLVNGRPLDS-SF 834
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 80 EKRTQFIGRvfQDPKMGTAprmTVAENLllatkrgkrRFLKIRKLKQNLPRFKK---LAAVMN-NGLENRLNTFV----E 151
Cdd:TIGR00956 835 QRSIGYVQQ--QDLHLPTS---TVRESL---------RFSAYLRQPKSVSKSEKmeyVEEVIKlLEMESYADAVVgvpgE 900
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 152 GLSGGQRQALSFLMATIERPDILL-LDEHTAALDPHTSENL------LAVTDQqikenkltALMITHHMEDALKYG--NR 222
Cdd:TIGR00956 901 GLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAWSIcklmrkLADHGQ--------AILCTIHQPSAILFEefDR 972
|
....*..
gi 489745462 223 LLVLKDG 229
Cdd:TIGR00956 973 LLLLQKG 979
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
26-232 |
4.63e-09 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 55.59 E-value: 4.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGhDITKMSeekrtqfigrvfqdPKMGTAPRMTVAE 105
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIA--------------ISAGLSGQLTGIE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 N-----LLLATKRGkrrflKIRKLKQNLPRFKKLAAVMNNGlenrlntfVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PRK13546 105 NiefkmLCMGFKRK-----EIKAMTPKIIEFSELGEFIYQP--------VKKYSSGMRAKLGFSINITVNPDILVIDEAL 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 489745462 181 AALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVK 232
Cdd:PRK13546 172 SVGDQTFAQKCLDKI-YEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLK 222
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
19-229 |
4.85e-09 |
|
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: 55.30 E-value: 4.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 19 DGEIVPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTA 98
Cdd:cd03288 30 ENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQDPILFSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 prmTVAENLLLATKRGKRRF---LKIRKLK---QNLPrfKKLAAVMNNGLENrlntfvegLSGGQRQALSFLMATIERPD 172
Cdd:cd03288 110 ---SIRFNLDPECKCTDDRLweaLEIAQLKnmvKSLP--GGLDAVVTEGGEN--------FSVGQRQLFCLARAFVRKSS 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 173 ILLLDEHTAALDPHTsENLL------AVTDQqikenklTALMITHHMEDALKyGNRLLVLKDG 229
Cdd:cd03288 177 ILIMDEATASIDMAT-ENILqkvvmtAFADR-------TVVTIAHRVSTILD-ADLVLVLSRG 230
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
24-211 |
6.08e-09 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 55.90 E-value: 6.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfllhnghditkmseEKRTQ---FIGRVFQDPKMGtaPR 100
Cdd:PRK11819 21 QILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG--------------EARPApgiKVGYLPQEPQLD--PE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 101 MTVAENLLLA---TKRGKRRFLKI-RKLKQNLPRFKKLAAVM---------NNG--LENRL------------NTFVEGL 153
Cdd:PRK11819 85 KTVRENVEEGvaeVKAALDRFNEIyAAYAEPDADFDALAAEQgelqeiidaADAwdLDSQLeiamdalrcppwDAKVTKL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 154 SGGQRQ--ALSFLMatIERPDILLLDEHTAALDPHTSENLlavtDQQIKENKLTALMITH 211
Cdd:PRK11819 165 SGGERRrvALCRLL--LEKPDMLLLDEPTNHLDAESVAWL----EQFLHDYPGTVVAVTH 218
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
24-217 |
8.42e-09 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 54.19 E-value: 8.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSL--RPDSGFLlhnghditkmseekrtqfigrVFQDPKMGtaPRM 101
Cdd:COG2401 44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCV---------------------DVPDNQFG--REA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLATKrgkrrflkirklkqnlprFKKLAAVMNN-GLE---NRLNTFVEgLSGGQRQALSFLMATIERPDILLLD 177
Cdd:COG2401 101 SLIDAIGRKGD------------------FKDAVELLNAvGLSdavLWLRRFKE-LSTGQKFRFRLALLLAERPKLLVID 161
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 489745462 178 EHTAALDPHTSEnLLAVTDQQI-KENKLTALMITHHME--DAL 217
Cdd:COG2401 162 EFCSHLDRQTAK-RVARNLQKLaRRAGITLVVATHHYDviDDL 203
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
63-228 |
1.04e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 63 DSGFLLHNGHDITKMSEEKRTQFIGRVFQDPKMGTaprMTVAENLllatkrgkrRFLKIRKLKQNLPRFKKLAAV--MNN 140
Cdd:PTZ00265 1275 NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFN---MSIYENI---------KFGKEDATREDVKRACKFAAIdeFIE 1342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 141 GLENRLNTFV----EGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHtSENLLAVTDQQIKENKLTALMITHHMEDA 216
Cdd:PTZ00265 1343 SLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSN-SEKLIEKTIVDIKDKADKTIITIAHRIAS 1421
|
170
....*....|..
gi 489745462 217 LKYGNRLLVLKD 228
Cdd:PTZ00265 1422 IKRSDKIVVFNN 1433
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
30-228 |
2.33e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.25 E-value: 2.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 30 DLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQD-------PKMGTAPRmT 102
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRnntdmlsPGEDDTGR-T 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATKrgkrrflkirklkqNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQ-RQALsFLMATIERPDILLLDEHTA 181
Cdd:PRK10938 102 TAEIIQDEVK--------------DPARCEQLAQQF--GITALLDRRFKYLSTGEtRKTL-LCQALMSEPDLLILDEPFD 164
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 489745462 182 ALDpHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLKD 228
Cdd:PRK10938 165 GLD-VASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLAD 210
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
154-234 |
2.39e-08 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 53.97 E-value: 2.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 154 SGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDGKVKA 233
Cdd:NF000106 146 SGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGA-TVLLTTQYMEEAEQLAHELTVIDRGRVIA 224
|
.
gi 489745462 234 D 234
Cdd:NF000106 225 D 225
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
32-211 |
2.62e-08 |
|
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: 54.02 E-value: 2.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 32 KIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfllhnghditKMSEEKRT----QFIGRVFQdpkmgtaprMTVAEnl 107
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEG----------EVDEDLKIsykpQYISPDYD---------GTVEE-- 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 108 LLATKRGKR---RFLK---IRKLkqnlprfkklaavmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTA 181
Cdd:COG1245 421 FLRSANTDDfgsSYYKteiIKPL----------------GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 484
|
170 180 190
....*....|....*....|....*....|...
gi 489745462 182 ALDphtSENLLAVTD---QQIKENKLTALMITH 211
Cdd:COG1245 485 HLD---VEQRLAVAKairRFAENRGKTAMVVDH 514
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
23-230 |
2.74e-08 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 53.97 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 23 VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDIT-KMSEEKRTQFIGRVFQDpkMGTAPRM 101
Cdd:PRK10982 11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQE--LNLVLQR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLATKRGKRRFLKIRKLKQNLPR-FKKLaavmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PRK10982 89 SVMDNMWLGRYPTKGMFVDQDKMYRDTKAiFDEL------DIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 489745462 181 AALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGK 230
Cdd:PRK10982 163 SSLTEKEVNHLFTII-RKLKERGCGIVYISHKMEEIFQLCDEITILRDGQ 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
26-185 |
2.78e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 53.98 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDitkMSEEK-RTQFIGRVfqdpkmgtA------ 98
Cdd:NF033858 17 LDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGD---MADARhRRAVCPRI--------Aympqgl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 -----PRMTVAENL-----LLATKRGKRRfLKIRKLKQ--NLPRFKKLAAvmnnglenrlntfveG-LSGGQRQALSFLM 165
Cdd:NF033858 86 gknlyPTLSVFENLdffgrLFGQDAAERR-RRIDELLRatGLAPFADRPA---------------GkLSGGMKQKLGLCC 149
|
170 180
....*....|....*....|
gi 489745462 166 ATIERPDILLLDEHTAALDP 185
Cdd:NF033858 150 ALIHDPDLLILDEPTTGVDP 169
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
28-231 |
1.23e-07 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 52.17 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 28 GIDLKIKagdfITIIGTNGAGKSTLLNTIAGSLRPDSgfllhnghditkmseekrtqfiGRVFQDPKMgtapRMTV---- 103
Cdd:PLN03073 531 GIDLDSR----IAMVGPNGIGKSTILKLISGELQPSS----------------------GTVFRSAKV----RMAVfsqh 580
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 -------AENLLLATKRGKRRFLKiRKLKQNLPRFkklaAVMNNGLENRLNTfvegLSGGQRQALSFLMATIERPDILLL 176
Cdd:PLN03073 581 hvdgldlSSNPLLYMMRCFPGVPE-QKLRAHLGSF----GVTGNLALQPMYT----LSGGQKSRVAFAKITFKKPHILLL 651
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 177 DEHTAALDPHTSENLLavtdQQIKENKLTALMITHhmEDALKYG--NRLLVLKDGKV 231
Cdd:PLN03073 652 DEPSNHLDLDAVEALI----QGLVLFQGGVLMVSH--DEHLISGsvDELWVVSEGKV 702
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
24-232 |
1.26e-07 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 52.43 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfllhnGHDITKmseekrtqfiGRVFQDPKMGTAPRMTV 103
Cdd:PLN03130 631 PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD-----ASVVIR----------GTVAYVPQVSWIFNATV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLATKRGKRRFLK---IRKLKQNLprfkklaAVMNNGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:PLN03130 696 RDNILFGSPFDPERYERaidVTALQHDL-------DLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 489745462 181 AALDPHTSENllaVTDQQIKE--NKLTALMITHHMEdALKYGNRLLVLKDGKVK 232
Cdd:PLN03130 769 SALDAHVGRQ---VFDKCIKDelRGKTRVLVTNQLH-FLSQVDRIILVHEGMIK 818
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
3-231 |
2.59e-07 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 51.01 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKTTVKTADGEI------VPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITK 76
Cdd:PRK10261 311 EPILQVRNLVTRFPLRSGLLnrvtreVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDT 390
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 77 MSEEK------RTQFIgrvFQDPKMGTAPRMTVAENLLLAtkrgkrrfLKIRKLKQNLPRFKKLAAVMNN-GL--ENRLN 147
Cdd:PRK10261 391 LSPGKlqalrrDIQFI---FQDPYASLDPRQTVGDSIMEP--------LRVHGLLPGKAAAARVAWLLERvGLlpEHAWR 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 148 tFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDALKYGNRLLVLK 227
Cdd:PRK10261 460 -YPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMY 538
|
....
gi 489745462 228 DGKV 231
Cdd:PRK10261 539 LGQI 542
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
29-241 |
3.43e-07 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 50.59 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 29 IDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPD-SGFLLHNGHDI-TKMSEEKRTQFIGRVFQDPKM-GTAPRMTVAE 105
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGKPVdIRNPAQAIRAGIAMVPEDRKRhGIVPILGVGK 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 106 NLLLATKRgkrRFLKIRKLKQNlprfKKLAAVMNNGLENRLNTF-----VEGLSGGQRQALSFLMATIERPDILLLDEHT 180
Cdd:TIGR02633 359 NITLSVLK---SFCFKMRIDAA----AELQIIGSAIQRLKVKTAspflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPT 431
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489745462 181 AALDPHTSENLLAVTDQQIKENkLTALMITHHMEDALKYGNRLLVLKDGKVKAD-INEQEKQ 241
Cdd:TIGR02633 432 RGVDVGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKLKGDfVNHALTQ 492
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
3-229 |
3.47e-07 |
|
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: 49.16 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKTTVKTADGEIvPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGslRPDSGF----LLHNGHDITKms 78
Cdd:cd03232 1 GSVLTWKNLNYTVPVKGGKR-QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG--RKTAGVitgeILINGRPLDK-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 79 eeKRTQFIGRVFQDPKMgtAPRMTVAENLLLATkrgkrrflKIRklkqnlprfkklaavmnnglenrlntfveGLSGGQR 158
Cdd:cd03232 76 --NFQRSTGYVEQQDVH--SPNLTVREALRFSA--------LLR-----------------------------GLSVEQR 114
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 159 QALSFLMATIERPDILLLDEHTAALDPHTSENL------LAVTDQqikenkltALMITHHM--EDALKYGNRLLVLKDG 229
Cdd:cd03232 115 KRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIvrflkkLADSGQ--------AILCTIHQpsASIFEKFDRLLLLKRG 185
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
25-231 |
1.07e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMS-EEKRTQFiGRVFQDPKMGTAprmTV 103
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGlRELRRQF-SMIPQDPVLFDG---TV 1400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENL---LLATKRGKRRFLKIRKLKQNLprfkklaAVMNNGLENRLntfVEG---LSGGQRQALSFLMATIER-PDILLL 176
Cdd:PTZ00243 1401 RQNVdpfLEASSAEVWAALELVGLRERV-------ASESEGIDSRV---LEGgsnYSVGQRQLMCMARALLKKgSGFILM 1470
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 177 DEHTAALDPhtsenllaVTDQQIKENKLTA------LMITHHMEDALKYgNRLLVLKDGKV 231
Cdd:PTZ00243 1471 DEATANIDP--------ALDRQIQATVMSAfsaytvITIAHRLHTVAQY-DKIIVMDHGAV 1522
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
29-185 |
1.15e-06 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 49.35 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 29 IDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSG--FLLhnGHDItkmseekrtqfigrvfqDPK-MGTAPR---M- 101
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGeaWLF--GQPV-----------------DAGdIATRRRvgyMs 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 ---------TVAENLLL--------ATKRGKRrflkirkLKQNLPRFkklaavmnnGLENRLNTFVEGLSGGQRQALSFL 164
Cdd:NF033858 346 qafslygelTVRQNLELharlfhlpAAEIAAR-------VAEMLERF---------DLADVADALPDSLPLGIRQRLSLA 409
|
170 180
....*....|....*....|.
gi 489745462 165 MATIERPDILLLDEHTAALDP 185
Cdd:NF033858 410 VAVIHKPELLILDEPTSGVDP 430
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
3-191 |
1.16e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 49.18 E-value: 1.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVKTTVktaDGEIvpILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfLLHNGhdiTKMSEEKR 82
Cdd:PRK11147 317 KIVFEMENVNYQI---DGKQ--LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG-RIHCG---TKLEVAYF 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 83 TQFigRVFQDPKmgtaprMTVAENLllatKRGKRRflkirklkqnlprfkklaaVMNNGLEN--------------RLNT 148
Cdd:PRK11147 388 DQH--RAELDPE------KTVMDNL----AEGKQE-------------------VMVNGRPRhvlgylqdflfhpkRAMT 436
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 489745462 149 FVEGLSGGQRQALsfLMATI-ERP-DILLLDEHTAALDPHTSENL 191
Cdd:PRK11147 437 PVKALSGGERNRL--LLARLfLKPsNLLILDEPTNDLDVETLELL 479
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
21-189 |
1.21e-06 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 49.39 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 21 EIVP--ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGfllhnghditKMSEEKRtqfIGRVFQDPKMGTA 98
Cdd:PTZ00243 669 ELEPkvLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEG----------RVWAERS---IAYVPQQAWIMNA 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 99 prmTVAENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAvmnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDE 178
Cdd:PTZ00243 736 ---TVRGNILFFDEEDAARLADAVRVSQLEADLAQLGG----GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
|
170
....*....|.
gi 489745462 179 HTAALDPHTSE 189
Cdd:PTZ00243 809 PLSALDAHVGE 819
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
4-216 |
1.29e-06 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.86 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 4 PILELKDVktTVKTADGeivPILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSlRPdSGFllhnGHDITKMSEEKRT 83
Cdd:PRK10938 259 PRIVLNNG--VVSYNDR---PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGD-HP-QGY----SNDLTLFGRRRGS 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 84 --------QFIGRV----FQDPKMGTAPRmtvaeNLLLATkrgkrrFLKIRKLKQNLP-RFKKLAAVMNN--GLENRL-N 147
Cdd:PRK10938 328 getiwdikKHIGYVssslHLDYRVSTSVR-----NVILSG------FFDSIGIYQAVSdRQQKLAQQWLDilGIDKRTaD 396
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489745462 148 TFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALMITHHMEDA 216
Cdd:PRK10938 397 APFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAEDA 465
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
34-184 |
2.01e-06 |
|
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213203 [Multi-domain] Cd Length: 255 Bit Score: 47.75 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 34 KAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGhDITKMSEEKRTQFIGRVFQDPKMGTAPRMTVAENLLLATKR 113
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPP-DWDEILDEFRGSELQNYFTKLLEGDVKVIVKPQYVDLIPKA 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 114 GKRRFLKIRKLKQNLPRFKKLAAVMnnGLENRLNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALD 184
Cdd:cd03236 103 VKGKVGELLKKKDERGKLDELVDQL--ELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLD 171
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
39-218 |
7.00e-06 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 45.63 E-value: 7.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 39 ITII-GTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTqFIGRvfqdpKMGTAPRMTVAENLLLatkrgkrr 117
Cdd:PRK13541 28 ITYIkGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCT-YIGH-----NLGLKLEMTVFENLKF-------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 118 FLKIRKLKQNLPrfkklAAVMNNGLENRLNTFVEGLSGGQRQ--ALSFLMATieRPDILLLDEHTAALDPHTSE---NLL 192
Cdd:PRK13541 94 WSEIYNSAETLY-----AAIHYFKLHDLLDEKCYSLSSGMQKivAIARLIAC--QSDLWLLDEVETNLSKENRDllnNLI 166
|
170 180
....*....|....*....|....*.
gi 489745462 193 AvtdqqIKENKLTALMITHHMEDALK 218
Cdd:PRK13541 167 V-----MKANSGGIVLLSSHLESSIK 187
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-240 |
7.32e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 46.54 E-value: 7.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 24 PILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDI-TKMSEEKRTQFIGRVFQDPKM-GTAPRM 101
Cdd:PRK10762 266 PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVvTRSPQDGLANGIVYISEDRKRdGLVLGM 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLA-----TKRGKRrfLKIRKLKQNLPRFKKLAAVMNNGLENRLNTfvegLSGGQRQALSFLMATIERPDILLL 176
Cdd:PRK10762 346 SVKENMSLTalryfSRAGGS--LKHADEQQAVSDFIRLFNIKTPSMEQAIGL----LSGGNQQKVAIARGLMTRPKVLIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489745462 177 DEHTAALDPHTSENLLAVTDqQIKENKLTALMITHHMEDALKYGNRLLVLKDGKVKADIN----EQEK 240
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLIN-QFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTreqaTQEK 486
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
6-252 |
7.99e-06 |
|
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: 46.00 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 6 LELKDVktTVKTADGEIVpILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDsGFLLHNGHDITKMSEEKRTQF 85
Cdd:cd03289 3 MTVKDL--TAKYTEGGNA-VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 86 IGRVFQDPKMGTAprmTVAENLLLATKRGKRRFLKIRK---LKQNLPRFK-KLAAVMNNGlenrlnTFVegLSGGQRQAL 161
Cdd:cd03289 79 FGVIPQKVFIFSG---TFRKNLDPYGKWSDEEIWKVAEevgLKSVIEQFPgQLDFVLVDG------GCV--LSHGHKQLM 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 162 SFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKEnkLTALMITHHMEdALKYGNRLLVLKDGKVK------ADI 235
Cdd:cd03289 148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFAD--CTVILSEHRIE-AMLECQRFLVIEENKVRqydsiqKLL 224
|
250
....*....|....*....
gi 489745462 236 NEQE--KQNLKVSDLYKYF 252
Cdd:cd03289 225 NEKShfKQAISPSDRLKLF 243
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
25-65 |
1.69e-05 |
|
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: 45.31 E-value: 1.69e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSG 65
Cdd:TIGR03719 337 LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSG 377
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
41-65 |
1.98e-05 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 45.11 E-value: 1.98e-05
10 20
....*....|....*....|....*
gi 489745462 41 IIGTNGAGKSTLLNTIAGSLRPDSG 65
Cdd:PRK11819 355 IIGPNGAGKSTLFKMITGQEQPDSG 379
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
26-213 |
2.97e-05 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 44.10 E-value: 2.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLlhnghDITKMSEEK--RTQFIGRVFQDPKMGTAPRMTV 103
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKI-----SILGQPTRQalQKNLVAYVPQSEEVDWSFPVLV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 aENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAVmnNGLENRLNTFVEgLSGGQRQALSFLMATIERPDILLLDEHTAAL 183
Cdd:PRK15056 98 -EDVVMMGRYGHMGWLRRAKKRDRQIVTAALARV--DMVEFRHRQIGE-LSGGQKKRVFLARAIAQQGQVILLDEPFTGV 173
|
170 180 190
....*....|....*....|....*....|
gi 489745462 184 DPHTSENLLAVTDQQIKENKlTALMITHHM 213
Cdd:PRK15056 174 DVKTEARIISLLRELRDEGK-TMLVSTHNL 202
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
36-215 |
6.50e-05 |
|
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: 41.98 E-value: 6.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 36 GDFITIIGTNGAGKSTLLNTIAGSLRPDS-GFLLHNGHDITKMSEEKRTQFIGrvfqdpkmgtaprmtvaenlllatkrg 114
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGgGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 115 krrflkirklkqnlprfkklaavmnnglenrlNTFVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLA- 193
Cdd:smart00382 55 --------------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLl 102
|
170 180
....*....|....*....|....*.
gi 489745462 194 ----VTDQQIKENKLTALMITHHMED 215
Cdd:smart00382 103 eelrLLLLLKSEKNLTVILTTNDEKD 128
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-184 |
7.70e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 43.68 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGslRPDSGFLlhNGhDITKMSEEKRTQFIGRV--FQDPKMGTAPRMT 102
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYI--EG-DIRISGFPKKQETFARIsgYCEQNDIHSPQVT 969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 103 VAENLLLATkrgkrrFLKIRK--LKQNLPRFkkLAAVMN-NGLENRLNTFV-----EGLSGGQRQALSFLMATIERPDIL 174
Cdd:PLN03140 970 VRESLIYSA------FLRLPKevSKEEKMMF--VDEVMElVELDNLKDAIVglpgvTGLSTEQRKRLTIAVELVANPSII 1041
|
170
....*....|
gi 489745462 175 LLDEHTAALD 184
Cdd:PLN03140 1042 FMDEPTSGLD 1051
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
25-65 |
1.03e-04 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 43.23 E-value: 1.03e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSG 65
Cdd:PRK10636 327 ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG 367
|
|
| ABC_sbcCD |
cd03279 |
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ... |
41-229 |
1.47e-04 |
|
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.
Pssm-ID: 213246 [Multi-domain] Cd Length: 213 Bit Score: 41.87 E-value: 1.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 41 IIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSEEKRTQFIGRVFQdpkmgtaprmtvaenlllatkRGKRRFLK 120
Cdd:cd03279 33 ICGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQ---------------------LGGKKYRV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 121 IRKLKQNLPRFKKLAAVMNNGLENRLNTFVEGLSGGQ--RQALSFLMATIE--------RPDILLLDEHTAALDPHTSEN 190
Cdd:cd03279 92 ERSRGLDYDQFTRIVLLPQGEFDRFLARPVSTLSGGEtfLASLSLALALSEvlqnrggaRLEALFIDEGFGTLDPEALEA 171
|
170 180 190
....*....|....*....|....*....|....*....
gi 489745462 191 LLAVTDQQIKENKLTaLMITHHMEDALKYGNRLLVLKDG 229
Cdd:cd03279 172 VATALELIRTENRMV-GVISHVEELKERIPQRLEVIKTP 209
|
|
| SbcC |
COG0419 |
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair]; |
39-212 |
1.61e-04 |
|
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
Pssm-ID: 440188 [Multi-domain] Cd Length: 204 Bit Score: 41.53 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 39 ITIIGTNGAGKSTLLNTIA----GSLRPDSGF---LLHNGHDITKMS-----EEKR---TQFIGRVFQDPKMGTAPRMTV 103
Cdd:COG0419 26 NLIVGPNGAGKSTILEAIRyalyGKARSRSKLrsdLINVGSEEASVElefehGGKRyriERRQGEFAEFLEAKPSERKEA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 104 AENLLLaTKRGKRRFLKIRKLKQNLPRFKKLAAVMNNGLENRLNTF-----VEGLSGGQRQALSflMATIERpdiLLLDe 178
Cdd:COG0419 106 LKRLLG-LEIYEELKERLKELEEALESALEELAELQKLKQEILAQLsgldpIETLSGGERLRLA--LADLLS---LILD- 178
|
170 180 190
....*....|....*....|....*....|....*
gi 489745462 179 hTAALDPHTSENLL-AVTDQQIkenkltalmITHH 212
Cdd:COG0419 179 -FGSLDEERLERLLdALEELAI---------ITHV 203
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
2-239 |
1.83e-04 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 42.46 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 2 TKPILELKDVKTTvktaDGEIVpilKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFLLHNGHDITKMSE-- 79
Cdd:PRK09700 262 HETVFEVRNVTSR----DRKKV---RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPld 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 80 --EKRTQFIGRVFQDpkMGTAPRMTVAENLLLAtkrgkrRFLKIRKLKQNLPRF-----KKLAAVMNNGLE---NRLNTF 149
Cdd:PRK09700 335 avKKGMAYITESRRD--NGFFPNFSIAQNMAIS------RSLKDGGYKGAMGLFhevdeQRTAENQRELLAlkcHSVNQN 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 150 VEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKlTALMITHHMEDALKYGNRLLVLKDG 229
Cdd:PRK09700 407 ITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEG 485
|
250
....*....|
gi 489745462 230 KVKADINEQE 239
Cdd:PRK09700 486 RLTQILTNRD 495
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
33-184 |
5.58e-04 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 40.95 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 33 IKAGDFITIIGTNGAGKSTLLNTIAGSLRPD-----------------SGFLLHNghDITKMSEEK-----RTQFIGRVf 90
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNlgdyeeepswdevlkrfRGTELQN--YFKKLYNGEikvvhKPQYVDLI- 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 91 qdPKmgtAPRMTVAENLLLATKRGKRRFLkIRKLkqnlprfkklaavmnnGLENRLNTFVEGLSGG--QRQALSflmATI 168
Cdd:PRK13409 173 --PK---VFKGKVRELLKKVDERGKLDEV-VERL----------------GLENILDRDISELSGGelQRVAIA---AAL 227
|
170
....*....|....*..
gi 489745462 169 ER-PDILLLDEHTAALD 184
Cdd:PRK13409 228 LRdADFYFFDEPTSYLD 244
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-231 |
5.92e-04 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 40.80 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 3 KPILELKDVkttvkTADGeivpiLKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGsLRP-DSGFLLHNGHDITKMSEEK 81
Cdd:PRK15439 266 APVLTVEDL-----TGEG-----FRNISLEVRAGEILGLAGVVGAGRTELAETLYG-LRPaRGGRIMLNGKEINALSTAQ 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 82 RTQfIGRVF--QDPKMG----TAPrmtVAENLLLATKRGKRRFLKIRKLKQNLPRFKKLAAVMNNGLENRlntfVEGLSG 155
Cdd:PRK15439 335 RLA-RGLVYlpEDRQSSglylDAP---LAWNVCALTHNRRGFWIKPARENAVLERYRRALNIKFNHAEQA----ARTLSG 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489745462 156 GQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTdQQIKENKLTALMITHHMEDALKYGNRLLVLKDGKV 231
Cdd:PRK15439 407 GNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
25-208 |
6.04e-04 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 40.98 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 25 ILKGIDLKIKAGDFITIIGTNGAGKSTLLNTIAGSLRPD---SGFLLHNGHDITKMSEEKRTQFIGRvfQDPKMGTaprM 101
Cdd:PLN03140 180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRKTSAYISQ--NDVHVGV---M 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 102 TVAENLLLATK---RGKRRFL---KIRKLKQN--LPR-----FKKLAAVmnNGLENRLNT-------------------- 148
Cdd:PLN03140 255 TVKETLDFSARcqgVGTRYDLlseLARREKDAgiFPEaevdlFMKATAM--EGVKSSLITdytlkilgldickdtivgde 332
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 149 FVEGLSGGQRQALSFLMATIERPDILLLDEHTAALDPHTSENLLAVTDQQIKENKLTALM 208
Cdd:PLN03140 333 MIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM 392
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
112-224 |
8.38e-04 |
|
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 39.23 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 112 KRGKRRFLKIRKL--KQNLPRFKKLAAVMNNGLEN-RLNTFVEGLSGGQRQAL---SFLMATIErPDILLLDEHTAALDP 185
Cdd:cd03238 44 ASGKARLISFLPKfsRNKLIFIDQLQFLIDVGLGYlTLGQKLSTLSGGELQRVklaSELFSEPP-GTLFILDEPSTGLHQ 122
|
90 100 110
....*....|....*....|....*....|....*....
gi 489745462 186 HTSENLLAVTDqQIKENKLTALMITHHmEDALKYGNRLL 224
Cdd:cd03238 123 QDINQLLEVIK-GLIDLGNTVILIEHN-LDVLSSADWII 159
|
|
| COG3910 |
COG3910 |
Predicted ATPase [General function prediction only]; |
23-57 |
1.23e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.98 E-value: 1.23e-03
10 20 30
....*....|....*....|....*....|....*..
gi 489745462 23 VPILKGID-LKIKAGdfITII-GTNGAGKSTLLNTIA 57
Cdd:COG3910 24 LPAVRNLEgLEFHPP--VTFFvGENGSGKSTLLEAIA 58
|
|
| uvrA |
PRK00349 |
excinuclease ABC subunit UvrA; |
26-56 |
1.42e-03 |
|
excinuclease ABC subunit UvrA;
Pssm-ID: 234734 [Multi-domain] Cd Length: 943 Bit Score: 39.67 E-value: 1.42e-03
10 20 30
....*....|....*....|....*....|.
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTI 56
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLINET 655
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
32-240 |
1.99e-03 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 39.14 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 32 KIKAGDFITIIGTNGAGKSTLLNTIAGSLRPDS-GFLLHNGHDIT-KMSEEKRTQFIGRVFQDPKM-GTAPRMTVAENLL 108
Cdd:PRK13549 284 SLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWeGEIFIDGKPVKiRNPQQAIAQGIAMVPEDRKRdGIVPVMGVGKNIT 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 109 LAtkrgkrrflkirklkqNLPRFKKlAAVMNNGLEN----------RLNTF-----VEGLSGGQRQALSFLMATIERPDI 173
Cdd:PRK13549 364 LA----------------ALDRFTG-GSRIDDAAELktilesiqrlKVKTAspelaIARLSGGNQQKAVLAKCLLLNPKI 426
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489745462 174 LLLDEHTAALDPHTSENLLAVTDQQIKENkLTALMITHHMEDALKYGNRLLVLKDGKVKAD-INE---QEK 240
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQG-VAIIVISSELPEVLGLSDRVLVMHEGKLKGDlINHnltQEQ 496
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
33-65 |
3.71e-03 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 37.17 E-value: 3.71e-03
10 20 30
....*....|....*....|....*....|...
gi 489745462 33 IKAGDFITIIGTNGAGKSTLLNTIAGSLRPDSG 65
Cdd:cd03222 22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD 54
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
153-220 |
4.54e-03 |
|
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213245 [Multi-domain] Cd Length: 197 Bit Score: 37.06 E-value: 4.54e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489745462 153 LSGGQRQ--ALSFLMATIE-RPD-ILLLDEHTAALDPHTSENLLAVTDQQIKENKLtaLMITHH---ME--DALkYG 220
Cdd:cd03278 114 LSGGEKAltALALLFAIFRvRPSpFCVLDEVDAALDDANVERFARLLKEFSKETQF--IVITHRkgtMEaaDRL-YG 187
|
|
| UvrA |
COG0178 |
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair]; |
26-56 |
6.25e-03 |
|
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 37.70 E-value: 6.25e-03
10 20 30
....*....|....*....|....*....|.
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTI 56
Cdd:COG0178 621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVNDI 651
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
26-56 |
6.47e-03 |
|
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.69 E-value: 6.47e-03
10 20 30
....*....|....*....|....*....|.
gi 489745462 26 LKGIDLKIKAGDFITIIGTNGAGKSTLLNTI 56
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLINDT 654
|
|
| TMPK |
cd01672 |
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the ... |
38-62 |
7.08e-03 |
|
Thymidine monophosphate kinase (TMPK), also known as thymidylate kinase, catalyzes the phosphorylation of thymidine monophosphate (TMP) to thymidine diphosphate (TDP) utilizing ATP as its preferred phophoryl donor. TMPK represents the rate-limiting step in either de novo or salvage biosynthesis of thymidine triphosphate (TTP).
Pssm-ID: 238835 Cd Length: 200 Bit Score: 36.48 E-value: 7.08e-03
10 20
....*....|....*....|....*
gi 489745462 38 FITIIGTNGAGKSTLLNTIAGSLRP 62
Cdd:cd01672 2 FIVFEGIDGAGKTTLIELLAERLEA 26
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
146-211 |
7.33e-03 |
|
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.
Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.18 E-value: 7.33e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 489745462 146 LNTFVEGLSGGQRQ--ALSFLM--ATIERPDILLLDEHTAALDPHTSENLLAVtdqqIKE---NKLTALMITH 211
Cdd:cd03227 71 LIFTRLQLSGGEKElsALALILalASLKPRPLYILDEIDRGLDPRDGQALAEA----ILEhlvKGAQVIVITH 139
|
|
| COG3950 |
COG3950 |
Predicted ATP-binding protein involved in virulence [General function prediction only]; |
26-144 |
9.39e-03 |
|
Predicted ATP-binding protein involved in virulence [General function prediction only];
Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 36.51 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489745462 26 LKGI-DLKI---KAGDFITIIGTNGAGKSTLLNTIAGSLRPDSGFL---LHNGHDITKMSEEKRTQFI-----GRVFQDP 93
Cdd:COG3950 11 FRGFeDLEIdfdNPPRLTVLVGENGSGKTTLLEAIALALSGLLSRLddvKFRKLLIRNGEFGDSAKLIlyygtSRLLLDG 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 489745462 94 KMGTAPRMTVAENlllatkrgkRRFLKIRKLKQNLPRFKKLAAVMNNGLEN 144
Cdd:COG3950 91 PLKKLERLKEEYF---------SRLDGYDSLLDEDSNLREFLEWLREYLED 132
|
|
| |
