|
Name |
Accession |
Description |
Interval |
E-value |
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-255 |
1.17e-146 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 410.25 E-value: 1.17e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:COG1101 1 MLELKNLSKTFNPGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPSMGTCPSLTVLENMALADNKGSSFLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAML 160
Cdd:COG1101 81 YIGRVFQDPMMGTAPSMTIEENLALAYRRGKRRGLRRGLTKKRRELFRELLATLGLGLENRLDTKVGLLSGGQRQALSLL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 161 IATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGEDKKVLD 240
Cdd:COG1101 161 MATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRIILDVSGEEKKKLT 240
|
250
....*....|....*
gi 1852789824 241 VRDLTNRFDEISVED 255
Cdd:COG1101 241 VEDLLELFEEIRGEE 255
|
|
| LolD |
COG1136 |
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis]; |
1-227 |
3.66e-56 |
|
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 179.47 E-value: 3.66e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:COG1136 4 LLELRNLTKSYGTGEGEVTAL-RGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 F----IGRVFQDPSMgtCPSLTVLENMALAdnkgssfLLQRGVNRR-RTQHYREELSLLhmGLEDKLGVQVGSLSGGQRQ 155
Cdd:COG1136 83 LrrrhIGFVFQFFNL--LPELTALENVALP-------LLLAGVSRKeRRERARELLERV--GLGDRLDHRPSQLSGGQQQ 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 156 --ALAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAvAYGDRLLMMHRGHI 227
Cdd:COG1136 152 rvAIARALVN-RP-KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELA-ARADRVIRLRDGRI 222
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
2-227 |
6.76e-55 |
|
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: 175.76 E-value: 6.76e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:cd03255 1 IELKNLSKTYGGGGEKVQAL-KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 ----IGRVFQDPSMgtCPSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQ-- 155
Cdd:cd03255 80 rrrhIGFVFQSFNL--LPDLTALENVELP-------LLLAGVPKKERRERAEEL-LERVGLGDRLNHYPSELSGGQQQrv 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 156 ALAMLIATMSPInlLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAvAYGDRLLMMHRGHI 227
Cdd:cd03255 150 AIARALANDPKI--ILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
17-235 |
4.56e-48 |
|
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: 158.65 E-value: 4.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDP-SMGTCP 95
Cdd:COG1122 12 GGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLVFQNPdDQLFAP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 96 slTVLENMALAdnkgssfLLQRGVN----RRRTQHyreelSLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIAtMSPiNL 169
Cdd:COG1122 92 --TVEEDVAFG-------PENLGLPreeiRERVEE-----ALELVGLEHLADRPPHELSGGQKQrvAIAGVLA-MEP-EV 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 170 LILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRLNKEGK-TVIIVTHDLDLVAELADRVIVLDDGRIVADGTPRE 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
2-228 |
1.29e-47 |
|
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is comprised of proteins involved in the transport of apparently unrelated solutes and proteins specific for di- and oligosaccharides and polyols. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213226 [Multi-domain] Cd Length: 213 Bit Score: 156.91 E-value: 1.29e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrf 81
Cdd:cd03259 1 LELKGLSKTYG-----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRN-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSMgtCPSLTVLENMALAdnkgssflLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQ--ALAM 159
Cdd:cd03259 74 IGMVFQDYAL--FPHLTVAENIAFG--------LKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQrvALAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 160 LIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:cd03259 144 ALAR-EP-SLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
3-228 |
9.99e-47 |
|
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: 155.67 E-value: 9.99e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 3 RMEHIYKTFnpGSVneVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF- 81
Cdd:cd03219 2 EVRGLTKRF--GGL--VAL-DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLg 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSmgTCPSLTVLENMALA-DNKGSSFLLQRGVNRRRTQHYREELSLLH-MGLEDKLGVQVGSLSGGQRQAL-- 157
Cdd:cd03219 77 IGRTFQIPR--LFPELTVLENVMVAaQARTGSGLLLARARREEREARERAEELLErVGLADLADRPAGELSYGQQRRLei 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 158 AMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:cd03219 155 ARALAT-DP-KLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
15-240 |
1.00e-46 |
|
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: 155.97 E-value: 1.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtc 94
Cdd:COG1120 10 GYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYVPQEPPAP-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTVLENMALAdnkgssfllqR----GVNRRRTQHYRE--ELSLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIATMSP 166
Cdd:COG1120 88 FGLTVRELVALG----------RyphlGLFGRPSAEDREavEEALERTGLEHLADRPVDELSGGERQrvLIARALAQEPP 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 167 InlLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGEDKKVLD 240
Cdd:COG1120 158 L--LLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIV--AQGPPEEVLT 227
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
1-235 |
1.45e-46 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 155.60 E-value: 1.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYE--- 77
Cdd:COG3638 2 MLELRNLSKRYP----GGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRAlrr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 -RSRfIGRVFQDPSMgtCPSLTVLENmALADNKGSSFLLQRGVNRRRTQHYREELSLLH-MGLEDKLGVQVGSLSGGQRQ 155
Cdd:COG3638 78 lRRR-IGMIFQQFNL--VPRLSVLTN-VLAGRLGRTSTWRSLLGLFPPEDRERALEALErVGLADKAYQRADQLSGGQQQ 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 156 ALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:COG3638 154 RVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAE 233
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
10-226 |
4.90e-46 |
|
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: 153.01 E-value: 4.90e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 10 TFNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDP 89
Cdd:cd03225 6 SFSYPDGARPAL-DDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQNP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SMGTCpSLTVLENMALAdnkgssfLLQRGVNRRRTQHyREELSLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIAtMSPi 167
Cdd:cd03225 85 DDQFF-GPTVEEEVAFG-------LENLGLPEEEIEE-RVEEALELVGLEGLRDRSPFTLSGGQKQrvAIAGVLA-MDP- 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 168 NLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGH 226
Cdd:cd03225 154 DILLLDEPTAGLDPAGRRELLELLKKLKAEGK-TIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
1-250 |
1.02e-44 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 151.01 E-value: 1.02e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSvNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTkmkeyERSR 80
Cdd:COG1116 7 ALELRGVSKRFPTGG-GGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT-----GPGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPS-MgtcPSLTVLENMALAdnkgssfLLQRGVNRR-RTQHYREELSLlhMGLEDKLGVQVGSLSGGQRQ--- 155
Cdd:COG1116 81 DRGVVFQEPAlL---PWLTVLDNVALG-------LELRGVPKAeRRERARELLEL--VGLAGFEDAYPHQLSGGMRQrva 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 156 ---ALAMliatmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHR--GHImld 230
Cdd:COG1116 149 iarALAN-----DP-EVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRI--- 219
|
250 260
....*....|....*....|....*
gi 1852789824 231 aagedKKVLDV-----RDLTNRFDE 250
Cdd:COG1116 220 -----VEEIDVdlprpRDRELRTSP 239
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
1-233 |
5.69e-43 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 145.58 E-value: 5.69e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:COG2884 1 MIRFENVSKRYPGG----REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 F---IGRVFQDpsmgtC---PSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQR 154
Cdd:COG2884 77 LrrrIGVVFQD-----FrllPDRTVYENVALP-------LRVTGKSRKEIRRRVREV-LDLVGLSDKAKALPHELSGGEQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 155 QALAmlIA---TMSPInLLILDEHTAALDPHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDA 231
Cdd:COG2884 144 QRVA--IAralVNRPE-LLLADEPTGNLDPETSWEIMELLEEINRRG-TTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
|
..
gi 1852789824 232 AG 233
Cdd:COG2884 220 AR 221
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
2-227 |
6.97e-43 |
|
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: 144.92 E-value: 6.97e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTkmkeyERSRF 81
Cdd:cd03293 1 LEVRNVSKTY-GGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT-----GPGPD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSMgtCPSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREElsLLHM----GLEDKLGVQvgsLSGGQRQ-- 155
Cdd:cd03293 75 RGYVFQQDAL--LPWLTVLDNVALG-------LELQGVPKAEARERAEE--LLELvglsGFENAYPHQ---LSGGMRQrv 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 156 ALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMM--HRGHI 227
Cdd:cd03293 141 ALARALA-VDP-DVLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRI 212
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
15-227 |
7.74e-42 |
|
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: 141.03 E-value: 7.74e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQdpsmgtc 94
Cdd:cd03214 8 GYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 psltVLENMALADnkgssfLLQRGVNrrrtqhyreelsllhmgledklgvqvgSLSGGQRQ--ALAMLIATMSPInlLIL 172
Cdd:cd03214 81 ----ALELLGLAH------LADRPFN---------------------------ELSGGERQrvLLARALAQEPPI--LLL 121
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 173 DEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03214 122 DEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176
|
|
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
2-230 |
9.83e-41 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 140.20 E-value: 9.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnpGSVNEVvlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRf 81
Cdd:COG1131 1 IEVRGLTKRY--GDKTAL---DGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRR- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSMgtCPSLTVLENMALAdnkgSSFllqRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLI 161
Cdd:COG1131 75 IGYVPQEPAL--YPDLTVRENLRFF----ARL---YGLPRKEARERIDEL-LELFGLTDAADRKVGTLSGGMKQRLGLAL 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 162 ATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:COG1131 145 ALLHDPELLILDEPTSGLDPEARRELWELLRELAAEGK-TVLLSTHYLEEAERLCDRVAIIDKGRIVAD 212
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-235 |
1.03e-40 |
|
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: 146.20 E-value: 1.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:COG1123 260 LLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 F---IGRVFQDPSMGTCPSLTVLENMALAdnkgssfLLQRGVNRRRTqhyREE--LSLLHM-GL-EDKLGVQVGSLSGGQ 153
Cdd:COG1123 340 LrrrVQMVFQDPYSSLNPRMTVGDIIAEP-------LRLHGLLSRAE---RRErvAELLERvGLpPDLADRYPHELSGGQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 154 RQ--ALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDA 231
Cdd:COG1123 410 RQrvAIARALA-LEP-KLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDG 487
|
....
gi 1852789824 232 AGED 235
Cdd:COG1123 488 PTEE 491
|
|
| FetA |
COG4619 |
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism]; |
15-227 |
4.71e-40 |
|
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 137.64 E-value: 4.71e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMK--EYeRSRfIGRVFQDPSMG 92
Cdd:COG4619 9 RVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPppEW-RRQ-VAYVPQEPALW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 93 tcpSLTVLENMALADNkgssfLLQRGVNRRRTQHYreelsLLHMGL-EDKLGVQVGSLSGGQRQALAMLIATMSPINLLI 171
Cdd:COG4619 87 ---GGTVRDNLPFPFQ-----LRERKFDRERALEL-----LERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 172 LDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:COG4619 154 LDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
1-228 |
6.29e-40 |
|
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter subfamily specific for the transport of dipeptides, oligopeptides (OppD), and nickel (NikDE). The NikABCDE system of E. coli belongs to this family and is composed of the periplasmic binding protein NikA, two integral membrane components (NikB and NikC), and two ATPase (NikD and NikE). The NikABCDE transporter is synthesized under anaerobic conditions to meet the increased demand for nickel resulting from hydrogenase synthesis. The molecular mechanism of nickel uptake in many bacteria and most archaea is not known. Many other members of this ABC family are also involved in the uptake of dipeptides and oligopeptides. The oligopeptide transport system (Opp) is a five-component ABC transport composed of a membrane-anchored substrate binding proteins (SRP), OppA, two transmembrane proteins, OppB and OppC, and two ATP-binding domains, OppD and OppF.
Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 137.64 E-value: 6.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTF-NPGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE---Y 76
Cdd:cd03257 1 LLEVKNLSVSFpTGGGSVKAL--DDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRrlrK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 77 ERSRFIGRVFQDPSMGTCPSLTVLEnmALADnkgsSFLLQRGVNRRRTQHYREELSLLHMGL-EDKLGVQVGSLSGGQRQ 155
Cdd:cd03257 79 IRRKEIQMVFQDPMSSLNPRMTIGE--QIAE----PLRIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 156 --ALAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:cd03257 153 rvAIARALAL-NP-KLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
13-235 |
1.20e-39 |
|
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: 143.51 E-value: 1.20e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 13 PGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG---SGEIYVGDRQVTKMKEYERSRFIGRVFQDP 89
Cdd:COG1123 15 PGGDVPAV--DGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRGRRIGMVFQDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SMGTCPsLTVLENMALAdnkgssfLLQRGVNRRrtQHYREELSLLHM-GLEDKLGVQVGSLSGGQRQ--ALAMLIATMSP 166
Cdd:COG1123 93 MTQLNP-VTVGDQIAEA-------LENLGLSRA--EARARVLELLEAvGLERRLDRYPHQLSGGQRQrvAIAMALALDPD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 167 inLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:COG1123 163 --LLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEE 229
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
20-235 |
9.54e-39 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 134.48 E-value: 9.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFqDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF-IGRVFQDpsMGTCPSLT 98
Cdd:cd03224 15 ILF-GVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYVPEG--RRIFPELT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 99 VLENMALAdnkgsSFLLQRGVNRRRtqhyREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAA 178
Cdd:cd03224 92 VEENLLLG-----AYARRRAKRKAR----LERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEG 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 179 LDPHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:cd03224 163 LAPKIVEEIFEAIRELRDEG-VTILLVEQNARFALEIADRAYVLERGRVVLEGTAAE 218
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
3-235 |
5.91e-38 |
|
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: 133.08 E-value: 5.91e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 3 RMEHIYKTFNpgsvNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYE----R 78
Cdd:cd03256 2 EVENLSKTYP----NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqlR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 79 SRfIGRVFQDPSMgtCPSLTVLENmALADNKGSSFLLQRGVNRRRTQHYREELSLL-HMGLEDKLGVQVGSLSGGQRQAL 157
Cdd:cd03256 78 RQ-IGMIFQQFNL--IERLSVLEN-VLSGRLGRRSTWRSLFGLFPKEEKQRALAALeRVGLLDKAYQRADQLSGGQQQRV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 158 AMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:cd03256 154 AIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE 231
|
|
| PotA |
COG3842 |
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ... |
1-228 |
1.31e-37 |
|
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 134.84 E-value: 1.31e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYErsR 80
Cdd:COG3842 5 ALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEK--R 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQD----PSMgtcpslTVLENMAladnkgssF-LLQRGVNRR-RTQHYREELSLLHM-GLEDKLgvqVGSLSGGQ 153
Cdd:COG3842 78 NVGMVFQDyalfPHL------TVAENVA--------FgLRMRGVPKAeIRARVAELLELVGLeGLADRY---PHQLSGGQ 140
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 154 RQ--ALAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:COG3842 141 QQrvALARALAP-EP-RVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIE 215
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
1-232 |
5.19e-37 |
|
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: 130.50 E-value: 5.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYE--- 77
Cdd:TIGR02315 1 MLEVENLSKVYPNG----KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKlrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 -RSRfIGRVFQDPSMgtCPSLTVLENMaLADNKGSSFLLQRGVNRRRTQHYREELSLL-HMGLEDKLGVQVGSLSGGQRQ 155
Cdd:TIGR02315 77 lRRR-IGMIFQHYNL--IERLTVLENV-LHGRLGYKPTWRSLLGRFSEEDKERALSALeRVGLADKAYQRADQLSGGQQQ 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 156 ALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAA 232
Cdd:TIGR02315 153 RVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
2-227 |
1.06e-36 |
|
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: 129.54 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnpGSvnEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:cd03261 1 IELRGLTKSF--GG--RTVL-KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 ---IGRVFQDPSMGTcpSLTVLENMALadnkgssFLLQrgvNRRRTQHYREELSLLHM---GLEDKLGVQVGSLSGGQRQ 155
Cdd:cd03261 76 rrrMGMLFQSGALFD--SLTVFENVAF-------PLRE---HTRLSEEEIREIVLEKLeavGLRGAEDLYPAELSGGMKK 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 156 --ALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03261 144 rvALARALA-LDP-ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKI 215
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
1-244 |
1.08e-36 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 129.82 E-value: 1.08e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKmkeyeRSR 80
Cdd:COG1121 6 AIELENLTVSYG----GRPVL-EDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR-----ARR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQ----DPSMgtcPsLTVLENMAladnkgSSFLLQRGVNRRRTQHYREEL--SLLHMGLEDKLGVQVGSLSGGQR 154
Cdd:COG1121 76 RIGYVPQraevDWDF---P-ITVRDVVL------MGRYGRRGLFRRPSRADREAVdeALERVGLEDLADRPIGELSGGQQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 155 Q--ALAMLIATMSPinLLILDEHTAALDPHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHImldAA 232
Cdd:COG1121 146 QrvLLARALAQDPD--LLLLDEPFAGVDAATEEALYELLRELRREG-KTILVVTHDLGAVREYFDRVLLLNRGLV---AH 219
|
250
....*....|..
gi 1852789824 233 GEDKKVLDVRDL 244
Cdd:COG1121 220 GPPEEVLTPENL 231
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-230 |
1.10e-36 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the 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: 130.65 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:TIGR04521 1 IKLKNVSYIYQPGTPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 ---IGRVFQDPSMgtcpSL---TVLE-------NMALADNKgssfllqrgVNRRrtqhYREELSLlhMGLEDKLGVQvgS 148
Cdd:TIGR04521 81 rkkVGLVFQFPEH----QLfeeTVYKdiafgpkNLGLSEEE---------AEER----VKEALEL--VGLDEEYLER--S 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 149 ---LSGGQ--RQALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMH 223
Cdd:TIGR04521 140 pfeLSGGQmrRVAIAGVLA-MEP-EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMH 217
|
....*..
gi 1852789824 224 RGHIMLD 230
Cdd:TIGR04521 218 KGKIVLD 224
|
|
| GlnQ |
COG1126 |
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ... |
1-227 |
3.48e-36 |
|
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 128.19 E-value: 3.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTIL---NLLcgsLPLGSGEIYVGDRQVTkMKEYE 77
Cdd:COG1126 1 MIEIENLHKSFG----DLEVL-KGISLDVEKGEVVVIIGPSGSGKSTLLrciNLL---EEPDSGTITVDGEDLT-DSKKD 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 ----RSRfIGRVFQD----PSMgtcpslTVLENMALAdnkgssfLLQ-RGVNRRRTQHYREELsLLHMGLEDKLGVQVGS 148
Cdd:COG1126 72 inklRRK-VGMVFQQfnlfPHL------TVLENVTLA-------PIKvKKMSKAEAEERAMEL-LERVGLADKADAYPAQ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 149 LSGGQRQ------ALAMliatmSPiNLLILDEHTAALDPhssENVME-LT--QRVAKEkHVTMLMVTHNLKFAVAYGDRL 219
Cdd:COG1126 137 LSGGQQQrvaiarALAM-----EP-KVMLFDEPTSALDP---ELVGEvLDvmRDLAKE-GMTMVVVTHEMGFAREVADRV 206
|
....*...
gi 1852789824 220 LMMHRGHI 227
Cdd:COG1126 207 VFMDGGRI 214
|
|
| DppF |
COG1124 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
1-227 |
4.25e-36 |
|
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];
Pssm-ID: 440741 [Multi-domain] Cd Length: 248 Bit Score: 128.38 E-value: 4.25e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:COG1124 1 MLEVRNLSVSYGQGGRRVPVL-KDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPsMGTC-PSLTVLENMALAdnkgssfLLQRGVNRRRTQhyREELsLLHMGL-EDKLGVQVGSLSGGQRQALA 158
Cdd:COG1124 80 RVQMVFQDP-YASLhPRHTVDRILAEP-------LRIHGLPDREER--IAEL-LEQVGLpPSFLDRYPHQLSGGQRQRVA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 159 MLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:COG1124 149 IARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRI 217
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
2-228 |
6.64e-36 |
|
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: 127.24 E-value: 6.64e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVvlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERsrf 81
Cdd:cd03263 1 LQIRNLTKTYKKGTKPAV---DDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAAR--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 igrvfqdPSMGTCPS-------LTVLENMALadnkgssFLLQRGVNRRrtqHYREELSLL--HMGLEDKLGVQVGSLSGG 152
Cdd:cd03263 75 -------QSLGYCPQfdalfdeLTVREHLRF-------YARLKGLPKS---EIKEEVELLlrVLGLTDKANKRARTLSGG 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 153 QRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:cd03263 138 MKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLR 211
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
2-226 |
7.33e-36 |
|
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: 125.76 E-value: 7.33e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEY--ERS 79
Cdd:cd03229 1 LELKNVSKRYG-----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElpPLR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 80 RFIGRVFQDPSMgtCPSLTVLENMALAdnkgssfllqrgvnrrrtqhyreelsllhmgledklgvqvgsLSGGQRQALAM 159
Cdd:cd03229 76 RRIGMVFQDFAL--FPHLTVLENIALG------------------------------------------LSGGQQQRVAL 111
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 160 LIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGH 226
Cdd:cd03229 112 ARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
25-235 |
2.55e-35 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 126.02 E-value: 2.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 25 FNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrfIGRVFQDPSMgtCPSLTVLENMA 104
Cdd:COG3840 18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERP--VSMLFQENNL--FPHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 105 LAdnkgssflLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIATMSPInlLILDEHTAALDPH 182
Cdd:COG3840 94 LG--------LRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQrvALARCLVRKRPI--LLLDEPFSALDPA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 183 SSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:COG3840 164 LRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAA 216
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
2-230 |
6.32e-35 |
|
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];
Pssm-ID: 441875 [Multi-domain] Cd Length: 711 Bit Score: 131.88 E-value: 6.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNevvLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:COG2274 474 IELENVSFRYPGDSPP---VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQ 550
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSM--GtcpslTVLENMALADNKGSSFLLQR-----GVNrrrtqhyrEELSLLHMGLEDKLGVQVGSLSGGQR 154
Cdd:COG2274 551 IGVVLQDVFLfsG-----TIRENITLGDPDATDEEIIEaarlaGLH--------DFIEALPMGYDTVVGEGGSNLSGGQR 617
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 155 Q--ALAMLIATMSPInlLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHIMLD 230
Cdd:COG2274 618 QrlAIARALLRNPRI--LILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLS-TIRLADRIIVLDKGRIVED 690
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
15-226 |
8.25e-35 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 122.35 E-value: 8.25e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQdpsmgtc 94
Cdd:cd00267 8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 psltvlenmaladnkgssfllqrgvnrrrtqhyreelsllhmgledklgvqvgsLSGGQRQALAMLIATMSPINLLILDE 174
Cdd:cd00267 81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 175 HTAALDPHSSENVMELTQRVAKEkHVTMLMVTHNLKFAVAYGDRLLMMHRGH 226
Cdd:cd00267 107 PTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
17-225 |
9.18e-35 |
|
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: 123.80 E-value: 9.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKmkeyERSRfIGRVFQDPSMGTCPS 96
Cdd:cd03235 11 GHPVL-EDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEK----ERKR-IGYVPQRRSIDRDFP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENMALAdnkgssFLLQRGVNRRRTQHYREEL--SLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIAtmSPINLLIL 172
Cdd:cd03235 85 ISVRDVVLMG------LYGHKGLFRRLSKADKAKVdeALERVGLSELADRQIGELSGGQQQrvLLARALV--QDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 173 DEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRG 225
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLEYFDRVLLLNRT 208
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
22-227 |
1.45e-34 |
|
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: 123.83 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG-----SGEIYVGDRQVTKMKE--YERSRFIGRVFQDPSMGtc 94
Cdd:cd03260 16 LKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIpgapdEGEVLLDGKDIYDLDVdvLELRRRVGMVFQKPNPF-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 pSLTVLENMALADNKgssfllqRGVNRRRTQHYREELSLLHMGLEDKLG--VQVGSLSGGQRQ--ALAMLIAtMSPiNLL 170
Cdd:cd03260 94 -PGSIYDNVAYGLRL-------HGIKLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQrlCLARALA-NEP-EVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 171 ILDEHTAALDPHSSENVMELTQRVAKEkhVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03260 164 LLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRL 218
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
1-227 |
1.49e-34 |
|
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: 123.94 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:COG1127 5 MIEVRNLTKSFG----DRVVL-DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 F---IGRVFQDPSMGTcpSLTVLENMAladnkgssFLLqrgvnRRRTQHYREE-----LSLLHM-GLEDKLGVQVGSLSG 151
Cdd:COG1127 80 LrrrIGMLFQGGALFD--SLTVFENVA--------FPL-----REHTDLSEAEirelvLEKLELvGLPGAADKMPSELSG 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 152 GQRQ--ALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:COG1127 145 GMRKrvALARALA-LDP-EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKI 220
|
|
| ECF_ATPase_1 |
TIGR04520 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
2-230 |
1.79e-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: 124.85 E-value: 1.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVvlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYV-GDRQVTKMKEYERSR 80
Cdd:TIGR04520 1 IEVENVSFSYPESEKPAL---KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVdGLDTLDEENLWEIRK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPS---MGTcpslTVLENMALA-DNKGssflLQRGVNRRRTQHyreelSLLHMGLEDKLGVQVGSLSGGQRQ- 155
Cdd:TIGR04520 78 KVGMVFQNPDnqfVGA----TVEDDVAFGlENLG----VPREEMRKRVDE-----ALKLVGMEDFRDREPHLLSGGQKQr 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 156 -ALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVaYGDRLLMMHRGHIMLD 230
Cdd:TIGR04520 145 vAIAGVLA-MRP-DIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAV-LADRVIVMNKGKIVAE 217
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
2-226 |
2.96e-34 |
|
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: 121.34 E-value: 2.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIykTFN-PGSVNEVvlFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:cd03228 1 IEFKNV--SFSyPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPSMgtcPSLTVLENMaladnkgssfllqrgvnrrrtqhyreelsllhmgledklgvqvgsLSGGQRQ--ALA 158
Cdd:cd03228 77 NIAYVPQDPFL---FSGTIRENI---------------------------------------------LSGGQRQriAIA 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 159 -MLIATmSPInlLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGH 226
Cdd:cd03228 109 rALLRD-PPI--LILDEATSALDPETEALILEALRALAKGK--TVIVIAHRLS-TIRDADRIIVLDDGR 171
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
1-227 |
1.34e-33 |
|
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];
Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 121.89 E-value: 1.34e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKmKEYERSR 80
Cdd:COG4555 1 MIEVENLSKKYG-----KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPsmGTCPSLTVLENMALadnkgssFLLQRGVNRRRTQHYREELSLLhMGLEDKLGVQVGSLSGGQRQALAML 160
Cdd:COG4555 75 QIGVLPDER--GLYDRLTVRENIRY-------FAELYGLFDEELKKRIEELIEL-LGLEEFLDRRVGELSTGMKKKVALA 144
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 161 IATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:COG4555 145 RALVHDPKVLLLDEPTNGLDVMARRLLREILRALKKEGK-TVLFSSHIMQEVEALCDRVVILHKGKV 210
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
1-228 |
1.48e-33 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 124.42 E-value: 1.48e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnpGSVnEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSr 80
Cdd:COG3839 3 SLELENVSKSY--GGV-EAL--KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 fIGRVFQDPSMgtCPSLTVLENMALAdnkgssfLLQRGVN----RRRTqhyREELSLLhmGLEDKLGVQVGSLSGGQRQ- 155
Cdd:COG3839 77 -IAMVFQSYAL--YPHMTVYENIAFP-------LKLRKVPkaeiDRRV---REAAELL--GLEDLLDRKPKQLSGGQRQr 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 156 -ALAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:COG3839 142 vALGRALVR-EP-KVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQ 213
|
|
| TauB |
COG4525 |
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism]; |
1-235 |
1.65e-33 |
|
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 121.89 E-value: 1.65e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKmKEYERsr 80
Cdd:COG4525 3 MLTVRHVSVRY-PGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTG-PGADR-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 fiGRVFQDPSMgtCPSLTVLENMALAdnkgssflLQ-RGVNR-RRTQHYREELSLlhMGLEDKLGVQVGSLSGGQRQALA 158
Cdd:COG4525 79 --GVVFQKDAL--LPWLNVLDNVAFG--------LRlRGVPKaERRARAEELLAL--VGLADFARRRIWQLSGGMRQRVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 159 MLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMM--HRGHIM----LD-- 230
Cdd:COG4525 145 IARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIVerleLDfs 224
|
....*...
gi 1852789824 231 ---AAGED 235
Cdd:COG4525 225 rrfLAGED 232
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
2-228 |
6.92e-33 |
|
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: 118.90 E-value: 6.92e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrf 81
Cdd:cd03301 1 VELENVTKRFG-----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSMgtCPSLTVLENMALAdnkgssfLLQRGVNRRR-TQHYREELSLLhmGLEDKLGVQVGSLSGGQRQALAML 160
Cdd:cd03301 74 IAMVFQNYAL--YPHMTVYDNIAFG-------LKLRKVPKDEiDERVREVAELL--QIEHLLDRKPKQLSGGQRQRVALG 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 161 IATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:cd03301 143 RAIVREPKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQ 210
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
17-227 |
1.09e-32 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 124.87 E-value: 1.09e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMgtcPS 96
Cdd:COG4988 348 GGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWVPQNPYL---FA 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENMALADNKGSSFLLQRGVnrrRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIATMSPInlLILDE 174
Cdd:COG4988 425 GTIRENLRLGRPDASDEELEAAL---EAAGLDEFVAALPDGLDTPLGEGGRGLSGGQAQrlALARALLRDAPL--LLLDE 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 175 HTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:COG4988 500 PTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRI 549
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
2-228 |
1.53e-32 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 120.12 E-value: 1.53e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnPGsvNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:PRK13635 6 IRVEHISFRY-PD--AATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPS---MGTcpslTVLENMALAdnkgssfLLQRGVNR----RRTQhyrEELSLLHMglEDKLGVQVGSLSGGQR 154
Cdd:PRK13635 83 VGMVFQNPDnqfVGA----TVQDDVAFG-------LENIGVPReemvERVD---QALRQVGM--EDFLNREPHRLSGGQK 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 155 Q--ALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAvAYGDRLLMMHRGHIM 228
Cdd:PRK13635 147 QrvAIAGVLA-LQP-DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEIL 219
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
2-227 |
1.68e-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: 118.94 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVnevvLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:cd03295 1 IEFENVTKRYGGGKK----AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQdpSMGTCPSLTVLENMALADNkgssflLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLI 161
Cdd:cd03295 77 IGYVIQ--QIGLFPHMTVEENIALVPK------LLKWPKEKIRERADELLALVGLDPAEFADRYPHELSGGQQQRVGVAR 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 162 ATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03295 149 ALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEI 214
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
2-227 |
1.91e-32 |
|
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: 118.02 E-value: 1.91e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE--YERS 79
Cdd:cd03262 1 IEIKNLHKSFG----DFHVL-KGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 80 RFIGRVFQdpSMGTCPSLTVLENMALADNKgssfllQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQ--AL 157
Cdd:cd03262 76 QKVGMVFQ--QFNLFPHLTVLENITLAPIK------VKGMSKAEAEERALEL-LEKVGLADKADAYPAQLSGGQQQrvAI 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 158 AMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEkHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03262 147 ARALA-MNP-KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
2-227 |
2.19e-31 |
|
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: 114.03 E-value: 2.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVnevvlFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEyERSRF 81
Cdd:cd03230 1 IEVRNLSKRYGKKTA-----LDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPE-EVKRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSMGtcPSLTVLENMaladnkgssfllqrgvnrrrtqhyreelsllhmgledklgvqvgSLSGGQRQALAMLI 161
Cdd:cd03230 75 IGYLPEEPSLY--ENLTVRENL--------------------------------------------KLSGGMKQRLALAQ 108
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 162 ATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03230 109 ALLHDPELLILDEPTSGLDPESRREFWELLRELKKEG-KTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
23-227 |
4.90e-31 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 114.63 E-value: 4.90e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtcpSLTVLEN 102
Cdd:cd03254 20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLF---SGTIMEN 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 MALADNKGSSFLLQRGVnrrRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPH 182
Cdd:cd03254 97 IRLGRPNATDEEVIEAA---KEAGAHDFIMKLPNGYDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEATSNIDTE 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1852789824 183 SSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:cd03254 174 TEKLIQEALEKLMKGR--TSIIIAHRLS-TIKNADKILVLDDGKI 215
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
21-235 |
8.58e-31 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 114.87 E-value: 8.58e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGTcpSLTVL 100
Cdd:PRK13548 17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLPQHSSLSF--PFTVE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 E--NMALADNKGSsfllqRGVNRRRTQHYREELSLLHmgLEDKLgvqVGSLSGG--QRQALAMLIATMSPIN----LLIL 172
Cdd:PRK13548 95 EvvAMGRAPHGLS-----RAEDDALVAAALAQVDLAH--LAGRD---YPQLSGGeqQRVQLARVLAQLWEPDgpprWLLL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 173 DEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:PRK13548 165 DEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAE 227
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
22-177 |
1.42e-30 |
|
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: 111.20 E-value: 1.42e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtcPSLTVLE 101
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLF--PRLTVRE 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 102 NMALAdnkGSSFLLQRGVNRRRTQHYREELSLLHMgLEDKLGVQVGSLSGGQRQ--ALAMLIATMSPInlLILDEHTA 177
Cdd:pfam00005 79 NLRLG---LLLKGLSKREKDARAEEALEKLGLGDL-ADRPVGERPGTLSGGQRQrvAIARALLTKPKL--LLLDEPTA 150
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
22-227 |
3.06e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 118.34 E-value: 3.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtcpSLTVLE 101
Cdd:COG1132 356 LKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQDTFLF---SGTIRE 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 102 NMALADNKGSsfllqrgvnrrrtqhyREEL------SLLH---MGLEDKLGVQVG----SLSGGQRQ--ALAMLIATMSP 166
Cdd:COG1132 433 NIRYGRPDAT----------------DEEVeeaakaAQAHefiEALPDGYDTVVGergvNLSGGQRQriAIARALLKDPP 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 167 InlLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:COG1132 497 I--LILDEATSALDTETEALIQEALERLMKGR--TTIVIAHRLS-TIRNADRILVLDDGRI 552
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
2-227 |
5.45e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 113.58 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVT---KMKEYER 78
Cdd:PRK13634 3 ITFQKVEHRYQYKTPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITagkKNKKLKP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 79 SR-FIGRVFQDPSMgtcpSL---TVLENMALADnkgSSFllqrGVNRRRT-QHYREELSLLhmGL-EDKLGVQVGSLSGG 152
Cdd:PRK13634 83 LRkKVGIVFQFPEH----QLfeeTVEKDICFGP---MNF----GVSEEDAkQKAREMIELV--GLpEELLARSPFELSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 153 Q--RQALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK13634 150 QmrRVAIAGVLA-MEP-EVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTV 224
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-218 |
1.08e-29 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 115.89 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKM--KEYER 78
Cdd:COG1129 4 LLEMRGISKSF-GG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRspRDAQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 79 SRfIGRVFQDPSMgtCPSLTVLENMALADNKGSSFLLQRGVNRRRTQhyreELsLLHMGLEDKLGVQVGSLSGGQRQALA 158
Cdd:COG1129 79 AG-IAIIHQELNL--VPNLSVAENIFLGREPRRGGLIDWRAMRRRAR----EL-LARLGLDIDPDTPVGDLSVAQQQLVE 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 159 MLIATMSPINLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLK--FAVAygDR 218
Cdd:COG1129 151 IARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDevFEIA--DR 209
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
1-227 |
1.50e-29 |
|
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: 110.75 E-value: 1.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYE--- 77
Cdd:cd03258 1 MIELKNVSKVF-GDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrk 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 RSRFIGRVFQdpSMGTCPSLTVLENMALAdnkgssfLLQRGVNR-RRTQHYREELSLLhmGLEDKLGVQVGSLSGGQRQ- 155
Cdd:cd03258 80 ARRRIGMIFQ--HFNLLSSRTVFENVALP-------LEIAGVPKaEIEERVLELLELV--GLEDKADAYPAQLSGGQKQr 148
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 156 -ALAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03258 149 vGIARALAN-NP-KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEV 219
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
23-222 |
1.73e-29 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 115.85 E-value: 1.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMgtcPSLTVLEN 102
Cdd:TIGR02857 339 RPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFL---FAGTIAEN 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 MALADNKGSSFLLQRGVNRRRTQhyrEELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPH 182
Cdd:TIGR02857 416 IRLARPDASDAEIREALERAGLD---EFVAALPQGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDAE 492
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1852789824 183 SSENVMELTQRVAKEKhvTMLMVTHNLKFAVAYgDRLLMM 222
Cdd:TIGR02857 493 TEAEVLEALRALAQGR--TVLLVTHRLALAALA-DRIVVL 529
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
17-207 |
4.00e-29 |
|
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: 109.11 E-value: 4.00e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRfIGRVFQDPsmGTCPS 96
Cdd:COG4133 13 GERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRR-LAYLGHAD--GLKPE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENMALadnkgssFLLQRGVNRRRTQHyrEELsLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIATMSPinLLILDE 174
Cdd:COG4133 90 LTVRENLRF-------WAALYGLRADREAI--DEA-LEAVGLAGLADLPVRQLSAGQKRrvALARLLLSPAP--LWLLDE 157
|
170 180 190
....*....|....*....|....*....|...
gi 1852789824 175 HTAALDPHSSENVMELTQRvAKEKHVTMLMVTH 207
Cdd:COG4133 158 PFTALDAAGVALLAELIAA-HLARGGAVLLTTH 189
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
2-227 |
6.44e-29 |
|
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: 109.25 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrf 81
Cdd:cd03300 1 IELENVSKFYG----GFVAL-DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRP-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQdpSMGTCPSLTVLENMAladnkgssFLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQ--ALAM 159
Cdd:cd03300 74 VNTVFQ--NYALFPHLTVFENIA--------FGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQrvAIAR 143
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 160 LIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03300 144 ALV-NEP-KVLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKI 209
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
24-227 |
6.55e-29 |
|
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: 108.73 E-value: 6.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrfIGRVFQDPSMgtCPSLTVLENM 103
Cdd:cd03298 16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP--VSMLFQENNL--FAHLTVEQNV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 104 ALADNKGssfLLQRGVNRRRTqhyreELSLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIATMSPInlLILDEHTAALDP 181
Cdd:cd03298 92 GLGLSPG---LKLTAEDRQAI-----EVALARVGLAGLEKRLPGELSGGERQrvALARVLVRDKPV--LLLDEPFAALDP 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1852789824 182 HSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03298 162 ALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
18-230 |
2.63e-28 |
|
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: 107.80 E-value: 2.63e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 18 EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRfIGRVFQDPSmgtcpsl 97
Cdd:cd03267 33 EVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRR-IGVVFGQKT------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 98 TVLENMALADnkgsSFLLQR---GVNRRRTQHYREELSLLhMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDE 174
Cdd:cd03267 105 QLWWDLPVID----SFYLLAaiyDLPPARFKKRLDELSEL-LDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 175 HTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:cd03267 180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
5-236 |
2.87e-28 |
|
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: 107.07 E-value: 2.87e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 5 EHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRfIGR 84
Cdd:cd03265 4 ENLVKKYG-----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRR-IGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 85 VFQDPSMGtcPSLTVLENMALadnKGSSFLLQRGVNRRRTqhyrEELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATM 164
Cdd:cd03265 78 VFQDLSVD--DELTGWENLYI---HARLYGVPGAERRERI----DEL-LDFVGLLEAADRLVKTYSGGMRRRLEIARSLV 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 165 SPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM-LDAAGEDK 236
Cdd:cd03265 148 HRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIaEGTPEELK 220
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
1-230 |
2.93e-28 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 107.87 E-value: 2.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVnevvlFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERS- 79
Cdd:PRK09493 1 MIEFKNVSKHFGPTQV-----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLi 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 80 -RFIGRVFQDPSMgtCPSLTVLENMALADNKgssfllQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALA 158
Cdd:PRK09493 76 rQEAGMVFQQFYL--FPHLTALENVMFGPLR------VRGASKEEAEKQAREL-LAKVGLAERAHHYPSELSGGQQQRVA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 159 MLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:PRK09493 147 IARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEG-MTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
|
|
| urea_trans_UrtE |
TIGR03410 |
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ... |
24-242 |
3.91e-28 |
|
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: 107.23 E-value: 3.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF-IGRVFQdpSMGTCPSLTVLEN 102
Cdd:TIGR03410 18 GVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYVPQ--GREIFPRLTVEEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 maladnkgssflLQRG--VNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:TIGR03410 96 ------------LLTGlaALPRRSRKIPDEIYELFPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQ 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 181 PHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGEDKKVLDVR 242
Cdd:TIGR03410 164 PSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVR 225
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
2-228 |
9.19e-28 |
|
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: 106.96 E-value: 9.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTF--NPGSVNE-----------------VVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGE 62
Cdd:cd03294 1 IKIKGLYKIFgkNPQKAFKllakgkskeeilkktgqTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 63 IYVGDRQVTKMKEYE----RSRFIGRVFQdpSMGTCPSLTVLENMALAdnkgssfLLQRGVNRR-RTQHYREELSLlhMG 137
Cdd:cd03294 81 VLIDGQDIAAMSRKElrelRRKKISMVFQ--SFALLPHRTVLENVAFG-------LEVQGVPRAeREERAAEALEL--VG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 138 LEDKLGVQVGSLSGGQRQ--ALAMLIATMSPInlLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAY 215
Cdd:cd03294 150 LEGWEHKYPDELSGGMQQrvGLARALAVDPDI--LLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRL 227
|
250
....*....|...
gi 1852789824 216 GDRLLMMHRGHIM 228
Cdd:cd03294 228 GDRIAIMKDGRLV 240
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
23-225 |
1.58e-27 |
|
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: 105.63 E-value: 1.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTkmkEYERSRFIgrVFQDPSMgtCPSLTVLEN 102
Cdd:TIGR01184 2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT---EPGPDRMV--VFQNYSL--LPWLTVREN 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 MALADNKgssfllqrgVNRRRTQHYREELSLLHM---GLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAAL 179
Cdd:TIGR01184 75 IALAVDR---------VLPDLSKSERRAIVEEHIalvGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGAL 145
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1852789824 180 DPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRG 225
Cdd:TIGR01184 146 DALTRGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
25-230 |
1.79e-27 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 105.43 E-value: 1.79e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 25 FNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrfIGRVFQDPSMgtCPSLTVLENMA 104
Cdd:PRK10771 18 FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRP--VSMLFQENNL--FSHLTVAQNIG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 105 LADNKGssflLQRGVNRRRTQHYREElsllHMGLEDKLGVQVGSLSGGQRQ--ALAMLIATMSPInlLILDEHTAALDPH 182
Cdd:PRK10771 94 LGLNPG----LKLNAAQREKLHAIAR----QMGIEDLLARLPGQLSGGQRQrvALARCLVREQPI--LLLDEPFSALDPA 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1852789824 183 SSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
6-230 |
2.71e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 106.29 E-value: 2.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 6 HIYktfNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVT--KMKEYERSRFIG 83
Cdd:PRK13637 10 HIY---MEGTPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 84 RVFQDPSMGTCPSlTVLENMALA-DNKGssfLLQRGVNRRrtqhYREELSLLHMGLEDKLGVQVGSLSGGQ--RQALAML 160
Cdd:PRK13637 87 LVFQYPEYQLFEE-TIEKDIAFGpINLG---LSEEEIENR----VKRAMNIVGLDYEDYKDKSPFELSGGQkrRVAIAGV 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 161 IAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:PRK13637 159 VA-MEP-KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQ 226
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
3-227 |
2.91e-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: 104.26 E-value: 2.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 3 RMEHIYKTFNPGSVnevvLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVtkmKEYERSRFI 82
Cdd:cd03226 1 RIENISFSYKKGTE----ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 83 GRVFQDPS--MGTCpslTVLENMAL-ADNKGSSfllqrgvnRRRTQHYREELSLLhmGLEDKLGVqvgSLSGGQRQALAM 159
Cdd:cd03226 74 GYVMQDVDyqLFTD---SVREELLLgLKELDAG--------NEQAETVLKDLDLY--ALKERHPL---SLSGGQKQRLAI 137
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 160 LIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03226 138 AAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAI 204
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
24-227 |
4.21e-27 |
|
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: 103.91 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIA---EGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQV----TKMKEYERSRFIGRVFQDPSMgtCPS 96
Cdd:cd03297 12 DFTLKIDfdlNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLfdsrKKINLPPQQRKIGLVFQQYAL--FPH 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENMAladnkgssFLLQRGVNRRRTQHYREELSLlhMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHT 176
Cdd:cd03297 90 LNVRENLA--------FGLKRKRNREDRISVDELLDL--LGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPF 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 177 AALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03297 160 SALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRL 210
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
2-227 |
4.70e-27 |
|
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: 104.34 E-value: 4.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrf 81
Cdd:cd03296 3 IEVRNVSKRFG-----DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSMgtCPSLTVLENMA--LADNKGSSFLLQRGVNRRrtqhYREELSLLHM-GLEDKLGVQvgsLSGGQRQ--A 156
Cdd:cd03296 76 VGFVFQHYAL--FRHMTVFDNVAfgLRVKPRSERPPEAEIRAK----VHELLKLVQLdWLADRYPAQ---LSGGQRQrvA 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 157 LAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03296 147 LARALA-VEP-KVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
13-230 |
1.09e-26 |
|
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: 103.05 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 13 PGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSM- 91
Cdd:cd03245 13 PNQEIPAL--DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLf 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 -GtcpslTVLENMALADNKGSSFLLQR-----GVNrrrtqhyreELSLLH-MGLEDKLGVQVGSLSGGQRQALAMLIATM 164
Cdd:cd03245 91 yG-----TLRDNITLGAPLADDERILRaaelaGVT---------DFVNKHpNGLDLQIGERGRGLSGGQRQAVALARALL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 165 SPINLLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKFaVAYGDRLLMMHRGHIMLD 230
Cdd:cd03245 157 NDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSL-LDLVDRIIVMDSGRIVAD 219
|
|
| CysA |
COG1118 |
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ... |
5-227 |
4.69e-26 |
|
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 104.07 E-value: 4.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 5 EHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQV-TKMKEYERSrfIG 83
Cdd:COG1118 6 RNISKRFG-----SFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERR--VG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 84 RVFQDPSMgtCPSLTVLENMA--LADNKGSsfllqRGVNRRRTqhyREELSLLHM-GLEDKLGVQvgsLSGGQRQ--ALA 158
Cdd:COG1118 79 FVFQHYAL--FPHMTVAENIAfgLRVRPPS-----KAEIRARV---EELLELVQLeGLADRYPSQ---LSGGQRQrvALA 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 159 -MLIAtmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:COG1118 146 rALAV--EP-EVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRI 212
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
1-207 |
9.19e-26 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 103.23 E-value: 9.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGslpL---GSGEIYVGDRQVTKMKEYE 77
Cdd:COG1135 1 MIELENLSKTF-PTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL---LerpTSGSVLVDGVDLTALSERE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 RSRF---IGRVFQDPS-MgtcPSLTVLENMALAdnkgssfLLQRGVNRRRtqhyREE--LSLLHM-GLEDKLGVQVGSLS 150
Cdd:COG1135 77 LRAArrkIGMIFQHFNlL---SSRTVAENVALP-------LEIAGVPKAE----IRKrvAELLELvGLSDKADAYPSQLS 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 151 GGQRQ------ALAMliatmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTH 207
Cdd:COG1135 143 GGQKQrvgiarALAN-----NP-KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH 199
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
2-227 |
9.37e-26 |
|
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: 100.56 E-value: 9.37e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE----YE 77
Cdd:cd03292 1 IEFINVTKTYPNG----TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGraipYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 RsRFIGRVFQDPSMgtCPSLTVLENMALAdnkgssfLLQRGVNRRRTQHyREELSLLHMGLEDKLGVQVGSLSGGQRQAL 157
Cdd:cd03292 77 R-RKIGVVFQDFRL--LPDRNVYENVAFA-------LEVTGVPPREIRK-RVPAALELVGLSHKHRALPAELSGGEQQRV 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 158 AMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKeKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03292 146 AIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINK-AGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
24-225 |
1.12e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 101.75 E-value: 1.12e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPS---MGTCPSLTV- 99
Cdd:PRK13648 27 DVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHIGIVFQNPDnqfVGSIVKYDVa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 --LENMALADNKgssflLQRGVNRrrtqhyreelSLLHMGLEDKLGVQVGSLSGGQRQ--ALAMLIAtMSPiNLLILDEH 175
Cdd:PRK13648 107 fgLENHAVPYDE-----MHRRVSE----------ALKQVDMLERADYEPNALSGGQKQrvAIAGVLA-LNP-SVIILDEA 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1852789824 176 TAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAyGDRLLMMHRG 225
Cdd:PRK13648 170 TSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKG 218
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
26-227 |
1.71e-25 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 104.54 E-value: 1.71e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLgSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMgtcPSLTVLENMAL 105
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELDPESWRKHLSWVGQNPQL---PHGTLRDNVLL 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 106 ADNKGSSFLLQRGVNRRRTQhyrEELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSE 185
Cdd:PRK11174 446 GNPDASDEQLQQALENAWVS---EFLPLLPQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQ 522
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1852789824 186 NVMELTQRVAKEKhvTMLMVTHNLKFAVAYgDRLLMMHRGHI 227
Cdd:PRK11174 523 LVMQALNAASRRQ--TTLMVTHQLEDLAQW-DQIWVMQDGQI 561
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
2-227 |
1.84e-25 |
|
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: 98.27 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnpGSVneVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTkMKEYERSRF 81
Cdd:cd03216 1 LELRGITKRF--GGV--KAL-DGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVS-FASPRDARR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 --IGRVFQdpsmgtcpsltvlenmaladnkgssfllqrgvnrrrtqhyreelsllhmgledklgvqvgsLSGGQRQALAM 159
Cdd:cd03216 75 agIAMVYQ-------------------------------------------------------------LSVGERQMVEI 93
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 160 LIATMSPINLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03216 94 ARALARNARLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRV 160
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
15-249 |
2.32e-25 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 103.00 E-value: 2.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPS---- 90
Cdd:PRK09536 12 EFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVPQDTSlsfe 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 91 --------MGTCPSLTVLENMALADNKGssflLQRGVNRRRTQHYREElsllhmgledklgvQVGSLSGGQRQ--ALAML 160
Cdd:PRK09536 92 fdvrqvveMGRTPHRSRFDTWTETDRAA----VERAMERTGVAQFADR--------------PVTSLSGGERQrvLLARA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 161 IATMSPInlLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGEDKKVLD 240
Cdd:PRK09536 154 LAQATPV--LLLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVR--AAGPPADVLT 228
|
....*....
gi 1852789824 241 VRDLTNRFD 249
Cdd:PRK09536 229 ADTLRAAFD 237
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
1-239 |
2.65e-25 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 103.57 E-value: 2.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPgsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVtkmkeyersR 80
Cdd:COG3845 5 ALELRGITKRFGG-----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPV---------R 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 F----------IGRVFQDPSMgtCPSLTVLENMALADNKGSSFLLQRGVNRRRTqhyrEELSlLHMGLEDKLGVQVGSLS 150
Cdd:COG3845 71 IrsprdaialgIGMVHQHFML--VPNLTVAENIVLGLEPTKGGRLDRKAARARI----RELS-ERYGLDVDPDAKVEDLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 151 GGQRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHIM-- 228
Cdd:COG3845 144 VGEQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAEGK-SIIFITHKLREVMAIADRVTVLRRGKVVgt 222
|
250
....*....|.
gi 1852789824 229 LDAAGEDKKVL 239
Cdd:COG3845 223 VDTAETSEEEL 233
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
24-239 |
3.21e-25 |
|
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: 99.72 E-value: 3.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrfIGRVFQDPSMgtCPSLTVLENM 103
Cdd:cd03299 17 NVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRD--ISYVPQNYAL--FPHMTVYKNI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 104 ALAdnkgssfLLQRGVNRRRTQHYREELSLLhMGLEDKLGVQVGSLSGG--QRQALAMLIaTMSPiNLLILDEHTAALDP 181
Cdd:cd03299 93 AYG-------LKKRKVDKKEIERKVLEIAEM-LGIDHLLNRKPETLSGGeqQRVAIARAL-VVNP-KILLLDEPFSALDV 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 182 HSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGEDKKVL 239
Cdd:cd03299 163 RTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI--QVGKPEEVF 218
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
2-244 |
3.22e-25 |
|
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: 99.48 E-value: 3.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPgsvNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYV-GDRQVTKMKEYERsR 80
Cdd:cd03252 1 ITFEHVRFRYKP---DGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVdGHDLALADPAWLR-R 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDpsmGTCPSLTVLENMALADNKGSsflLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAML 160
Cdd:cd03252 77 QVGVVLQE---NVLFNRSIRDNIALADPGMS---MERVIEAAKLAGAHDFISELPEGYDTIVGEQGAGLSGGQRQRIAIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 161 IATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHIMldAAGEDKKVLD 240
Cdd:cd03252 151 RALIHNPRILIFDEATSALDYESEHAIMRNMHDICAGR--TVIIIAHRLS-TVKNADRIIVMEKGRIV--EQGSHDELLA 225
|
....
gi 1852789824 241 VRDL 244
Cdd:cd03252 226 ENGL 229
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
1-239 |
3.23e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 100.45 E-value: 3.23e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNevvLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:PRK13632 7 MIKVENVSFSYPNSENN---ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPS---MGtcpsLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELSlLHMGLEDKLGVQVGSLSGGQRQAL 157
Cdd:PRK13632 84 KIGIIFQNPDnqfIG----ATVEDDIAFG-------LENKKVPPKKMKDIIDDLA-KKVGMEDYLDKEPQNLSGGQKQRV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 158 AmlIATMSPIN--LLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAyGDRLLMMHRGHIMldAAGED 235
Cdd:PRK13632 152 A--IASVLALNpeIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAIL-ADKVIVFSEGKLI--AQGKP 226
|
....
gi 1852789824 236 KKVL 239
Cdd:PRK13632 227 KEIL 230
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
24-228 |
5.07e-25 |
|
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: 100.90 E-value: 5.07e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG---SGEIYVGDRQVTKMKEYERSRFIGR----VFQDPsMGTC-P 95
Cdd:COG0444 23 GVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKELRKIRGReiqmIFQDP-MTSLnP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 96 SLTVLENMALAdnkgssFLLQRGVNRR-RTQHYREELSLlhMGLEDKLGV------QvgsLSGGQRQ--ALAMLIAtMSP 166
Cdd:COG0444 102 VMTVGDQIAEP------LRIHGGLSKAeARERAIELLER--VGLPDPERRldryphE---LSGGMRQrvMIARALA-LEP 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 167 iNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLkfAVAYG--DRLLMMHRGHIM 228
Cdd:COG0444 170 -KLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDL--GVVAEiaDRVAVMYAGRIV 230
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
17-207 |
8.79e-25 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 97.94 E-value: 8.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG---SGEIYVGDRQVTKMKEYERSrfIGRVFQDPSMgt 93
Cdd:COG4136 12 GGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQRR--IGILFQDDLL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 94 CPSLTVLENMALAdnkgssflLQRGVNRR----RTQHYREELSLLHMGLEDklgvqVGSLSGGQRQALAMLIATMSPINL 169
Cdd:COG4136 88 FPHLSVGENLAFA--------LPPTIGRAqrraRVEQALEEAGLAGFADRD-----PATLSGGQRARVALLRALLAEPRA 154
|
170 180 190
....*....|....*....|....*....|....*...
gi 1852789824 170 LILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTH 207
Cdd:COG4136 155 LLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTH 192
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-248 |
1.03e-24 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 98.45 E-value: 1.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG-----SGEIYVGDRQVTKMKEYERSRFIGRVFQDP 89
Cdd:PRK14247 12 SFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIFKMDVIELRRRVQMVFQIP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SmgTCPSLTVLENMALAdnkgssFLLQRGVNRRRTQHYREELSL----LHMGLEDKLGVQVGSLSGGQRQALAMLIATMS 165
Cdd:PRK14247 92 N--PIPNLSIFENVALG------LKLNRLVKSKKELQERVRWALekaqLWDEVKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 166 PINLLILDEHTAALDPHSSENVMELTQRVAKEkhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGEDKKVLDVRDLT 245
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELT 241
|
...
gi 1852789824 246 NRF 248
Cdd:PRK14247 242 EKY 244
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
1-249 |
1.15e-24 |
|
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA [Inorganic ion transport and metabolism];
Pssm-ID: 440736 [Multi-domain] Cd Length: 250 Bit Score: 98.23 E-value: 1.15e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIyktfnpgSV--NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSG-EIYVGDRQVTKMKEYE 77
Cdd:COG1119 3 LLELRNV-------TVrrGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 -RSRfIGRVfqDPSMGT--CPSLTVLEnMALAdnkG--SSFLLQRGVNRRRTQHYREELSLLhmGLEDKLGVQVGSLSGG 152
Cdd:COG1119 76 lRKR-IGLV--SPALQLrfPRDETVLD-VVLS---GffDSIGLYREPTDEQRERARELLELL--GLAHLADRPFGTLSQG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 153 QRQaLAMLI-ATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldA 231
Cdd:COG1119 147 EQR-RVLIArALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV--A 223
|
250
....*....|....*...
gi 1852789824 232 AGEDKKVLDVRDLTNRFD 249
Cdd:COG1119 224 AGPKEEVLTSENLSEAFG 241
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
1-239 |
1.32e-24 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 98.91 E-value: 1.32e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVnevvLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYV-----GDrqVTKMKE 75
Cdd:PRK13644 1 MIRLENVSYSYPDGTP----ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVsgidtGD--FSKLQG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 76 YErsRFIGRVFQDPSMGTCpSLTVLENMALadnkGSSFLLQRGVNRRRtqhyREELSLLHMGLEDKLGVQVGSLSGGQRQ 155
Cdd:PRK13644 75 IR--KLVGIVFQNPETQFV-GRTVEEDLAF----GPENLCLPPIEIRK----RVDRALAEIGLEKYRHRSPKTLSGGQGQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 156 ALAML-IATMSPiNLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKfAVAYGDRLLMMHRGHIMLDaaGE 234
Cdd:PRK13644 144 CVALAgILTMEP-ECLIFDEVTSMLDPDSGIAVLERIKKL-HEKGKTIVYITHNLE-ELHDADRIIVMDRGKIVLE--GE 218
|
....*
gi 1852789824 235 DKKVL 239
Cdd:PRK13644 219 PENVL 223
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
24-230 |
1.44e-24 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 98.21 E-value: 1.44e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERsrfigRVFQDPSMgtCPSLTVLENM 103
Cdd:PRK11247 30 QLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAGTAPLAEAREDTR-----LMFQDARL--LPWKKVIDNV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 104 ALAdnkgssfllQRGvnrrrtqHYREEL--SLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDP 181
Cdd:PRK11247 103 GLG---------LKG-------QWRDAAlqALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDA 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1852789824 182 HSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:PRK11247 167 LTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD 215
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
13-237 |
2.21e-24 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 101.72 E-value: 2.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 13 PGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLL-CGSLPlGSGEIYVGDRQVTKMKEYE----RSRFIGRVFQ 87
Cdd:PRK10535 15 PSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgCLDKP-TSGTYRVAGQDVATLDADAlaqlRREHFGFIFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 88 DPSMgtCPSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPI 167
Cdd:PRK10535 94 RYHL--LSHLTAAQNVEVP-------AVYAGLERKQRLLRAQEL-LQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 168 NLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAvAYGDRLLMMHRGHIMLDAAGEDKK 237
Cdd:PRK10535 164 QVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVA-AQAERVIEIRDGEIVRNPPAQEKV 231
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
18-227 |
2.22e-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: 97.23 E-value: 2.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 18 EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGTCpsl 97
Cdd:cd03249 15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDG--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 98 TVLENMALADNKgssfllqrgvnrrRTQHYREE---LSLLH---MGLEDKLGVQVG----SLSGGQRQALAMLIATMSPI 167
Cdd:cd03249 92 TIAENIRYGKPD-------------ATDEEVEEaakKANIHdfiMSLPDGYDTLVGergsQLSGGQKQRIAIARALLRNP 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 168 NLLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:cd03249 159 KILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLS-TIRNADLIAVLQNGQV 215
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
1-257 |
5.51e-24 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 96.69 E-value: 5.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:COG4604 1 MIEIKNVSKRYG----GKVVL-DDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPSMGTcpSLTVLENMALAD---NKGssfllqrgvnrRRTQHYRE--ELSLLHMGLEDKLGVQVGSLSGGQRQ 155
Cdd:COG4604 76 RLAILRQENHINS--RLTVRELVAFGRfpySKG-----------RLTAEDREiiDEAIAYLDLEDLADRYLDELSGGQRQ 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 156 -A-LAMLIATMSPInlLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAG 233
Cdd:COG4604 143 rAfIAMVLAQDTDY--VLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVV--AQG 218
|
250 260
....*....|....*....|....*
gi 1852789824 234 EDKKVLDVRDLTNRFD-EISVEDGN 257
Cdd:COG4604 219 TPEEIITPEVLSDIYDtDIEVEEID 243
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
2-235 |
1.04e-23 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 97.87 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVnevvlFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKmkeyeRS-- 79
Cdd:PRK11432 7 VVLKNITKRFGSNTV-----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH-----RSiq 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 80 -RFIGRVFQdpsmgtcpSLTVLENMALADNKGSSFLLQrGVNR-RRTQHYREELSLLHM-GLEDKLgvqVGSLSGGQRQA 156
Cdd:PRK11432 77 qRDICMVFQ--------SYALFPHMSLGENVGYGLKML-GVPKeERKQRVKEALELVDLaGFEDRY---VDQISGGQQQR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 157 LAMLIATMSPINLLILDEHTAALDPH----SSENVMELTQRVakekHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAA 232
Cdd:PRK11432 145 VALARALILKPKVLLFDEPLSNLDANlrrsMREKIRELQQQF----NITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGS 220
|
...
gi 1852789824 233 GED 235
Cdd:PRK11432 221 PQE 223
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
22-209 |
1.05e-23 |
|
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.
Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 99.36 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSM-GTcpslTVL 100
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCAQDAHLfDT----TVR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALADNKGSSFLLQRGVNRRRTQHYREELSllhMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:TIGR02868 427 ENLRLARPDATDEELWAALERVGLADWLRALP---DGLDTVLGEGGARLSGGERQRLALARALLADAPILLLDEPTEHLD 503
|
170 180
....*....|....*....|....*....
gi 1852789824 181 PHSSENVMELTQRVAKEKhvTMLMVTHNL 209
Cdd:TIGR02868 504 AETADELLEDLLAALSGR--TVVLITHHL 530
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
18-227 |
1.44e-23 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 99.02 E-value: 1.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 18 EVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPsmgtcpsl 97
Cdd:PRK10790 354 NLVL-QNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQDP-------- 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 98 tvlenMALADNKGSSFLLQRGVNRRRTQHYREELSL------LHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLI 171
Cdd:PRK10790 425 -----VVLADTFLANVTLGRDISEEQVWQALETVQLaelarsLPDGLYTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 172 LDEHTAALDPHSSENVMELTQRVakEKHVTMLMVTHNLKFAVAyGDRLLMMHRGHI 227
Cdd:PRK10790 500 LDEATANIDSGTEQAIQQALAAV--REHTTLVVIAHRLSTIVE-ADTILVLHRGQA 552
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
17-230 |
2.17e-23 |
|
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: 93.15 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEyERSRFIGRVFQDPSMGtcpS 96
Cdd:cd03247 13 QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISVLNQRPYLF---D 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENmaladnkgssfllqrgvnrrrtqhyreelsllhmgledkLGVQvgsLSGGQRQALAMLIATMSPINLLILDEHT 176
Cdd:cd03247 89 TTLRNN---------------------------------------LGRR---FSGGERQRLALARILLQDAPIVLLDEPT 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 177 AALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHIMLD 230
Cdd:cd03247 127 VGLDPITERQLLSLIFEVLKDK--TLIWITHHLT-GIEHMDKILFLENGKIIMQ 177
|
|
| ModC |
COG4148 |
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ... |
24-233 |
2.56e-23 |
|
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: 96.71 E-value: 2.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDR------QVTKMKEYERSrfIGRVFQDPSMgtCPSL 97
Cdd:COG4148 17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqdsaRGIFLPPHRRR--IGYVFQEARL--FPHL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 98 TVLENMALAdnkgssflLQRGVNRRRTQHYREELSLLhmGLEDKLGVQVGSLSGGQRQ--ALAMLIATmSPiNLLILDEH 175
Cdd:COG4148 93 SVRGNLLYG--------RKRAPRAERRISFDEVVELL--GIGHLLDRRPATLSGGERQrvAIGRALLS-SP-RLLLMDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 176 TAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAG 233
Cdd:COG4148 161 LAALDLARKAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV--ASG 216
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
24-227 |
3.18e-23 |
|
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: 93.80 E-value: 3.18e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFvAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRfIGRVFQDPsmGTCPSLTV---L 100
Cdd:cd03264 18 GVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRR-IGYLPQEF--GVYPNFTVrefL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALAdnkgssfllqRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:cd03264 94 DYIAWL----------KGIPSKEVKARVDEV-LELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLD 162
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1852789824 181 PHSSENVMELTQRVAKEKhvTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03264 163 PEERIRFRNLLSELGEDR--IVILSTHIVEDVESLCNQVAVLNKGKL 207
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-256 |
5.00e-23 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.54 E-value: 5.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTF-----NPGSVN-----------EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIY 64
Cdd:COG4586 1 IIEVENLSKTYrvyekEPGLKGalkglfrreyrEVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 65 VGDRQVTKmkeyERSRF---IGRVF-Q------DpsmgtcpsLTVLEnmaladnkgsSFLLQR---GVNRRRTQHYREEL 131
Cdd:COG4586 81 VLGYVPFK----RRKEFarrIGVVFgQrsqlwwD--------LPAID----------SFRLLKaiyRIPDAEYKKRLDEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 132 SLLhMGLEDKLGVQVGSLSGGQRqalaM---LIATM--SPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVT 206
Cdd:COG4586 139 VEL-LDLGELLDTPVRQLSLGQR----MrceLAAALlhRP-KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTS 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 207 HNLKFAVAYGDRLLMMHRGHIMLDAAGED-------KKVLDVrDLTNRFDEISVEDG 256
Cdd:COG4586 213 HDMDDIEALCDRVIVIDHGRIIYDGSLEElkerfgpYKTIVL-ELAEPVPPLELPRG 268
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
4-240 |
1.12e-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: 96.73 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 4 MEHIykTFNPGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIG 83
Cdd:TIGR01193 476 INDV--SYSYGYGSNIL--SDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 84 RVFQDPSMGTCpslTVLENMALADNKGSSfllQRGVNRR-RTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIA 162
Cdd:TIGR01193 552 YLPQEPYIFSG---SILENLLLGAKENVS---QDEIWAAcEIAEIKDDIENMPLGYQTELSEEGSSISGGQKQRIALARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 163 TMSPINLLILDEHTAALDPHSSENVMEltqRVAKEKHVTMLMVTHNLKFAvAYGDRLLMMHRGHIMLDaaGEDKKVLD 240
Cdd:TIGR01193 626 LLTDSKVLILDESTSNLDTITEKKIVN---NLLNLQDKTIIFVAHRLSVA-KQSDKIIVLDHGKIIEQ--GSHDELLD 697
|
|
| AztA |
NF040873 |
zinc ABC transporter ATP-binding protein AztA; |
20-222 |
1.59e-22 |
|
zinc ABC transporter ATP-binding protein AztA;
Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 91.14 E-value: 1.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGdrqvtkmkeyeRSRFIGRVFQDPSMGTCPSLTV 99
Cdd:NF040873 6 PVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRA-----------GGARVAYVPQRSEVPDSLPLTV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMALadnkgsSFLLQRGVNRRRTQHYREEL--SLLHMGLEDKLGVQVGSLSGGQRQA--LAMLIATMSpiNLLILDEH 175
Cdd:NF040873 75 RDLVAM------GRWARRGLWRRLTRDDRAAVddALERVGLADLAGRQLGELSGGQRQRalLAQGLAQEA--DLLLLDEP 146
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1852789824 176 TAALDPHSSENVMELTQRVAKEKhVTMLMVTHNLKfAVAYGDRLLMM 222
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHARG-ATVVVVTHDLE-LVRRADPCVLL 191
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
2-227 |
2.59e-22 |
|
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: 91.84 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPgsvNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:cd03218 1 LRAENLSKRYGK---RKVV--NGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 -IGRVFQDPSMGTcpSLTVLENMALAdnkgssfLLQRGVNR----RRTQHYREELSLLHmgLEDKLGvqvGSLSGGQRQA 156
Cdd:cd03218 76 gIGYLPQEASIFR--KLTVEENILAV-------LEIRGLSKkereEKLEELLEEFHITH--LRKSKA---SSLSGGERRR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 157 LAmlIATMSPIN--LLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03218 142 VE--IARALATNpkFLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKV 211
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
24-227 |
2.64e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 92.87 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPS---MGTcpslTVL 100
Cdd:PRK13650 25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPDnqfVGA----TVE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALA-DNKGSSflLQRGVNRrrtqhYREELSLLhmGLEDKLGVQVGSLSGGQRQ--ALAMLIAtMSPiNLLILDEHTA 177
Cdd:PRK13650 101 DDVAFGlENKGIP--HEEMKER-----VNEALELV--GMQDFKEREPARLSGGQKQrvAIAGAVA-MRP-KIIILDEATS 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1852789824 178 ALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:PRK13650 170 MLDPEGRLELIKTIKGIRDDYQMTVISITHDLD-EVALSDRVLVMKNGQV 218
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
2-227 |
4.23e-22 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 93.56 E-value: 4.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrf 81
Cdd:PRK11000 4 VTLRNVTKAYG-----DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG-- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQdpSMGTCPSLTVLENMaladnkgsSFLLQ-RGVNR----RRTQHYREELSLLHMgledkLGVQVGSLSGGQRQA 156
Cdd:PRK11000 77 VGMVFQ--SYALYPHLSVAENM--------SFGLKlAGAKKeeinQRVNQVAEVLQLAHL-----LDRKPKALSGGQRQR 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 157 LAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK11000 142 VAIGRTLVAEPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRV 212
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
4-228 |
5.58e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 91.99 E-value: 5.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 4 MEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQV----TKMKEYER- 78
Cdd:PRK13645 9 LDNVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIpanlKKIKEVKRl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 79 SRFIGRVFQDPSMGTCPSlTVLENMALADnkgssflLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQ--RQA 156
Cdd:PRK13645 89 RKEIGLVFQFPEYQLFQE-TIEKDIAFGP-------VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQkrRVA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 157 LAMLIATMSpiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK13645 161 LAGIIAMDG--NTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVI 230
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
1-227 |
6.68e-22 |
|
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: 90.50 E-value: 6.68e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:cd03266 1 MITADALTKRFRDVKKTVQAV-DGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 fIGRVFQdpSMGTCPSLTVLENMALadnkgssFLLQRGVNRRRTQHYREELSLLhMGLEDKLGVQVGSLSGGQRQALAML 160
Cdd:cd03266 80 -LGFVSD--STGLYDRLTARENLEY-------FAGLYGLKGDELTARLEELADR-LGMEELLDRRVGGFSTGMRQKVAIA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 161 IATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03266 149 RALVHDPPVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRV 214
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
1-228 |
7.35e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 91.72 E-value: 7.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVT---KMKEYE 77
Cdd:PRK13643 1 MIKFEKVNYTYQPNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSstsKQKEIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 RSR-FIGRVFQDPSMGTCPSlTVLENMALADNkgssfllQRGVNRRRTQHYREElSLLHMGLEDKLGVQVG-SLSGGQ-- 153
Cdd:PRK13643 81 PVRkKVGVVFQFPESQLFEE-TVLKDVAFGPQ-------NFGIPKEKAEKIAAE-KLEMVGLADEFWEKSPfELSGGQmr 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 154 RQALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK13643 152 RVAIAGILA-MEP-EVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHII 223
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
1-234 |
1.04e-21 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 90.84 E-value: 1.04e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNEVVlfqdfNLQIAEGSFVAVVGSNGSGKTTILNLLCGslpLGSGEIYVG----------DRQV 70
Cdd:PRK09984 4 IIRVEKLAKTFNQHQALHAV-----DLNIHHGEMVALLGPSGSGKSTLLRHLSG---LITGDKSAGshiellgrtvQREG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 71 TKMKEYERSR-FIGRVFQDPSMgtCPSLTVLENMaLADNKGSSFLLQRGVNR-RRTQHYREELSLLHMGLEDKLGVQVGS 148
Cdd:PRK09984 76 RLARDIRKSRaNTGYIFQQFNL--VNRLSVLENV-LIGALGSTPFWRTCFSWfTREQKQRALQALTRVGMVHFAHQRVST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 149 LSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK09984 153 LSGGQQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVF 232
|
....*.
gi 1852789824 229 LDAAGE 234
Cdd:PRK09984 233 YDGSSQ 238
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
2-229 |
1.25e-21 |
|
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: 89.26 E-value: 1.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnpGSVNEVvlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTkmkeYERSRF 81
Cdd:cd03269 1 LEVENVTKRF--GRVTAL---DDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDpsMGTCPSLTVLENMAladnkgssFLLQ-RGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAML 160
Cdd:cd03269 72 IGYLPEE--RGLYPKMKVIDQLV--------YLAQlKGLKKEEARRRIDEW-LERLELSEYANKRVEELSKGNQQKVQFI 140
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 161 IATMSPINLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIML 229
Cdd:cd03269 141 AAVIHDPELLILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
1-234 |
1.88e-21 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 90.14 E-value: 1.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnPGsvnEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKmKEYERsr 80
Cdd:PRK11248 1 MLQISHLYADY-GG---KPAL-EDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG-PGAER-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 fiGRVFQDPsmGTCPSLTVLENMAladnkgssFLLQ-RGVNR-RRTQHYREELSLLhmGLEDKLGVQVGSLSGGQRQALA 158
Cdd:PRK11248 73 --GVVFQNE--GLLPWRNVQDNVA--------FGLQlAGVEKmQRLEIAHQMLKKV--GLEGAEKRYIWQLSGGQRQRVG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 159 MLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRG------HIMLD-- 230
Cdd:PRK11248 139 IARALAANPQLLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGpgrvveRLPLNfa 218
|
....*..
gi 1852789824 231 ---AAGE 234
Cdd:PRK11248 219 rrfVAGE 225
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
1-240 |
3.96e-21 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 88.99 E-value: 3.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTF-----------------NPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEI 63
Cdd:COG1134 4 MIEVENVSKSYrlyhepsrslkelllrrRRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 64 YVGdrqvtkmkeyersrfiGRV--FQDPSMGTCPSLTVLENMALadnkGSSFLlqrGVNRRRTQHYR---EELSllhmGL 138
Cdd:COG1134 84 EVN----------------GRVsaLLELGAGFHPELTGRENIYL----NGRLL---GLSRKEIDEKFdeiVEFA----EL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 139 EDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPH----SSENVMELtqrvaKEKHVTMLMVTHNLKFAVA 214
Cdd:COG1134 137 GDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAfqkkCLARIREL-----RESGRTVIFVSHSMGAVRR 211
|
250 260
....*....|....*....|....*.
gi 1852789824 215 YGDRLLMMHRGHIMLDaaGEDKKVLD 240
Cdd:COG1134 212 LCDRAIWLEKGRLVMD--GDPEEVIA 235
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
9-227 |
5.03e-21 |
|
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.
Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 87.97 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 9 KTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVgDRQVTKMKEyersrfIGRVFQd 88
Cdd:cd03220 25 ILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV-RGRVSSLLG------LGGGFN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 89 psmgtcPSLTVLENMALadnkgssFLLQRGVNRRRTQHYRE---ELSllhmGLEDKLGVQVGSLSGGQRQALAMLIATMS 165
Cdd:cd03220 97 ------PELTGRENIYL-------NGRLLGLSRKEIDEKIDeiiEFS----ELGDFIDLPVKTYSSGMKARLAFAIATAL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 166 PINLLILDEHTAALDPHSSENVME-LTQRVAKEKhvTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03220 160 EPDILLIDEVLAVGDAAFQEKCQRrLRELLKQGK--TVILVSHDPSSIKRLCDRALVLEKGKI 220
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
21-238 |
9.16e-21 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 88.65 E-value: 9.16e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFqDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVT---KMKEYERSR-FIGRVFQDPSMGTCPS 96
Cdd:PRK13649 23 LF-DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsKNKDIKQIRkKVGLVFQFPESQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 lTVLENMALA-DNKGSSfllqrgvNRRRTQHYREELSLLHMGlEDKLGVQVGSLSGGQ--RQALAMLIAtMSPiNLLILD 173
Cdd:PRK13649 102 -TVLKDVAFGpQNFGVS-------QEEAEALAREKLALVGIS-ESLFEKNPFELSGGQmrRVAIAGILA-MEP-KILVLD 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 174 EHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLdaAGEDKKV 238
Cdd:PRK13649 171 EPTAGLDPKGRKELMTLFKKL-HQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVL--SGKPKDI 232
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
27-244 |
1.38e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 87.87 E-value: 1.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 27 LQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSmGTCPSLTVLENMALA 106
Cdd:PRK13647 26 LSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGLVFQDPD-DQVFSSTVWDDVAFG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 107 D-NKGssfLLQRGVNRRrtqhYREELSLLHM-GLEDKLGVQvgsLSGGQ--RQALAMLIAtMSPiNLLILDEHTAALDPH 182
Cdd:PRK13647 105 PvNMG---LDKDEVERR----VEEALKAVRMwDFRDKPPYH---LSYGQkkRVAIAGVLA-MDP-DVIVLDEPMAYLDPR 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 183 SSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGeDKKVLDVRDL 244
Cdd:PRK13647 173 GQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVL--AEG-DKSLLTDEDI 230
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
1-228 |
1.66e-20 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 87.50 E-value: 1.66e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTIL---NLLcgSLPlGSGEIYVGD------RQVT 71
Cdd:PRK11264 3 AIEVKNLVKKFH----GQTVL-HGIDLEVKPGEVVAIIGPSGSGKTTLLrciNLL--EQP-EAGTIRVGDitidtaRSLS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 72 KMKEYERS--RFIGRVFQdpSMGTCPSLTVLENMAladnKGSsfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSL 149
Cdd:PRK11264 75 QQKGLIRQlrQHVGFVFQ--NFNLFPHRTVLENII----EGP--VIVKGEPKEEATARAREL-LAKVGLAGKETSYPRRL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 150 SGGQRQALAMLIA-TMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK11264 146 SGGQQQRVAIARAlAMRP-EVILFDEPTSALDPELVGEVLNTIRQLAQEKR-TMVIVTHEMSFARDVADRAIFMDQGRIV 223
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
10-227 |
1.98e-20 |
|
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: 85.35 E-value: 1.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 10 TFNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDP 89
Cdd:cd03246 7 SFRYPGAEPPVL-RNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SM--GTcpsltvlenmaLADNkgssfllqrgvnrrrtqhyreelsllhmgledklgvqvgSLSGGQRQALAMLIATMSPI 167
Cdd:cd03246 86 ELfsGS-----------IAEN---------------------------------------ILSGGQRQRLGLARALYGNP 115
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 168 NLLILDEHTAALDPHSSENVMELTQRvAKEKHVTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:cd03246 116 RILVLDEPNSHLDVEGERALNQAIAA-LKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
1-207 |
2.39e-20 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 88.32 E-value: 2.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTIL---NLLcgSLPlGSGEIYVGDRQVTKMKEYE 77
Cdd:PRK11153 1 MIELKNISKVF-PQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIrciNLL--ERP-TSGRVLVDGQDLTALSEKE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 RSRF---IGRVFQDPSMGTcpSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQR 154
Cdd:PRK11153 77 LRKArrqIGMIFQHFNLLS--SRTVFDNVALP-------LELAGTPKAEIKARVTEL-LELVGLSDKADRYPAQLSGGQK 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 155 Q--ALAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTH 207
Cdd:PRK11153 147 QrvAIARALAS-NP-KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
1-228 |
2.64e-20 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 87.98 E-value: 2.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGD----------RQV 70
Cdd:PRK13631 21 ILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDiyigdkknnhELI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 71 T-----KMKEYERSR-FIGRVFQDPSM----GTCPSLTVLENMALADNKGSSfllqrgvnRRRTQHYreelsLLHMGL-E 139
Cdd:PRK13631 101 TnpyskKIKNFKELRrRVSMVFQFPEYqlfkDTIEKDIMFGPVALGVKKSEA--------KKLAKFY-----LNKMGLdD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 140 DKLGVQVGSLSGGQ--RQALAMLIATMSPInlLILDEHTAALDPHSSENVMELTQRvAKEKHVTMLMVTHNLKFAVAYGD 217
Cdd:PRK13631 168 SYLERSPFGLSGGQkrRVAIAGILAIQPEI--LIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVAD 244
|
250
....*....|.
gi 1852789824 218 RLLMMHRGHIM 228
Cdd:PRK13631 245 EVIVMDKGKIL 255
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
2-232 |
2.97e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 87.19 E-value: 2.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVT------KMKE 75
Cdd:PRK13641 3 IKFENVDYIYSPGTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpetgnkNLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 76 YERSrfIGRVFQdpsmgtCPSLTVLENMALAD------NKGSSfllqrgvnrrrTQHYREELS--LLHMGLEDKLGVQVG 147
Cdd:PRK13641 83 LRKK--VSLVFQ------FPEAQLFENTVLKDvefgpkNFGFS-----------EDEAKEKALkwLKKVGLSEDLISKSP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 148 -SLSGGQ--RQALAMLIATMSPInlLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHR 224
Cdd:PRK13641 144 fELSGGQmrRVAIAGVMAYEPEI--LCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEH 220
|
....*...
gi 1852789824 225 GHIMLDAA 232
Cdd:PRK13641 221 GKLIKHAS 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
2-227 |
3.09e-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: 86.13 E-value: 3.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVnevvLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:cd03253 1 IEFENVTFAYDPGRP----VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDpsmgtcpslTVLENMALADNkgssflLQRG---------VNRRRTQHYREELsllhMGLEDKLGVQVGS---- 148
Cdd:cd03253 77 IGVVPQD---------TVLFNDTIGYN------IRYGrpdatdeevIEAAKAAQIHDKI----MRFPDGYDTIVGErglk 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 149 LSGGQRQ--ALAMLIATMSPInlLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGH 226
Cdd:cd03253 138 LSGGEKQrvAIARAILKNPPI--LLLDEATSALDTHTEREIQAALRDVSKGR--TTIVIAHRLS-TIVNADKIIVLKDGR 212
|
.
gi 1852789824 227 I 227
Cdd:cd03253 213 I 213
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
2-225 |
3.62e-20 |
|
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: 85.21 E-value: 3.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGdrqvtkmkeyersrf 81
Cdd:cd03250 1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 igrvfqdPSMGTCPSLTVLENMALADNK--GSSFLLQRgvnrrrtqhYRE---------ELSLLHMGLEDKLGVQVGSLS 150
Cdd:cd03250 66 -------GSIAYVSQEPWIQNGTIRENIlfGKPFDEER---------YEKvikacalepDLEILPDGDLTEIGEKGINLS 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 151 GGQRQALAMLIATMSPINLLILDEHTAALDPHSSENVME--LTQRVAKEKhvTMLMVTHNLKFaVAYGDRLLMMHRG 225
Cdd:cd03250 130 GGQKQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFEncILGLLLNNK--TRILVTHQLQL-LPHADQIVVLDNG 203
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
9-227 |
3.83e-20 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 86.02 E-value: 3.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 9 KTFNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKM----KEYERSRFIGR 84
Cdd:PRK11629 13 KRYQEGSVQTDVL-HNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLssaaKAELRNQKLGF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 85 VFQDPSMgtCPSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATM 164
Cdd:PRK11629 92 IYQFHHL--LPDFTALENVAMP-------LLIGKKKPAEINSRALEM-LAAVGLEHRANHRPSELSGGERQRVAIARALV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 165 SPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYgDRLLMMHRGHI 227
Cdd:PRK11629 162 NNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRL 223
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
1-227 |
3.92e-20 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 88.97 E-value: 3.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRqvTKMKEY--ER 78
Cdd:COG0488 315 VLELEGLSKSYG-----DKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGET--VKIGYFdqHQ 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 79 SRFigrvfqDPSMgtcpslTVLENMaladnkgssfllQRGVNRRRTQHYReelSLL-HMGL-EDKLGVQVGSLSGGQRQA 156
Cdd:COG0488 388 EEL------DPDK------TVLDEL------------RDGAPGGTEQEVR---GYLgRFLFsGDDAFKPVGVLSGGEKAR 440
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 157 LAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKekhvTMLMVTHNLKF--AVAygDRLLMMHRGHI 227
Cdd:COG0488 441 LALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFPG----TVLLVSHDRYFldRVA--TRILEFEDGGV 507
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
26-232 |
4.00e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 87.07 E-value: 4.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSmGTCPSLTVLENMAL 105
Cdd:PRK13642 27 SFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPD-NQFVGATVEDDVAF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 106 A-DNKGSSfllqrgvnrRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAML-IATMSPiNLLILDEHTAALDPHS 183
Cdd:PRK13642 106 GmENQGIP---------REEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAgIIALRP-EIIILDESTSMLDPTG 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1852789824 184 SENVMELTQRVAKEKHVTMLMVTHNLKFAvAYGDRLLMMHRGHIMLDAA 232
Cdd:PRK13642 176 RQEIMRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAA 223
|
|
| nickel_nikE |
TIGR02769 |
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ... |
6-228 |
4.96e-20 |
|
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: 86.40 E-value: 4.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 6 HIYKT--FNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF-- 81
Cdd:TIGR02769 10 HTYRTggLFGAKQRAPVL-TNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFrr 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 -IGRVFQDPSMGTCPSLTVLENMALADNKGSSflLQRGVNRRRTQHYREELSLL--HMgleDKLGVQvgsLSGGQRQALA 158
Cdd:TIGR02769 89 dVQLVFQDSPSAVNPRMTVRQIIGEPLRHLTS--LDESEQKARIAELLDMVGLRseDA---DKLPRQ---LSGGQLQRIN 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 159 MLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:TIGR02769 161 IARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIV 230
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
2-228 |
5.68e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 86.76 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVT-KMKEYE--- 77
Cdd:PRK13646 3 IRFDNVSYTYQKGTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDKYirp 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 -RSRfIGRVFQDPsmgtcpsltvlENMALADNKGSSFLL---QRGVNRRRTQHYREELsLLHMGLE-DKLGVQVGSLSGG 152
Cdd:PRK13646 83 vRKR-IGMVFQFP-----------ESQLFEDTVEREIIFgpkNFKMNLDEVKNYAHRL-LMDLGFSrDVMSQSPFQMSGG 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 153 QRQALAML-IATMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK13646 150 QMRKIAIVsILAMNP-DIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
2-227 |
1.33e-19 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 86.54 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEyERsRF 81
Cdd:PRK09452 15 VELRGISKSFD----GKEVI-SNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPA-EN-RH 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQdpSMGTCPSLTVLENMALAdnkgssFLLQRGVNRRRTQHYREELSLLHmgLEDKLGVQVGSLSGGQRQALAMLI 161
Cdd:PRK09452 88 VNTVFQ--SYALFPHMTVFENVAFG------LRMQKTPAAEITPRVMEALRMVQ--LEEFAQRKPHQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 162 ATMSPINLLILDEHTAALDpHSSENVM--ELTQrVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK09452 158 AVVNKPKVLLLDESLSALD-YKLRKQMqnELKA-LQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
2-228 |
1.33e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.62 E-value: 1.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnPGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSL---PLGSGEIYVGDRQVTKMKEYER 78
Cdd:PRK13640 6 VEFKHVSFTY-PDSKKPAL--NDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVWDI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 79 SRFIGRVFQDPS---MGTcpslTVLENMALAdnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQ 155
Cdd:PRK13640 83 REKVGIVFQNPDnqfVGA----TVGDDVAFG-------LENRAVPRPEMIKIVRDV-LADVGMLDYIDSEPANLSGGQKQ 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 156 ALAML-IATMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAvAYGDRLLMMHRGHIM 228
Cdd:PRK13640 151 RVAIAgILAVEP-KIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLL 222
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
22-230 |
1.42e-19 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 85.28 E-value: 1.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVtkmkEYERS------RFIGRVFQDPSmGTCP 95
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI----DYSRKglmklrESVGMVFQDPD-NQLF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 96 SLTVLENMAL-ADNKGssflLQRGVNRRRTQHYREELSLLHmgLEDKlgvQVGSLSGGQRQALAML-IATMSPiNLLILD 173
Cdd:PRK13636 97 SASVYQDVSFgAVNLK----LPEDEVRKRVDNALKRTGIEH--LKDK---PTHCLSFGQKKRVAIAgVLVMEP-KVLVLD 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 174 EHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:PRK13636 167 EPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQ 223
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
1-227 |
2.43e-19 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 84.47 E-value: 2.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPgsvNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTIL---NLLcgSLPlGSGEIYV------------ 65
Cdd:COG4598 8 ALEVRDLHKSFGD---LEVL--KGVSLTARKGDVISIIGSSGSGKSTFLrciNLL--ETP-DSGEIRVggeeirlkpdrd 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 66 GDRQVTKMKEYERSRF-IGRVFQdpSMGTCPSLTVLENMALADnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGV 144
Cdd:COG4598 80 GELVPADRRQLQRIRTrLGMVFQ--SFNLWSHMTVLENVIEAP------VHVLGRPKAEAIERAEAL-LAKVGLADKRDA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 145 QVGSLSGGQRQ------ALAMliatmSPiNLLILDEHTAALDPhssenvmELTQRVAK------EKHVTMLMVTHNLKFA 212
Cdd:COG4598 151 YPAHLSGGQQQraaiarALAM-----EP-EVMLFDEPTSALDP-------ELVGEVLKvmrdlaEEGRTMLVVTHEMGFA 217
|
250
....*....|....*
gi 1852789824 213 VAYGDRLLMMHRGHI 227
Cdd:COG4598 218 RDVSSHVVFLHQGRI 232
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
1-230 |
2.49e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 84.75 E-value: 2.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHI-YKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE-YER 78
Cdd:PRK13633 4 MIKCKNVsYKYESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlWDI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 79 SRFIGRVFQDPSMGTCPSLtVLENMALadnkGSSFLlqrGVNRRRTQHyREELSLLHMGLEDKLGVQVGSLSGGQRQ--A 156
Cdd:PRK13633 84 RNKAGMVFQNPDNQIVATI-VEEDVAF----GPENL---GIPPEEIRE-RVDESLKKVGMYEYRRHAPHLLSGGQKQrvA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 157 LAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAyGDRLLMMHRGHIMLD 230
Cdd:PRK13633 155 IAGILA-MRP-ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVME 225
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
23-232 |
2.82e-19 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 84.27 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSmgTCPSLTVLEn 102
Cdd:PRK10253 24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLAQNAT--TPGDITVQE- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 maladnkgssfLLQRGvnrrRTQH------YREE------LSLLHMGLEDKLGVQVGSLSGGQRQA--LAMLIATMSPIn 168
Cdd:PRK10253 101 -----------LVARG----RYPHqplftrWRKEdeeavtKAMQATGITHLADQSVDTLSGGQRQRawIAMVLAQETAI- 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 169 lLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAA 232
Cdd:PRK10253 165 -MLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGA 227
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
2-227 |
4.51e-19 |
|
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: 86.61 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVvlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrf 81
Cdd:TIGR01257 929 VCVKNLVKIFEPSGRPAV---DRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQ-- 1003
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 igrvfqdpSMGTCPS-------LTVLENMAL-ADNKGSSFllqrgvnrrRTQHYREELSLLHMGLEDKLGVQVGSLSGGQ 153
Cdd:TIGR01257 1004 --------SLGMCPQhnilfhhLTVAEHILFyAQLKGRSW---------EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGM 1066
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 154 RQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:TIGR01257 1067 QRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGR--TIIMSTHHMDEADLLGDRIAIISQGRL 1138
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
17-193 |
4.69e-19 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 82.61 E-value: 4.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGrvfqdPSMGTCPS 96
Cdd:PRK13539 13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLG-----HRNAMKPA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENMAL-ADNKGSsfllqrgvnrrrtqhyrEELSLLH----MGLEDKLGVQVGSLSGGQ--RQALAMLIATMSPInl 169
Cdd:PRK13539 88 LTVAENLEFwAAFLGG-----------------EELDIAAaleaVGLAPLAHLPFGYLSAGQkrRVALARLLVSNRPI-- 148
|
170 180
....*....|....*....|....
gi 1852789824 170 LILDEHTAALDPHSSENVMELTQR 193
Cdd:PRK13539 149 WILDEPTAALDAAAVALFAELIRA 172
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
4-234 |
4.73e-19 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 83.00 E-value: 4.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 4 MEHIYKTFNPGSVN--EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTkmkEYERSRF 81
Cdd:PRK11614 1 MEKVMLSFDKVSAHygKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTAKI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 I----------GRVFQdpsmgtcpSLTVLENMALadnkGSSFllqrgVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSG 151
Cdd:PRK11614 78 MreavaivpegRRVFS--------RMTVEENLAM----GGFF-----AERDQFQERIKWVYELFPRLHERRIQRAGTMSG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 152 GQRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDA 231
Cdd:PRK11614 141 GEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLED 219
|
...
gi 1852789824 232 AGE 234
Cdd:PRK11614 220 TGD 222
|
|
| MsbA_lipidA |
TIGR02203 |
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ... |
2-227 |
6.46e-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: 85.54 E-value: 6.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnPGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:TIGR02203 331 VEFRNVTFRY-PGRDRPAL--DSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQ 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDpsmgtcpslTVLENMALADNKGSSFLlqRGVNRRRTQHYREELSL------LHMGLEDKLGVQVGSLSGGQRQ 155
Cdd:TIGR02203 408 VALVSQD---------VVLFNDTIANNIAYGRT--EQADRAEIERALAAAYAqdfvdkLPLGLDTPIGENGVLLSGGQRQ 476
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 156 ALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:TIGR02203 477 RLAIARALLKDAPILILDEATSALDNESERLVQAALERLMQGR--TTLVIAHRLS-TIEKADRIVVMDDGRI 545
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
23-227 |
6.49e-19 |
|
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: 82.66 E-value: 6.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtcpSLTVLEN 102
Cdd:cd03251 19 RDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQDVFLF---NDTVAEN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 MALADnkgssfllqRGVNRRRTQHyREELSLLH---MGLEDKLGVQVGS----LSGGQRQALAMLIATMSPINLLILDEH 175
Cdd:cd03251 96 IAYGR---------PGATREEVEE-AARAANAHefiMELPEGYDTVIGErgvkLSGGQRQRIAIARALLKDPPILILDEA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 176 TAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:cd03251 166 TSALDTESERLVQAALERLMKNR--TTFVIAHRLS-TIENADRIVVLEDGKI 214
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
20-228 |
1.22e-18 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 82.53 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQdpSMGTCPSLTV 99
Cdd:PRK10575 25 TLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQ--QLPAAEGMTV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMALADNKGSSFLLQRGVNRRrtQHYREELSLLhmGLEDKLGVQVGSLSGGQRQA--LAMLIATMSpiNLLILDEHTA 177
Cdd:PRK10575 103 RELVAIGRYPWHGALGRFGAADR--EKVEEAISLV--GLKPLAHRLVDSLSGGERQRawIAMLVAQDS--RCLLLDEPTS 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 178 ALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK10575 177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
1-219 |
1.23e-18 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 81.75 E-value: 1.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGSvNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERS- 79
Cdd:PRK10584 6 IVEVHHLKKSVGQGE-HELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAk 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 80 ---RFIGRVFQdpSMGTCPSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQA 156
Cdd:PRK10584 85 lraKHVGFVFQ--SFMLIPTLNALENVELP-------ALLRGESSRQSRNGAKAL-LEQLGLGKRLDHLPAQLSGGEQQR 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 157 LAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRL 219
Cdd:PRK10584 155 VALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRL 217
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
23-242 |
1.49e-18 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 81.98 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDP------------S 90
Cdd:PRK11231 19 NDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLALLPQHHltpegitvrelvA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 91 MGTCPSLTVLENMALADNKgssfLLQRGVNRRRTQHyreelsllhmgLEDKLgvqVGSLSGGQRQA--LAMLIATMSPIn 168
Cdd:PRK11231 99 YGRSPWLSLWGRLSAEDNA----RVNQAMEQTRINH-----------LADRR---LTDLSGGQRQRafLAMVLAQDTPV- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 169 lLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED-------KKVLDV 241
Cdd:PRK11231 160 -VLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEvmtpgllRTVFDV 237
|
.
gi 1852789824 242 R 242
Cdd:PRK11231 238 E 238
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
2-231 |
1.52e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 82.83 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEI---YVGDRQVTKMKEYE- 77
Cdd:PRK13651 3 IKVKNIVKIFNKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewiFKDEKNKKKTKEKEk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 --------RSRF------------IGRVFQDPSMGTCPSlTVLENMALAdnkGSSFLLQRGVNRRRTQHYREELSLLhmg 137
Cdd:PRK13651 83 vleklviqKTRFkkikkikeirrrVGVVFQFAEYQLFEQ-TIEKDIIFG---PVSMGVSKEEAKKRAAKYIELVGLD--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 138 lEDKLGVQVGSLSGGQ--RQALAMLIAtMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAY 215
Cdd:PRK13651 156 -ESYLQRSPFELSGGQkrRVALAGILA-MEP-DFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEW 231
|
250
....*....|....*.
gi 1852789824 216 GDRLLMMHRGHIMLDA 231
Cdd:PRK13651 232 TKRTIFFKDGKIIKDG 247
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
20-227 |
1.76e-18 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 81.60 E-value: 1.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFqDFNLQIAEGSFVAVVGSNGSGKTT---ILNLLcgSLPlGSGEIYVGDRQV-----TKMKE-YERSRFIGRVFQDPS 90
Cdd:PRK11124 17 ALF-DITLDCPQGETLVLLGPSGAGKSSllrVLNLL--EMP-RSGTLNIAGNHFdfsktPSDKAiRELRRNVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 91 MgtCPSLTVLENMALADNKgssfllQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLL 170
Cdd:PRK11124 93 L--WPHLTVQQNLIEAPCR------VLGLSKDQALARAEKL-LERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 171 ILDEHTAALDPHSSENVMELTQRVAkEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK11124 164 LFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHI 219
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
24-225 |
2.25e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 83.35 E-value: 2.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrfIGRVFQdpSMGTCPSLTVLENM 103
Cdd:PRK11607 37 DVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP--INMMFQ--SYALFPHMTVEQNI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 104 A--LADNKgssflLQRGVNRRRTQhyrEELSLLHMglEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDP 181
Cdd:PRK11607 113 AfgLKQDK-----LPKAEIASRVN---EMLGLVHM--QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1852789824 182 HSSE----NVMELTQRVAkekhVTMLMVTHNLKFAVAYGDRLLMMHRG 225
Cdd:PRK11607 183 KLRDrmqlEVVDILERVG----VTCVMVTHDQEEAMTMAGRIAIMNRG 226
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
33-227 |
2.32e-18 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 82.16 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 33 SFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSmGTCPSLTVLENMALADnkgss 112
Cdd:PRK13652 31 SRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPD-DQIFSPTVEQDIAFGP----- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 113 flLQRGVNRRRTQHYREElsLLHM-GLEDKLGVQVGSLSGGQ--RQALAMLIAtMSPiNLLILDEHTAALDPHSSENVME 189
Cdd:PRK13652 105 --INLGLDEETVAHRVSS--ALHMlGLEELRDRVPHHLSGGEkkRVAIAGVIA-MEP-QVLVLDEPTAGLDPQGVKELID 178
|
170 180 190
....*....|....*....|....*....|....*...
gi 1852789824 190 LTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK13652 179 FLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRI 216
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
12-228 |
2.73e-18 |
|
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: 83.58 E-value: 2.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 12 NPGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKT----TILNLLCGSLPLGSGEIYVGDRQVTKMKEYE----RSRFIG 83
Cdd:COG4172 18 QGGGTVEAV--KGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSERElrriRGNRIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 84 RVFQDPsMgTC--PSLTVLENMAladnkgSSFLLQRGVNRRRTQhyREELSLLHM-GL---EDKLGV---QvgsLSGGQR 154
Cdd:COG4172 96 MIFQEP-M-TSlnPLHTIGKQIA------EVLRLHRGLSGAAAR--ARALELLERvGIpdpERRLDAyphQ---LSGGQR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 155 Q--ALAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNL----KFAvaygDRLLMMHRGHIM 228
Cdd:COG4172 163 QrvMIAMALAN-EP-DLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLgvvrRFA----DRVAVMRQGEIV 236
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
1-234 |
4.59e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 80.30 E-value: 4.59e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPGsvNEVVLFQDFNLQIAEGSFVavVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYE--- 77
Cdd:PRK10908 1 MIRFEHVSKAYLGG--RQALQGVTFHMRPGEMAFL--TGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 78 RSRFIGRVFQDPSMgtCPSLTVLENMALAdnkgssfLLQRGVN----RRRTQhyreeLSLLHMGLEDKLGVQVGSLSGGQ 153
Cdd:PRK10908 77 LRRQIGMIFQDHHL--LMDRTVYDNVAIP-------LIIAGASgddiRRRVS-----AALDKVGLLDKAKNFPIQLSGGE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 154 RQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQ---RVAkekhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:PRK10908 143 QQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEefnRVG----VTVLMATHDIGLISRRSYRMLTLSDGHLHGG 218
|
....
gi 1852789824 231 AAGE 234
Cdd:PRK10908 219 VGGE 222
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
24-227 |
5.78e-18 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 80.47 E-value: 5.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTIL---NLLCGSLPlG---SGEIYVGDRQV--TKMKEYE-RSRfIGRVFQDPsmgtC 94
Cdd:COG1117 29 DINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLIP-GarvEGEILLDGEDIydPDVDVVElRRR-VGMVFQKP----N 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 P-SLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELSLLHMGL----EDKLGVQVGSLSGGQRQAL--AMLIAtMSPi 167
Cdd:COG1117 103 PfPKSIYDNVAYG-------LRLHGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLciARALA-VEP- 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 168 NLLILDEHTAALDPHSSENVMELTQRVAKEkhVTMLMVTHNLKFA--VAygDRLLMMHRGHI 227
Cdd:COG1117 174 EVLLMDEPTSALDPISTAKIEELILELKKD--YTIVIVTHNMQQAarVS--DYTAFFYLGEL 231
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
1-230 |
9.01e-18 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 80.54 E-value: 9.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnpGSVneVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTkmkeYERSR 80
Cdd:COG4152 1 MLELKGLTKRF--GDK--TAV-DDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIG-----RvfqdpsmGTCPSLTVLENMA-LADNKGssflLQRGVNRRRTQHYREELsllhmGLEDKLGVQVGSLSGGQR 154
Cdd:COG4152 72 RIGylpeeR-------GLYPKMKVGEQLVyLARLKG----LSKAEAKRRADEWLERL-----GLGDRANKKVEELSKGNQ 135
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 155 QALAmLIATM--SPiNLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:COG4152 136 QKVQ-LIAALlhDP-ELLILDEPFSGLDPVNVELLKDVIREL-AAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLS 210
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
20-227 |
9.15e-18 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 79.67 E-value: 9.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFqDFNLQIAEGSFVAVVGSNGSGKTT---ILNLLcgSLPlGSGEIYVGDRQV---TKMKEYERS---RFIGRVFQDPS 90
Cdd:COG4161 17 ALF-DINLECPSGETLVLLGPSGAGKSSllrVLNLL--ETP-DSGQLNIAGHQFdfsQKPSEKAIRllrQKVGMVFQQYN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 91 MgtCPSLTVLENMALADNKgssfLLqrGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLL 170
Cdd:COG4161 93 L--WPHLTVMENLIEAPCK----VL--GLSKEQAREKAMKL-LARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQVL 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 171 ILDEHTAALDPHSSENVMELTQRVAkEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:COG4161 164 LFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRI 219
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
17-190 |
1.10e-17 |
|
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: 78.55 E-value: 1.10e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE--YERSRFIGRvfqdpSMGTC 94
Cdd:TIGR01189 11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDepHENILYLGH-----LPGLK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTVLENMaladnkgsSFLLQRGVNRRRTQHYreelSLLHMGLEDKLGVQVGSLSGGQ--RQALAMLIATMSPinLLIL 172
Cdd:TIGR01189 86 PELSALENL--------HFWAAIHGGAQRTIED----ALAAVGLTGFEDLPAAQLSAGQqrRLALARLWLSRRP--LWIL 151
|
170
....*....|....*...
gi 1852789824 173 DEHTAALDPHSSENVMEL 190
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGL 169
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
2-248 |
1.53e-17 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 80.51 E-value: 1.53e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGSVnevvlFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMkeYERSRF 81
Cdd:PRK10851 3 IEIANIKKSFGRTQV-----LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRL--HARDRK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSMGTcpSLTVLENMALadnkGSSFLLQRgvnRRRTQHY--REELSLLHM----GLEDKLGVQvgsLSGGQRQ 155
Cdd:PRK10851 76 VGFVFQHYALFR--HMTVFDNIAF----GLTVLPRR---ERPNAAAikAKVTQLLEMvqlaHLADRYPAQ---LSGGQKQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 156 --ALAMLIATMSPInlLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHImlDAAG 233
Cdd:PRK10851 144 rvALARALAVEPQI--LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI--EQAG 219
|
250
....*....|....*
gi 1852789824 234 EDKKVldVRDLTNRF 248
Cdd:PRK10851 220 TPDQV--WREPATRF 232
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
20-226 |
2.92e-17 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 79.87 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRfIGRVFQDPSMGtcPSLTV 99
Cdd:PRK13536 55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARAR-IGVVPQFDNLD--LEFTV 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMALAdnkGSSFllqrGVNRRRTqhyrEEL--SLLHMG-LEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHT 176
Cdd:PRK13536 132 RENLLVF---GRYF----GMSTREI----EAVipSLLEFArLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPT 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 177 AALDPHSSENVME-LTQRVAKEKhvTMLMVTHNLKFAVAYGDRLLMMHRGH 226
Cdd:PRK13536 201 TGLDPHARHLIWErLRSLLARGK--TILLTTHFMEEAERLCDRLCVLEAGR 249
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
21-225 |
3.05e-17 |
|
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: 77.21 E-value: 3.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG--SGEIYVGDRQVTKMKEYERSRFigrVFQDPSmgTCPSLT 98
Cdd:cd03213 24 LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKIIGY---VPQDDI--LHPTLT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 99 VLENMALAdnkgssfllqrgvnrrrtqhyreelsllhmgledklgVQVGSLSGGQRQ----ALAMLiatMSPiNLLILDE 174
Cdd:cd03213 99 VRETLMFA-------------------------------------AKLRGLSGGERKrvsiALELV---SNP-SLLFLDE 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 175 HTAALDPHSSENVMELTQRVAKEkHVTMLMVTHNLK---FAVAygDRLLMMHRG 225
Cdd:cd03213 138 PTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSseiFELF--DKLLLLSQG 188
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
13-227 |
3.29e-17 |
|
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: 77.70 E-value: 3.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 13 PGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG---SGEIYVGDRQvtkMKEYERSRFIGRVFQDP 89
Cdd:cd03234 14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQP---RKPDQFQKCVAYVRQDD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SmgTCPSLTVLENMALAdnkgSSFLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINL 169
Cdd:cd03234 91 I--LLPGLTVRETLTYT----AILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKV 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 170 LILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTH-------NLkFavaygDRLLMMHRGHI 227
Cdd:cd03234 165 LILDEPTSGLDSFTALNLVSTLSQLARRNR-IVILTIHqprsdlfRL-F-----DRILLLSSGEI 222
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
22-228 |
3.82e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 80.25 E-value: 3.82e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtcpSLTVLE 101
Cdd:PRK11160 356 LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISVVSQRVHLF---SATLRD 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 102 NMALADNKGSSfllqrgvnrrrtqhyrEELS--LLHMGLEDKL-------------GVQvgsLSGGQRQALAMLIATMSP 166
Cdd:PRK11160 433 NLLLAAPNASD----------------EALIevLQQVGLEKLLeddkglnawlgegGRQ---LSGGEQRRLGIARALLHD 493
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 167 INLLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHIM 228
Cdd:PRK11160 494 APLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITHRLT-GLEQFDRICVMDNGQII 552
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
3-248 |
3.91e-17 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 80.22 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 3 RMEHIYKTFnPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGS--GEIYVgDRQVTKMKEYERSR 80
Cdd:NF040905 3 EMRGITKTF-PG----VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGSyeGEILF-DGEVCRFKDIRDSE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPSMGTCPSLTVLENMALADNKGSsfllqRGV-NRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQ---- 155
Cdd:NF040905 77 ALGIVIIHQELALIPYLSIAENIFLGNERAK-----RGViDWNETNRRAREL-LAKVGLDESPDTLVTDIGVGKQQlvei 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 156 --ALAmliatmSPINLLILDEHTAALDPHSSENVMELTqRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM--LDA 231
Cdd:NF040905 151 akALS------KDVKLLILDEPTAALNEEDSAALLDLL-LELKAQGITSIIISHKLNEIRRVADSITVLRDGRTIetLDC 223
|
250 260
....*....|....*....|...
gi 1852789824 232 AG----EDKKVLDV--RDLTNRF 248
Cdd:NF040905 224 RAdevtEDRIIRGMvgRDLEDRY 246
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
27-245 |
5.49e-17 |
|
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: 79.85 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 27 LQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYV--GDRQV--TKMKEYERSR---FIGRVFQDPSMgtCPSLTV 99
Cdd:TIGR03269 305 LEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvGDEWVdmTKPGPDGRGRakrYIGILHQEYDL--YPHRTV 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMAladnKGSSFLLQRGVNRRRTQHyreelSLLHMGLEDKLGVQV-----GSLSGGQRQALAMLIATMSPINLLILDE 174
Cdd:TIGR03269 383 LDNLT----EAIGLELPDELARMKAVI-----TLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIVILDE 453
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 175 HTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGEDKKVldVRDLT 245
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIV--KIGDPEEI--VEELT 520
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-212 |
6.18e-17 |
|
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: 76.31 E-value: 6.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE--YERSRFIGRVFQDPSmGTC 94
Cdd:TIGR01166 3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKglLERRQRVGLVFQDPD-DQL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTVLENMALAD-NKGssfLLQRGVNRRrtqhYREELSLLHM-GLEDKLgvqVGSLSGGQRQALAMLIA-TMSPiNLLI 171
Cdd:TIGR01166 82 FAADVDQDVAFGPlNLG---LSEAEVERR----VREALTAVGAsGLRERP---THCLSGGEKKRVAIAGAvAMRP-DVLL 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1852789824 172 LDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFA 212
Cdd:TIGR01166 151 LDEPTAGLDPAGREQMLAILRRL-RAEGMTVVISTHDVDLA 190
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
24-227 |
9.73e-17 |
|
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: 76.38 E-value: 9.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKM-KEYERSRfIGRVFQDPSM--GTcpsltVL 100
Cdd:cd03244 22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIgLHDLRSR-ISIIPQDPVLfsGT-----IR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMAlADNKGSSFLLQRGVNRrrtQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:cd03244 96 SNLD-PFGEYSDEELWQALER---VGLKEFVESLPGGLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1852789824 181 PHSsenvMELTQRVAKE--KHVTMLMVTHNLKFAVAYgDRLLMMHRGHI 227
Cdd:cd03244 172 PET----DALIQKTIREafKDCTVLTIAHRLDTIIDS-DRILVLDKGRV 215
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
16-225 |
1.31e-16 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 76.95 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 16 VNEVvlfqdfNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF-IGRVFQDPSMgtC 94
Cdd:PRK11300 21 VNNV------NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMgVVRTFQHVRL--F 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTVLENMALADNKGSSFLLQRGVNR----RRTQhyREELS-----LLHMGLEDKLGVQVGSLSGGQRQALAMLIATMS 165
Cdd:PRK11300 93 REMTVIENLLVAQHQQLKTGLFSGLLKtpafRRAE--SEALDraatwLERVGLLEHANRQAGNLAYGQQRRLEIARCMVT 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 166 PINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRG 225
Cdd:PRK11300 171 QPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQG 230
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
2-231 |
1.47e-16 |
|
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: 75.72 E-value: 1.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFnpGSVNEVvlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTkmKEYERSRF 81
Cdd:cd03268 1 LKTNDLTKTY--GKKRVL---DDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ--KNIEALRR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPsmGTCPSLTVLENMALadnkgssFLLQRGVNRRRTQHYREELsllhmGLEDKLGVQVGSLSGGQRQALAMLI 161
Cdd:cd03268 74 IGALIEAP--GFYPNLTARENLRL-------LARLLGIRKKRIDEVLDVV-----GLKDSAKKKVKGFSLGMKQRLGIAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 162 ATMSPINLLILDEHTAALDPhssENVMELTQ--RVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDA 231
Cdd:cd03268 140 ALLGNPDLLILDEPTNGLDP---DGIKELREliLSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
1-257 |
1.48e-16 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 78.67 E-value: 1.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNPgsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSR 80
Cdd:PRK09700 5 YISMAGIGKSFGP-----VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 F-IGRVFQDPSMgtCPSLTVLENMALADNKGSSFLlqrGVN--RRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQAL 157
Cdd:PRK09700 80 LgIGIIYQELSV--IDELTVLENLYIGRHLTKKVC---GVNiiDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 158 AMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGH-----IMLDAA 232
Cdd:PRK09700 155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSsvcsgMVSDVS 233
|
250 260
....*....|....*....|....*.
gi 1852789824 233 GEDKKVLDV-RDLTNRFDEISVEDGN 257
Cdd:PRK09700 234 NDDIVRLMVgRELQNRFNAMKENVSN 259
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
24-228 |
1.56e-16 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 77.61 E-value: 1.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQV--TKMKEY---ERSRfIGRVFQDPSMgtCPSLT 98
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLfdAEKGIClppEKRR-IGYVFQDARL--FPHYK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 99 VLENmaladnkgssflLQRGVNRRRTQHYREELSLLhmGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAA 178
Cdd:PRK11144 93 VRGN------------LRYGMAKSMVAQFDKIVALL--GIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLAS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 179 LD-PHSSEnVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK11144 159 LDlPRKRE-LLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVK 208
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
23-227 |
2.42e-16 |
|
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: 75.59 E-value: 2.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtcpSLTVLEN 102
Cdd:cd03248 31 QDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLF---ARSLQDN 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 MALADNKGSsflLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPH 182
Cdd:cd03248 108 IAYGLQSCS---FECVKEAAQKAHAHSFISELASGYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAE 184
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1852789824 183 SSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:cd03248 185 SEQQVQQALYDWPERR--TVLVIAHRLS-TVERADQILVLDGGRI 226
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
4-227 |
2.44e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.80 E-value: 2.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 4 MEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVgDRQVTkmkeyersrfIG 83
Cdd:COG0488 1 LENLSKSFG-----GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGLR----------IG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 84 RVFQDPSMGtcPSLTVLENMALADNKGSSFLLQRGVNRRRTQHYREELS------------------------LLHMGL- 138
Cdd:COG0488 65 YLPQEPPLD--DDLTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLErlaelqeefealggweaearaeeiLSGLGFp 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 139 EDKLGVQVGSLSGGQRQ--ALAMLIatMSPINLLILDEHTAALDPHSsenVMELTQRVAKEKHvTMLMVTHNLKF--AVA 214
Cdd:COG0488 143 EEDLDRPVSELSGGWRRrvALARAL--LSEPDLLLLDEPTNHLDLES---IEWLEEFLKNYPG-TVLVVSHDRYFldRVA 216
|
250
....*....|...
gi 1852789824 215 ygDRLLMMHRGHI 227
Cdd:COG0488 217 --TRILELDRGKL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
4-232 |
4.42e-16 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 75.49 E-value: 4.42e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 4 MEHIYKT--FNPGSVNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF 81
Cdd:PRK10419 9 LSHHYAHggLSGKHQHQTVL-NNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 ---IGRVFQDPSMGTCPSLTVLENMAladnKGSSFLLqrGVNRRRTQHYREELsLLHMGLEDKLGVQV-GSLSGGQRQ-- 155
Cdd:PRK10419 88 rrdIQMVFQDSISAVNPRKTVREIIR----EPLRHLL--SLDKAERLARASEM-LRAVDLDDSVLDKRpPQLSGGQLQrv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 156 ----ALAMliatmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDA 231
Cdd:PRK10419 161 clarALAV-----EP-KLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQ 234
|
.
gi 1852789824 232 A 232
Cdd:PRK10419 235 P 235
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
23-235 |
9.40e-16 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 74.16 E-value: 9.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERS-RFIGRVFQDPSMGTcpSLTVLE 101
Cdd:PRK10895 20 EDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARArRGIGYLPQEASIFR--RLSVYD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 102 N-MALADNKGSSFLLQRgvnRRRTQHYREELSLLHmgLEDKLGvqvGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:PRK10895 98 NlMAVLQIRDDLSAEQR---EDRANELMEEFHIEH--LRDSMG---QSLSGGERRRVEIARALAANPKFILLDEPFAGVD 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 181 PHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:PRK10895 170 PISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTE 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
18-207 |
1.10e-15 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 73.30 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 18 EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE-YERS-RFIGRVfqdpsMGTCP 95
Cdd:PRK13538 13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDeYHQDlLYLGHQ-----PGIKT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 96 SLTVLENMAladnkgssFL--LQRGVNRRRTQHYreelsLLHMGLEDKLGVQVGSLSGGQ--RQALAMLIATMSPinLLI 171
Cdd:PRK13538 88 ELTALENLR--------FYqrLHGPGDDEALWEA-----LAQVGLAGFEDVPVRQLSAGQqrRVALARLWLTRAP--LWI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1852789824 172 LDEHTAALDPHSsenVMELTQRVakEKHV----TMLMVTH 207
Cdd:PRK13538 153 LDEPFTAIDKQG---VARLEALL--AQHAeqggMVILTTH 187
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
24-227 |
1.41e-15 |
|
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: 75.63 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGD---RQVTKmkEYERsRFIGRVFQDpsmgtcpslTVL 100
Cdd:COG5265 376 GVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQ--ASLR-AAIGIVPQD---------TVL 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALADNkgssflLQRGvnrrRTQHYREE------LSLLH---MGLEDKLGVQVGS----LSGGQRQALAmlIATM--- 164
Cdd:COG5265 444 FNDTIAYN------IAYG----RPDASEEEveaaarAAQIHdfiESLPDGYDTRVGErglkLSGGEKQRVA--IARTllk 511
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 165 -SPInlLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHI 227
Cdd:COG5265 512 nPPI--LIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLS-TIVDADEILVLEAGRI 570
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
23-227 |
2.62e-15 |
|
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: 74.72 E-value: 2.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTT----ILNLLcGSlplgSGEIYVGDRQVTKMKEYE----RSRF-IgrVFQDP--SM 91
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTlglaLLRLI-PS----EGEIRFDGQDLDGLSRRAlrplRRRMqV--VFQDPfgSL 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 GtcPSLTVLENMA--LAdnkgssfLLQRGVNRR-RTQHYREELsllhmgledklgVQVG-----------SLSGGQRQAL 157
Cdd:COG4172 376 S--PRMTVGQIIAegLR-------VHGPGLSAAeRRARVAEAL------------EEVGldpaarhryphEFSGGQRQRI 434
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 158 AmlIA---TMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:COG4172 435 A--IAralILEP-KLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKV 504
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-220 |
2.71e-15 |
|
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: 72.83 E-value: 2.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSF-----VAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQdpsmgtcpslt 98
Cdd:cd03237 12 EFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSYKPQYIKADYEGTVRD----------- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 99 vlenmaladnkgssfLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAmLIATMS-PINLLILDEHTA 177
Cdd:cd03237 81 ---------------LLSSITKDFYTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVA-IAACLSkDADIYLLDEPSA 144
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1852789824 178 ALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLL 220
Cdd:cd03237 145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLI 187
|
|
| ArpD |
COG4618 |
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ... |
13-229 |
2.89e-15 |
|
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: 74.78 E-value: 2.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 13 PGSvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSM- 91
Cdd:COG4618 341 PGS--KRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELf 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 -GTcpsltVLENMA---------------LAdnkgssfllqrGVnrrrtqHyreELSL-LHMGLEDKLGVQVGSLSGGQR 154
Cdd:COG4618 419 dGT-----IAENIArfgdadpekvvaaakLA-----------GV------H---EMILrLPDGYDTRIGEGGARLSGGQR 473
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 155 Q--ALAmliATM--SPInLLILDEHTAALDPHSSENVMELTQRvAKEKHVTMLMVTHNLKfAVAYGDRLLMMHRGHIML 229
Cdd:COG4618 474 QriGLA---RALygDPR-LVVLDEPNSNLDDEGEAALAAAIRA-LKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQA 546
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
16-228 |
3.05e-15 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 73.16 E-value: 3.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 16 VNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDR------QVTKMKEYERSRFIGRVFQDP 89
Cdd:PRK14246 20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVFQQP 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SmgTCPSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELSLLHMGL----EDKLGVQVGSLSGGQRQALAMLIATMS 165
Cdd:PRK14246 100 N--PFPHLSIYDNIAYP-------LKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALAL 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 166 PINLLILDEHTAALDPHSSENVMELTQRVAKEkhVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELV 231
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
6-235 |
3.98e-15 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 74.32 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 6 HIYKTFnpgSVNEVVLFQDFNLQiaEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF-IGR 84
Cdd:PRK15439 16 SISKQY---SGVEVLKGIDFTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLgIYL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 85 VFQDPSMgtCPSLTVLENMAladnkgssFLLQRgvnRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATM 164
Cdd:PRK15439 91 VPQEPLL--FPNLSVKENIL--------FGLPK---RQASMQKMKQL-LAALGCQLDLDSSAGSLEVADRQIVEILRGLM 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 165 SPINLLILDEHTAALDPHSSENvmeLTQRVAK--EKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:PRK15439 157 RDSRILILDEPTASLTPAETER---LFSRIREllAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTAD 226
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
25-227 |
7.17e-15 |
|
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: 73.68 E-value: 7.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 25 FNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTK--MKEYeRSRFiGRVFQDPsmgtcpsltvlen 102
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTAdnREAY-RQLF-SAVFSDF------------- 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 maladnkgssFL------LQRGVNRRRTQHYreelsLLHMGLEDKLGVQVG-----SLSGGQRQALAMLIATMS--PInl 169
Cdd:COG4615 416 ----------HLfdrllgLDGEADPARAREL-----LERLELDHKVSVEDGrfsttDLSQGQRKRLALLVALLEdrPI-- 478
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 170 LILDEHTAALDPH-----SSENVMELtqrvaKEKHVTMLMVTHNLK-FAVAygDRLLMMHRGHI 227
Cdd:COG4615 479 LVFDEWAADQDPEfrrvfYTELLPEL-----KARGKTVIAISHDDRyFDLA--DRVLKMDYGKL 535
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
28-235 |
9.80e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 72.47 E-value: 9.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 28 QIAEGSFVAVVGSNGSGKT----TILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGR----VFQDPSMGTCPSLTV 99
Cdd:PRK11022 29 SVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKERRNLVGAevamIFQDPMTSLNPCYTV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 -LENM-ALADNKGSSfllqrgvnrRRTQHYREELSLLHMGLED---KLGVQVGSLSGG--QRQALAMLIATmSPiNLLIL 172
Cdd:PRK11022 109 gFQIMeAIKVHQGGN---------KKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGmsQRVMIAMAIAC-RP-KLLIA 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 173 DEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:PRK11022 178 DEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
31-207 |
1.05e-14 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 73.16 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 31 EGSFVAVVGSNGSGKTTILNLLCGSLP---LGSGEIYVGDRQVTKMKEYERSRFigrVFQDPSMgtCPSLTVLENMALAd 107
Cdd:TIGR00955 50 PGELLAVMGSSGAGKTTLMNALAFRSPkgvKGSGSVLLNGMPIDAKEMRAISAY---VQQDDLF--IPTLTVREHLMFQ- 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 108 nkgSSFLLQRGVNRRRTQHYREELsLLHMGLED----KLGV--QVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDP 181
Cdd:TIGR00955 124 ---AHLRMPRRVTKKEKRERVDEV-LQALGLRKcantRIGVpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDS 199
|
170 180
....*....|....*....|....*.
gi 1852789824 182 HSSENVMELTQRVAkEKHVTMLMVTH 207
Cdd:TIGR00955 200 FMAYSVVQVLKGLA-QKGKTIICTIH 224
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
26-227 |
1.21e-14 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 71.54 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYE--------------RSRfIGRVFQDPSM 91
Cdd:PRK10619 25 SLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDgqlkvadknqlrllRTR-LTMVFQHFNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 GTcpSLTVLENMALADNKgsSFLLQRGVNRRRTQHYreelsLLHMGLEDKLGVQVGS-LSGGQRQALAMLIATMSPINLL 170
Cdd:PRK10619 104 WS--HMTVLENVMEAPIQ--VLGLSKQEARERAVKY-----LAKVGIDERAQGKYPVhLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 171 ILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKI 230
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
25-248 |
1.50e-14 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 71.12 E-value: 1.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 25 FNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPlGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSmgTCPSLTVLENMA 104
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAELARHRAYLSQQQT--PPFAMPVFQYLT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 105 LAdnkgssflLQRGVNRRRTQHYREELSLLhMGLEDKLGVQVGSLSGG--QRQALAMLIATMSP-IN----LLILDEHTA 177
Cdd:PRK03695 92 LH--------QPDKTRTEAVASALNEVAEA-LGLDDKLGRSVNQLSGGewQRVRLAAVVLQVWPdINpagqLLLLDEPMN 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 178 ALDPhSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGhiMLDAAGEDKKVLDVRDLTNRF 248
Cdd:PRK03695 163 SLDV-AQQAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQG--KLLASGRRDEVLTPENLAQVF 230
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
17-248 |
1.51e-14 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 71.03 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG-----SGEIYVGDRQV--TKMKEYERSRFIGRVFQDP 89
Cdd:PRK14267 17 NHVI--KGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIysPDVDPIEVRREVGMVFQYP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SmgTCPSLTVLENMALAdnkgssFLLQRGVNRRRTQHYREELSLLHMGL----EDKLGVQVGSLSGGQRQALAMLIATMS 165
Cdd:PRK14267 95 N--PFPHLTIYDNVAIG------VKLNGLVKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAM 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 166 PINLLILDEHTAALDPHSSENVMELTQRVAKEkhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGEDKKVLD--VRD 243
Cdd:PRK14267 167 KPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLI--EVGPTRKVFEnpEHE 242
|
....*
gi 1852789824 244 LTNRF 248
Cdd:PRK14267 243 LTEKY 247
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
1-244 |
1.64e-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: 72.55 E-value: 1.64e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnpGSVNEVvlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGS--GEIYVGDR--QVTKMKEY 76
Cdd:TIGR02633 1 LLEMKGIVKTF--GGVKAL---DGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSplKASNIRDT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 77 ERSrfiGRVFQDPSMGTCPSLTVLENMALADN---KGSsfLLQRGVNRRRTQHYREELSLlhmgLEDKLGVQVGSLSGGQ 153
Cdd:TIGR02633 76 ERA---GIVIIHQELTLVPELSVAENIFLGNEitlPGG--RMAYNAMYLRAKNLLRELQL----DADNVTRPVGDYGGGQ 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 154 RQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTqRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRG-HImldaA 232
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDII-RDLKAHGVACVYISHKLNEVKAVCDTICVIRDGqHV----A 221
|
250
....*....|..
gi 1852789824 233 GEDKKVLDVRDL 244
Cdd:TIGR02633 222 TKDMSTMSEDDI 233
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
17-227 |
2.33e-14 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 71.41 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSrfIGRVFQD----PSMg 92
Cdd:PRK11650 17 TQVI--KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD--IAMVFQNyalyPHM- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 93 tcpslTVLENMALAdnkgssfLLQRGVNR----RRTQHYREELSLLHMgLEDKlgvqVGSLSGGQRQALAMLIATMSPIN 168
Cdd:PRK11650 92 -----SVRENMAYG-------LKIRGMPKaeieERVAEAARILELEPL-LDRK----PRELSGGQRQRVAMGRAIVREPA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 169 LLILDEHTAALDP----HSSENVMELTQRVAkekhVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK11650 155 VFLFDEPLSNLDAklrvQMRLEIQRLHRRLK----TTSLYVTHDQVEAMTLADRVVVMNGGVA 213
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
23-228 |
2.40e-14 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 71.99 E-value: 2.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYE----RSRFIGRVFQdpSMGTCPSLT 98
Cdd:PRK10070 45 KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAElrevRRKKIAMVFQ--SFALMPHMT 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 99 VLENMALAdnkgssfLLQRGVNRRRTQHYREElSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAA 178
Cdd:PRK10070 123 VLDNTAFG-------MELAGINAEERREKALD-ALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1852789824 179 LDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK10070 195 LDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
25-228 |
2.52e-14 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 71.48 E-value: 2.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 25 FNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLP----LGSGEIYVGDRQVTKMKEYERSRFIGR----VFQDPSmgTC-- 94
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERRKIIGReiamIFQEPS--SCld 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTVLENM--ALADNKGSSFLLQRGVNRRRtqhyrEELSLLHmgledKLGVQ-----VGS----LSGG--QRQALAMLI 161
Cdd:COG4170 104 PSAKIGDQLieAIPSWTFKGKWWQRFKWRKK-----RAIELLH-----RVGIKdhkdiMNSypheLTEGecQKVMIAMAI 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 162 ATmSPInLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:COG4170 174 AN-QPR-LLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTV 238
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
18-225 |
3.32e-14 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 70.60 E-value: 3.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 18 EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRfIGRVFQDPSMGtcPSL 97
Cdd:PRK13537 19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQR-VGVVPQFDNLD--PDF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 98 TVLENMALAdnkGSSFLLQRGVNRRRTQhyreelSLLHMG-LEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHT 176
Cdd:PRK13537 96 TVRENLLVF---GRYFGLSAAAARALVP------PLLEFAkLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPT 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1852789824 177 AALDPHSSENVME-LTQRVAKEKhvTMLMVTHNLKFAVAYGDRLLMMHRG 225
Cdd:PRK13537 167 TGLDPQARHLMWErLRSLLARGK--TILLTTHFMEEAERLCDRLCVIEEG 214
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
15-228 |
3.99e-14 |
|
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: 68.71 E-value: 3.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCG--SLPLGSGEIYVGDRQVTKMKEYERSRF-IGRVFQDPSm 91
Cdd:cd03217 9 SVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGhpKYEVTEGEILFKGEDITDLPPEERARLgIFLAFQYPP- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 gTCPSLTVLEnmaladnkgssFLlqRGVNrrrtqhyreelsllhmgledklgvqVGsLSGGQRQALAML-IATMSPiNLL 170
Cdd:cd03217 88 -EIPGVKNAD-----------FL--RYVN-------------------------EG-FSGGEKKRNEILqLLLLEP-DLA 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 171 ILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHN---LKFAVAygDRLLMMHRGHIM 228
Cdd:cd03217 127 ILDEPDSGLDIDALRLVAEVINKL-REEGKSVLIITHYqrlLDYIKP--DRVHVLYDGRIV 184
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
10-235 |
4.10e-14 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 71.69 E-value: 4.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 10 TFNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVgdrqvtkmkeyersrFIGRVFQDP 89
Cdd:PLN03130 621 YFSWDSKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------------IRGTVAYVP 685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SMGTCPSLTVLENMALadnkGSSFLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINL 169
Cdd:PLN03130 686 QVSWIFNATVRDNILF----GSPFDPERYERAIDVTALQHDLDLLPGGDLTEIGERGVNISGGQKQRVSMARAVYSNSDV 761
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 170 LILDEHTAALDPHSSENVMEltqRVAKE--KHVTMLMVTHNLKFaVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:PLN03130 762 YIFDDPLSALDAHVGRQVFD---KCIKDelRGKTRVLVTNQLHF-LSQVDRIILVHEGMIKEEGTYEE 825
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
20-235 |
6.01e-14 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 69.47 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG--------SGEIYVGDRQVTKMKEYERSRFIGRVFQDPSM 91
Cdd:PRK13547 15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 G---TCPSLTVLENMALADNKGSSFLLQRGVNRRrtqhyreelSLLHMGLEDKLGVQVGSLSGGQ------RQALAMLI- 161
Cdd:PRK13547 95 AfafSAREIVLLGRYPHARRAGALTHRDGEIAWQ---------ALALAGATALVGRDVTTLSGGElarvqfARVLAQLWp 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 162 --ATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:PRK13547 166 phDAAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPAD 241
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
23-228 |
7.78e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.82 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVtkmKEYERSRFIGRV---------FQDpsmgt 93
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQValvsqnvhlFND----- 431
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 94 cpslTVLENMALA-DNKGSSFLLQRGVnrrRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATM--SPInlL 170
Cdd:PRK11176 432 ----TIANNIAYArTEQYSREQIEEAA---RMAYAMDFINKMDNGLDTVIGENGVLLSGGQRQRIAIARALLrdSPI--L 502
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 171 ILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHIM 228
Cdd:PRK11176 503 ILDEATSALDTESERAIQAALDELQKNR--TSLVIAHRLS-TIEKADEILVVEDGEIV 557
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
15-208 |
8.01e-14 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 68.59 E-value: 8.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSM-GT 93
Cdd:PRK10247 16 LAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYCAQTPTLfGD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 94 cpslTVLENMAladnkgssFLLQrgVNRRRTQHYREELSLLHMGL-EDKLGVQVGSLSGGQRQALAMLIATMSPINLLIL 172
Cdd:PRK10247 96 ----TVYDNLI--------FPWQ--IRNQQPDPAIFLDDLERFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLL 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 1852789824 173 DEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHN 208
Cdd:PRK10247 162 DEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHD 197
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
24-228 |
8.29e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 70.38 E-value: 8.29e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPsmgtcpsltVLENM 103
Cdd:PRK13657 353 DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQDA---------GLFNR 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 104 ALADNkgssflLQRGvnrrRTQHYREELSL---------LHMGLEDKLGVQVG----SLSGGQRQALAMLIATM--SPIn 168
Cdd:PRK13657 424 SIEDN------IRVG----RPDATDEEMRAaaeraqahdFIERKPDGYDTVVGergrQLSGGERQRLAIARALLkdPPI- 492
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 169 lLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHIM 228
Cdd:PRK13657 493 -LILDEATSALDVETEAKVKAALDELMKGR--TTFIIAHRLS-TVRNADRILVFDNGRVV 548
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
24-225 |
1.39e-13 |
|
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: 67.74 E-value: 1.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIY---VGDRQVTKMKEYERSRF-IGRVFQDPSMgtcPSLTV 99
Cdd:cd03290 19 NINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsnKNESEPSFEATRSRNRYsVAYAAQKPWL---LNATV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMALadnkGSSFLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAAL 179
Cdd:cd03290 96 EENITF----GSPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERGINLSGGQRQRICVARALYQNTNIVFLDDPFSAL 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1852789824 180 DPHSSENVM-ELTQRVAKEKHVTMLMVTHNLKFaVAYGDRLLMMHRG 225
Cdd:cd03290 172 DIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQY-LPHADWIIAMKDG 217
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
22-240 |
1.48e-13 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 68.41 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEI-YV----GDRQVTKMKEYERsRFIGR-----VFQDPSM 91
Cdd:PRK11701 22 CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRmrdgQLRDLYALSEAER-RRLLRtewgfVHQHPRD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 GTCPSLTVLEN-----MALADNkgssfllQRGVNRRRTQHYREELSLLHMGLEDklgvQVGSLSGGQRQALAmlIA---T 163
Cdd:PRK11701 101 GLRMQVSAGGNigerlMAVGAR-------HYGDIRATAGDWLERVEIDAARIDD----LPTTFSGGMQQRLQ--IArnlV 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 164 MSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGEDKKVLD 240
Cdd:PRK11701 168 THP-RLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVV--ESGLTDQVLD 241
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
33-234 |
1.67e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 68.58 E-value: 1.67e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 33 SFVAVVGSNGSGKTTILNLLCG-----SLPLGSGEIYVGDRQVTKMKE-YERSRFIGRVFQDPSmgtcP-SLTVLENMaL 105
Cdd:PRK14271 48 AVTSLMGPTGSGKTTFLRTLNRmndkvSGYRYSGDVLLGGRSIFNYRDvLEFRRRVGMLFQRPN----PfPMSIMDNV-L 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 106 ADNKGSSfLLQRGVNRRRTQHYREELSLLHmGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSE 185
Cdd:PRK14271 123 AGVRAHK-LVPRKEFRGVAQARLTEVGLWD-AVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTE 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1852789824 186 NVMELTQRVAKEkhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGE 234
Cdd:PRK14271 201 KIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTE 247
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
22-227 |
1.72e-13 |
|
Second domain of the ATP-binding cassette component of monosaccharide transport system; This family represents domain II of the carbohydrate uptake proteins that transport only monosaccharides (Monos). The Carb_Monos family is involved in the uptake of monosaccharides, such as pentoses (such as xylose, arabinose, and ribose) and hexoses (such as xylose, arabinose, and ribose), that cannot be broken down to simple sugars by hydrolysis. In members of Carb_Monos family the single hydrophobic gene product forms a homodimer, while the ABC protein represents a fusion of two nucleotide-binding domains. However, it is assumed that two copies of the ABC domains are present in the assembled transporter.
Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 66.69 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF-IGRVFQDP-SMGTCPSLTV 99
Cdd:cd03215 16 VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgIAYVPEDRkREGLVLDLSV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMALADnkgssfllqrgvnrrrtqhyreelsllhmgledklgvqvgSLSGG--QRQALAMLIATmsPINLLILDEHTA 177
Cdd:cd03215 96 AENIALSS----------------------------------------LLSGGnqQKVVLARWLAR--DPRVLILDEPTR 133
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1852789824 178 ALDPHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03215 134 GVDVGAKAEIYRLIRELADAG-KAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-248 |
1.82e-13 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.57 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 4 MEHIYKTFnPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGS--GEIYVGDR--QVTKMKEYERS 79
Cdd:PRK13549 8 MKNITKTF-GG----VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGTyeGEIIFEGEelQASNIRDTERA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 80 RfIGRVFQDPSMgtCPSLTVLENMALADNkgssfLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAM 159
Cdd:PRK13549 83 G-IAIIHQELAL--VKELSVLENIFLGNE-----ITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 160 LIATMSPINLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRG-HIMLDAA---GED 235
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGrHIGTRPAagmTED 233
|
250
....*....|....*
gi 1852789824 236 KKVLDV--RDLTNRF 248
Cdd:PRK13549 234 DIITMMvgRELTALY 248
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
14-207 |
2.04e-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: 67.13 E-value: 2.04e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 14 GSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMK-EYERS-RFIGRVfqdPSM 91
Cdd:cd03231 8 CERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRdSIARGlLYLGHA---PGI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 GTcpSLTVLENMA-LADNKGSSFLLQrgvnrrrtqhyreelSLLHMGLEDKLGVQVGSLSGGQ--RQALAMLIATMSPin 168
Cdd:cd03231 85 KT--TLSVLENLRfWHADHSDEQVEE---------------ALARVGLNGFEDRPVAQLSAGQqrRVALARLLLSGRP-- 145
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1852789824 169 LLILDEHTAALDPHSsenVMELTQRVAK--EKHVTMLMVTH 207
Cdd:cd03231 146 LWILDEPTTALDKAG---VARFAEAMAGhcARGGMVVLTTH 183
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
26-238 |
2.43e-13 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 67.80 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE--YERSRFIGRVFQDPSmGTCPSLTVLENM 103
Cdd:PRK13639 22 NFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKslLEVRKTVGIVFQNPD-DQLFAPTVEEDV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 104 ALAD-NKGssfLLQRGVNRRrtqhYREELSLLHM-GLEDKlgvQVGSLSGGQ--RQALAMLIAtMSPiNLLILDEHTAAL 179
Cdd:PRK13639 101 AFGPlNLG---LSKEEVEKR----VKEALKAVGMeGFENK---PPHHLSGGQkkRVAIAGILA-MKP-EIIVLDEPTSGL 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 180 DPHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGEDKKV 238
Cdd:PRK13639 169 DPMGASQIMKLLYDLNKEG-ITIIISTHDVDLVPVYADKVYVMSDGKII--KEGTPKEV 224
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
15-181 |
2.94e-13 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 66.80 E-value: 2.94e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMkeyERSRFIGRVFQDPSMGtc 94
Cdd:PRK13543 20 SRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRG---DRSRFMAYLGHLPGLK-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTVLENMaladnkgsSFLlqRGVNRRRTQHYREElSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDE 174
Cdd:PRK13543 95 ADLSTLENL--------HFL--CGLHGRRAKQMPGS-ALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163
|
....*..
gi 1852789824 175 HTAALDP 181
Cdd:PRK13543 164 PYANLDL 170
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
19-228 |
3.12e-13 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 68.21 E-value: 3.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 19 VVLFQDFNLQIAEGSFVAVVGSNGSGKT----TILNLLCGSLPLGSGEIYVGdRQVTKMKEYE----RSRFIGRVFQDPS 90
Cdd:PRK09473 29 VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGRIGGSATFNG-REILNLPEKElnklRAEQISMIFQDPM 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 91 MGTCPSLTVLENMAladnkgSSFLLQRGVNRrrTQHYREELSLL---HMGLEDK-LGVQVGSLSGGQRQALAMLIATMSP 166
Cdd:PRK09473 108 TSLNPYMRVGEQLM------EVLMLHKGMSK--AEAFEESVRMLdavKMPEARKrMKMYPHEFSGGMRQRVMIAMALLCR 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 167 INLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK09473 180 PKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTM 241
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
1-227 |
5.22e-13 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 68.12 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MV--RMEHIY--KTFNPGsvnEVVL----------FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVG 66
Cdd:COG1129 236 MVgrELEDLFpkRAAAPG---EVVLeveglsvggvVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLD 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 67 DRQVTkmkeyersrfigrvFQDPS------MGTCP----------SLTVLENMALA--DNKGSSFLLQRGVNRRRTQHYR 128
Cdd:COG1129 313 GKPVR--------------IRSPRdairagIAYVPedrkgeglvlDLSIRENITLAslDRLSRGGLLDRRRERALAEEYI 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 129 EELSLLHMGLEDKlgvqVGSLSGG--QRQALAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKhVTMLMVT 206
Cdd:COG1129 379 KRLRIKTPSPEQP----VGNLSGGnqQKVVLAKWLAT-DP-KVLILDEPTRGIDVGAKAEIYRLIRELAAEG-KAVIVIS 451
|
250 260
....*....|....*....|.
gi 1852789824 207 HNLKFAVAYGDRLLMMHRGHI 227
Cdd:COG1129 452 SELPELLGLSDRILVMREGRI 472
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
25-247 |
1.44e-12 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 65.58 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 25 FNLQiaEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGTCPSLTVlenma 104
Cdd:PRK15112 34 FTLR--EGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRSQRIRMIFQDPSTSLNPRQRI----- 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 105 ladnkGSSFLLQRGVNRRRTQHYREE---LSLLHMGL-EDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:PRK15112 107 -----SQILDFPLRLNTDLEPEQREKqiiETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 181 PHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGEDKKVLDVRDLTNR 247
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHELTKR 248
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
20-211 |
2.11e-12 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 66.51 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDR-QVTKMKEYersrfigRVFQDPSMgtcpslT 98
Cdd:PRK11147 333 QLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTKlEVAYFDQH-------RAELDPEK------T 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 99 VLENmaLADNKGSSFllqrgVNRRRtqhyREELSLlhmgLEDKL------GVQVGSLSGGQRQALamLIAT--MSPINLL 170
Cdd:PRK11147 400 VMDN--LAEGKQEVM-----VNGRP----RHVLGY----LQDFLfhpkraMTPVKALSGGERNRL--LLARlfLKPSNLL 462
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1852789824 171 ILDEHTAALDPHSsenvMELTQRVAKEKHVTMLMVTHNLKF 211
Cdd:PRK11147 463 ILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHDRQF 499
|
|
| AppF |
COG4608 |
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ... |
27-228 |
2.25e-12 |
|
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 65.52 E-value: 2.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 27 LQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF---IGRVFQDPSMGTCPSLTVLENM 103
Cdd:COG4608 39 FDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLrrrMQMVFQDPYASLNPRMTVGDII 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 104 ALAdnkgssFLLQRGVNRRRTQHYREELsllhmgLEdklgvQVG-----------SLSGGQRQ------ALAmliatMSP 166
Cdd:COG4608 119 AEP------LRIHGLASKAERRERVAEL------LE-----LVGlrpehadryphEFSGGQRQrigiarALA-----LNP 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 167 iNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKfAVAY-GDRLLMMHRGHIM 228
Cdd:COG4608 177 -KLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLS-VVRHiSDRVAVMYLGKIV 237
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
22-238 |
2.49e-12 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 66.23 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYER----------SRFIGRVFQDPSM 91
Cdd:PRK15439 279 FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlarglvylpeDRQSSGLYLDAPL 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 G--TCpSLTVLENmaladnkgsSFLLQRGVNRRRTQHYREELSLLHMGLEDklgvQVGSLSGGQRQALamLIA---TMSP 166
Cdd:PRK15439 359 AwnVC-ALTHNRR---------GFWIKPARENAVLERYRRALNIKFNHAEQ----AARTLSGGNQQKV--LIAkclEASP 422
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 167 InLLILDEHTAALDPHSSENVMELTQRVAKEkHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGEDKKV 238
Cdd:PRK15439 423 Q-LLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAINV 492
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
23-239 |
2.53e-12 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 66.20 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF-IGRVFQDP-SMGTCPSLTVL 100
Cdd:COG3845 275 KDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVAYIPEDRlGRGLVPDMSVA 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMAL----ADNKGSSFLLQRGVNRRRTQHYREELSLLHMGLEDKlgvqVGSLSGG--QRQALAMLIAtmSPINLLILDE 174
Cdd:COG3845 355 ENLILgryrRPPFSRGGFLDRKAIRAFAEELIEEFDVRTPGPDTP----ARSLSGGnqQKVILARELS--RDPKLLIAAQ 428
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 175 HTAALDPHSSENVME--LTQRvakEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM--LDAAGEDKKVL 239
Cdd:COG3845 429 PTRGLDVGAIEFIHQrlLELR---DAGAAVLLISEDLDEILALSDRIAVMYEGRIVgeVPAAEATREEI 494
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
26-249 |
2.77e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 66.15 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDpsmgtcpsltvlenmal 105
Cdd:PRK10522 343 NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFSAVFTD----------------- 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 106 adnkgsSFLLQRGVNRRRTQHYRE--ELSLLHMGLEDKLGVQVG-----SLSGGQRQALAMLIATMSPINLLILDEHTAA 178
Cdd:PRK10522 406 ------FHLFDQLLGPEGKPANPAlvEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLALAEERDILLLDEWAAD 479
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 179 LDPH-SSENVMELTQRVaKEKHVTMLMVTH-NLKFAVAygDRLLMMHRGHIMlDAAGEDKKvLDVRDLTNRFD 249
Cdd:PRK10522 480 QDPHfRREFYQVLLPLL-QEMGKTIFAISHdDHYFIHA--DRLLEMRNGQLS-ELTGEERD-AASRDAVARTA 547
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
14-225 |
3.08e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 3.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 14 GSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKT----TILNLLcGSLPLG--SGEIYVGDRQVTKMKEYE----RSRFIG 83
Cdd:PRK15134 19 QTVRTVV--NDVSLQIEAGETLALVGESGSGKSvtalSILRLL-PSPPVVypSGDIRFHGESLLHASEQTlrgvRGNKIA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 84 RVFQDPSMGTCPSLTVLENMAladnkgSSFLLQRGVnrRRTQHYREELSLLhmgleDKLGVQVGS---------LSGGQR 154
Cdd:PRK15134 96 MIFQEPMVSLNPLHTLEKQLY------EVLSLHRGM--RREAARGEILNCL-----DRVGIRQAAkrltdyphqLSGGER 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 155 QALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRG 225
Cdd:PRK15134 163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNG 233
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
2-226 |
6.86e-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: 61.31 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGsvnevVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVtkmkeyersrf 81
Cdd:cd03221 1 IELENLSKTYGGK-----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGSTVK----------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQdpsmgtcpsltvlenmaladnkgssfllqrgvnrrrtqhyreelsllhmgledklgvqvgsLSGGQRQALAMLI 161
Cdd:cd03221 65 IGYFEQ-------------------------------------------------------------LSGGEKMRLALAK 83
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 162 ATMSPINLLILDEHTAALDPhssENVMELTQRVAKEKHvTMLMVTHNLKF--AVAygDRLLMMHRGH 226
Cdd:cd03221 84 LLLENPNLLLLDEPTNHLDL---ESIEALEEALKEYPG-TVILVSHDRYFldQVA--TKIIELEDGK 144
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
18-209 |
7.37e-12 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 64.74 E-value: 7.37e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 18 EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtcpSL 97
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLF---SG 569
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 98 TVLENMALADNKGSSFLLQrgvNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTA 177
Cdd:TIGR00958 570 SVRENIAYGLTDTPDEEIM---AAAKAANAHDFIMEFPNGYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATS 646
|
170 180 190
....*....|....*....|....*....|..
gi 1852789824 178 ALDPHSSENVMELTQRvakeKHVTMLMVTHNL 209
Cdd:TIGR00958 647 ALDAECEQLLQESRSR----ASRTVLLIAHRL 674
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
21-207 |
7.50e-12 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 62.66 E-value: 7.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTK-MKEYERSR-FIGRvfqdpSMGTCPSLT 98
Cdd:PRK13540 16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKdLCTYQKQLcFVGH-----RSGINPYLT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 99 VLENmALADNKGSSFLLQrgvnrrrtqhyREELSLLhMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAA 178
Cdd:PRK13540 91 LREN-CLYDIHFSPGAVG-----------ITELCRL-FSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157
|
170 180
....*....|....*....|....*....
gi 1852789824 179 LDPHSSENVMELTQRvAKEKHVTMLMVTH 207
Cdd:PRK13540 158 LDELSLLTIITKIQE-HRAKGGAVLLTSH 185
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
26-235 |
1.06e-11 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 63.67 E-value: 1.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCG----SLPLGSGEIYVGDRQVTKMKEYERSRFIGR----VFQDPSMGTCPSL 97
Cdd:PRK15093 27 SMTLTEGEIRGLVGESGSGKSLIAKAICGvtkdNWRVTADRMRFDDIDLLRLSPRERRKLVGHnvsmIFQEPQSCLDPSE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 98 TV----LENMALADNKGSSFllQRgVNRRRtqhyREELSLLH-MGLEDKLGVQVG---SLSGGQRQALAMLIATMSPINL 169
Cdd:PRK15093 107 RVgrqlMQNIPGWTYKGRWW--QR-FGWRK----RRAIELLHrVGIKDHKDAMRSfpyELTEGECQKVMIAIALANQPRL 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 170 LILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:PRK15093 180 LIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKE 245
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
2-207 |
1.97e-11 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 61.90 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFN-PGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLP--LGSGEIYVGDRQVtkmkeYER 78
Cdd:COG2401 25 ERVAIVLEAFGvELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKgtPVAGCVDVPDNQF-----GRE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 79 SRFIGRVFQDPSMGTcpSLTVLENMALADNkgssFLLqrgvnRRRtqhYREelsllhmgledklgvqvgsLSGGQ--RQA 156
Cdd:COG2401 100 ASLIDAIGRKGDFKD--AVELLNAVGLSDA----VLW-----LRR---FKE-------------------LSTGQkfRFR 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 157 LAMLIATmSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTH 207
Cdd:COG2401 147 LALLLAE-RP-KLLVIDEFCSHLDRQTAKRVARNLQKLARRAGITLVVATH 195
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
2-211 |
2.11e-11 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 63.37 E-value: 2.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNPGsvnevVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIyvgdrqvtkmKEYERSRf 81
Cdd:PRK15064 320 LEVENLTKGFDNG-----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV----------KWSENAN- 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 IGRVFQDPSMGTCPSLTVLENMALADNKGSSFLLQRGVNRRrtqhyreelsLLHMGleDKLGVQVGSLSGGQ--RQALAM 159
Cdd:PRK15064 384 IGYYAQDHAYDFENDLTLFDWMSQWRQEGDDEQAVRGTLGR----------LLFSQ--DDIKKSVKVLSGGEkgRMLFGK 451
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 160 LIatMSPINLLILDEHTAALDPHSSENVmeltqRVAKEKHV-TMLMVTHNLKF 211
Cdd:PRK15064 452 LM--MQKPNVLVMDEPTNHMDMESIESL-----NMALEKYEgTLIFVSHDREF 497
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
22-222 |
2.12e-11 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 62.59 E-value: 2.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 22 FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKeyeRSRFIGRVFQDPSMGTcpSLTVL- 100
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQAL---QKNLVAYVPQSEEVDW--SFPVLv 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALADNKGssfllQRGVNRRRTQHYRE--ELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAA 178
Cdd:PRK15056 98 EDVVMMGRYG-----HMGWLRRAKKRDRQivTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1852789824 179 LDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAVAYGDRLLMM 222
Cdd:PRK15056 173 VDVKTEARIISLLRELRDEGK-TMLVSTHNLGSVTEFCDYTVMV 215
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
24-227 |
2.15e-11 |
|
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: 61.66 E-value: 2.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPS--MGTCPSltvle 101
Cdd:cd03369 26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTlfSGTIRS----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 102 nmaladnkgssfllqrgvNRRRTQHYREElsllhmGLEDKLGVQVG--SLSGGQRQALAMLIATMSPINLLILDEHTAAL 179
Cdd:cd03369 101 ------------------NLDPFDEYSDE------EIYGALRVSEGglNLSQGQRQLLCLARALLKRPRVLVLDEATASI 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1852789824 180 DPHSSenvmELTQRVAKE--KHVTMLMVTHNLKFAVAYgDRLLMMHRGHI 227
Cdd:cd03369 157 DYATD----ALIQKTIREefTNSTILTIAHRLRTIIDY-DKILVMDAGEV 201
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
20-209 |
3.30e-11 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 61.70 E-value: 3.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE---YERSRFIGRVFQDPSMGTcpS 96
Cdd:PRK11831 21 CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRsrlYTVRKRMSMLFQSGALFT--D 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENMAladnkgssFLLQrgvnrrrtQHYREELSLLH---------MGLEDKLGVQVGSLSGG--QRQALAMLIAtMS 165
Cdd:PRK11831 99 MNVFDNVA--------YPLR--------EHTQLPAPLLHstvmmkleaVGLRGAAKLMPSELSGGmaRRAALARAIA-LE 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1852789824 166 PiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNL 209
Cdd:PRK11831 162 P-DLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDV 204
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-248 |
3.52e-11 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 62.90 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNL-----QIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIyvgDRQVT---KmKEYERSRFIGRVFQdpsmgtcp 95
Cdd:PRK13409 352 DFSLeveggEIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEV---DPELKisyK-PQYIKPDYDGTVED-------- 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 96 sltVLENMalADNKGSSFllqrgvnrrrtqhYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEH 175
Cdd:PRK13409 420 ---LLRSI--TDDLGSSY-------------YKSEI-IKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 480
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 176 TAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRlLMMHRG----HimldaaGEDKKVLDVRDLTNRF 248
Cdd:PRK13409 481 SAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDR-LMVFEGepgkH------GHASGPMDMREGMNRF 550
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
35-228 |
3.63e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 3.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 35 VAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGTCPSLTVLENMALADNKGSSFL 114
Cdd:PLN03232 1265 VGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPVLFSGTVRFNIDPFSEHNDADLWEA 1344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 115 LQRGvnrrrtqHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSenvmELTQRV 194
Cdd:PLN03232 1345 LERA-------HIKDVIDRNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRTD----SLIQRT 1413
|
170 180 190
....*....|....*....|....*....|....*.
gi 1852789824 195 AKE--KHVTMLMVTHNLKfAVAYGDRLLMMHRGHIM 228
Cdd:PLN03232 1414 IREefKSCTMLVIAHRLN-TIIDCDKILVLSSGQVL 1448
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
3-209 |
3.89e-11 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 62.62 E-value: 3.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 3 RMEHIYKTFnPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVtkmkeyersRF- 81
Cdd:PRK11288 6 SFDGIGKTF-PG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM---------RFa 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 ---------IGRVFQDpsMGTCPSLTVLENMALAD--NKGssfllqrGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLS 150
Cdd:PRK11288 72 sttaalaagVAIIYQE--LHLVPEMTVAENLYLGQlpHKG-------GIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLS 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 151 GGQRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVtMLMVTHNL 209
Cdd:PRK11288 143 IGQRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRM 200
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
23-217 |
6.13e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 60.95 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTIL------NLLC------GSLPLGSGEIYVGDrqvtkMKEYERSRFIGRVFQDPS 90
Cdd:PRK14243 27 KNVWLDIPKNQITAFIGPSGCGKSTILrcfnrlNDLIpgfrveGKVTFHGKNLYAPD-----VDPVEVRRRIGMVFQKPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 91 mgtcP-SLTVLENMAL-ADNKGSSFLLQRGVNRRRTQhyreelSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPIN 168
Cdd:PRK14243 102 ----PfPKSIYDNIAYgARINGYKGDMDELVERSLRQ------AALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPE 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1852789824 169 LLILDEHTAALDPHSSENVMELTQRVaKEKHvTMLMVTHNLKFAVAYGD 217
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHEL-KEQY-TIIIVTHNMQQAARVSD 218
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
1-225 |
7.72e-11 |
|
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]
Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 61.95 E-value: 7.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnPGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMkeyersr 80
Cdd:TIGR01257 1937 ILRLNELTKVY-SGTSSPAV--DRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTN------- 2006
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 fIGRVFQdpSMGTCPSLTVLENMALADNKGSSFLLQRGVNRRRTQHYrEELSLLHMGLEDKLGVQVGSLSGGQRQALAML 160
Cdd:TIGR01257 2007 -ISDVHQ--NMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKV-ANWSIQSLGLSLYADRLAGTYSGGNKRKLSTA 2082
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 161 IATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLmVTHNLKFAVAYGDRLLMMHRG 225
Cdd:TIGR01257 2083 IALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVL-TSHSMEECEALCTRLAIMVKG 2146
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
9-228 |
1.18e-10 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.27 E-value: 1.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 9 KTFN-PGSVNEVVlfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYE-RSRFiGRVF 86
Cdd:PRK10789 319 RQFTyPQTDHPAL--ENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSwRSRL-AVVS 395
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 87 QDPSMGtcpSLTVLENMALADNKGSSFLLQRgVNRRRTQHyrEELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSP 166
Cdd:PRK10789 396 QTPFLF---SDTVANNIALGRPDATQQEIEH-VARLASVH--DDILRLPQGYDTEVGERGVMLSGGQKQRISIARALLLN 469
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 167 INLLILDEHTAALDPHSSENVMELTQRVAKEKhvTMLMVTHNLKfAVAYGDRLLMMHRGHIM 228
Cdd:PRK10789 470 AEILILDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLS-ALTEASEILVMQHGHIA 528
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
23-225 |
1.41e-10 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 61.02 E-value: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVG-------DRQVTKMKEYERSRF-------IGRVFQD 88
Cdd:PRK10261 33 RNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDkmllrrrSRQVIELSEQSAAQMrhvrgadMAMIFQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 89 PSMGTCPSLTVLENMAladnkgSSFLLQRGVNRRRTqhYREELSLLHM----GLEDKLGVQVGSLSGGQRQALAMLIATM 164
Cdd:PRK10261 113 PMTSLNPVFTVGEQIA------ESIRLHQGASREEA--MVEAKRMLDQvripEAQTILSRYPHQLSGGMRQRVMIAMALS 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 165 SPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRG 225
Cdd:PRK10261 185 CRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQG 245
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
11-235 |
2.17e-10 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 60.81 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 11 FNPGSVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTK--MKEYERSRfIGRVFQD 88
Cdd:PTZ00265 390 FHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKdiNLKWWRSK-IGVVSQD 468
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 89 P-------------SMGTCPSLTVLENMALADNKGSsfllQRGVNRRRTQHYR------------EELSLLHM------- 136
Cdd:PTZ00265 469 PllfsnsiknnikySLYSLKDLEALSNYYNEDGNDS----QENKNKRNSCRAKcagdlndmsnttDSNELIEMrknyqti 544
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 137 -------------------GLEDKLGVQVGS----LSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQR 193
Cdd:PTZ00265 545 kdsevvdvskkvlihdfvsALPDKYETLVGSnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINN 624
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1852789824 194 VAKEKHVTMLMVTHNLKfAVAYGDRLLMM---HRGH-IMLDAAGED 235
Cdd:PTZ00265 625 LKGNENRITIIIAHRLS-TIRYANTIFVLsnrERGStVDVDIIGED 669
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
26-228 |
3.87e-10 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 58.95 E-value: 3.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF---IGRVFQDPSMGTCPSLTVLEN 102
Cdd:PRK15079 41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVrsdIQMIFQDPLASLNPRMTIGEI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 103 MAladnkgssfllqrgvNRRRTqhYREELSllhmGLEDKLGVQ-----VGSL-----------SGGQRQALAMLIATMSP 166
Cdd:PRK15079 121 IA---------------EPLRT--YHPKLS----RQEVKDRVKammlkVGLLpnlinryphefSGGQCQRIGIARALILE 179
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 167 INLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK15079 180 PKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAV 241
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
24-227 |
3.97e-10 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 59.99 E-value: 3.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPlgsgeiyvgdrqvtkmkEYERSRFIGRvfqdPSMGTCPSLTVLENM 103
Cdd:PLN03232 635 DINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-----------------HAETSSVVIR----GSVAYVPQVSWIFNA 693
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 104 ALADNK--GSSFLLQR---GVNRRRTQHyreELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAA 178
Cdd:PLN03232 694 TVRENIlfGSDFESERywrAIDVTALQH---DLDLLPGRDLTEIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 179 LDPHSSENVMEltqRVAKE--KHVTMLMVTHNLKFaVAYGDRLLMMHRGHI 227
Cdd:PLN03232 771 LDAHVAHQVFD---SCMKDelKGKTRVLVTNQLHF-LPLMDRIILVSEGMI 817
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
20-235 |
4.09e-10 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 59.79 E-value: 4.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVgdrqvtkmkeyERSrfIGRVFQDPSMGTCpslTV 99
Cdd:PTZ00243 674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWA-----------ERS--IAYVPQQAWIMNA---TV 737
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMALADNKGSSfLLQRGVnrrRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAAL 179
Cdd:PTZ00243 738 RGNILFFDEEDAA-RLADAV---RVSQLEADLAQLGGGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 180 DPHSSENVME--LTQRVAKEkhvTMLMVTHNLKFaVAYGDRLLMMHRGHIMLDAAGED 235
Cdd:PTZ00243 814 DAHVGERVVEecFLGALAGK---TRVLATHQVHV-VPRADYVVALGDGRVEFSGSSAD 867
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
26-218 |
6.43e-10 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 57.86 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLL------------CGSLPLGSGEIYvGDRQVTkmkeYERSRFIGRVFQDPSmgt 93
Cdd:PRK14239 25 SLDFYPNEITALIGPSGSGKSTLLRSInrmndlnpevtiTGSIVYNGHNIY-SPRTDT----VDLRKEIGMVFQQPN--- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 94 cP-SLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELSLLHMGL----EDKLGVQVGSLSGGQRQ--ALAMLIATmSP 166
Cdd:PRK14239 97 -PfPMSIYENVVYG-------LRLKGIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQrvCIARVLAT-SP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 167 iNLLILDEHTAALDPHSSENVmELTQRVAKEKHvTMLMVTHNLKFAVAYGDR 218
Cdd:PRK14239 168 -KIILLDEPTSALDPISAGKI-EETLLGLKDDY-TMLLVTRSMQQASRISDR 216
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
26-227 |
7.32e-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: 59.19 E-value: 7.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCGslplgsgeiyvgdrqvtKMKEYErsrfiGRVFQDPSMGTCPSLTVLENMAL 105
Cdd:TIGR00957 658 TFSIPEGALVAVVGQVGCGKSSLLSALLA-----------------EMDKVE-----GHVHMKGSVAYVPQQAWIQNDSL 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 106 ADNkgssFLLQRGVNRRRTQHYRE------ELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAAL 179
Cdd:TIGR00957 716 REN----ILFGKALNEKYYQQVLEacallpDLEILPSGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAV 791
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 180 DPHSSENVMELT---QRVAKEKhvTMLMVTHNLKFaVAYGDRLLMMHRGHI 227
Cdd:TIGR00957 792 DAHVGKHIFEHVigpEGVLKNK--TRILVTHGISY-LPQVDVIIVMSGGKI 839
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
21-209 |
1.86e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.58 E-value: 1.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLgSGEIYV-GDRQVTKMKEYERSRFIGRVFQDPSMgTCPSLTV 99
Cdd:PRK14258 22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNEL-ESEVRVeGRVEFFNQNIYERRVNLNRLRRQVSM-VHPKPNL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LEnMALADNkgssflLQRGVnrrRTQHYREELSL------------LHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPI 167
Cdd:PRK14258 100 FP-MSVYDN------VAYGV---KIVGWRPKLEIddivesalkdadLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKP 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1852789824 168 NLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNL 209
Cdd:PRK14258 170 KVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNL 211
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
19-227 |
2.19e-09 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 56.25 E-value: 2.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 19 VVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG----SGEIYVGDRQVTKMKEyeRSRFIGRVFQDPSMGTC 94
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGvrqtAGRVLLDGKPVAPCAL--RGRKIATIMQNPRSAFN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PsltvLENMAladNKGSSFLLQRGVNRRRTQhyreelsLLH----MGLEDK---LGVQVGSLSGG--QRQALAMliATMS 165
Cdd:PRK10418 94 P----LHTMH---THARETCLALGKPADDAT-------LTAaleaVGLENAarvLKLYPFEMSGGmlQRMMIAL--ALLC 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 166 PINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRI 219
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
21-225 |
4.73e-09 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 54.56 E-value: 4.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG--SGEIYVGDRQVTKmkeyERSRFIGRVFQDPSMGtcPSLT 98
Cdd:cd03232 22 LLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAGviTGEILINGRPLDK----NFQRSTGYVEQQDVHS--PNLT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 99 VLENMALadnkgsSFLLqRGvnrrrtqhyreelsllhmgledklgvqvgsLSGGQRQALAMLIATMSPINLLILDEHTAA 178
Cdd:cd03232 96 VREALRF------SALL-RG------------------------------LSVEQRKRLTIGVELAAKPSILFLDEPTSG 138
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1852789824 179 LDPHSSENVMELTQRVAKEKHvTMLMVTHNLKFAV-AYGDRLLMMHRG 225
Cdd:cd03232 139 LDSQAAYNIVRFLKKLADSGQ-AILCTIHQPSASIfEKFDRLLLLKRG 185
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
23-227 |
1.67e-08 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 54.79 E-value: 1.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYER-SRFIGRVFQD-PSMGTCPSLTVL 100
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAvKKGMAYITESrRDNGFFPNFSIA 359
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALADN------KGSSFLLQRGVNRRRTQHYREELSLLHMGLEDklgvQVGSLSGGQRQALAMLIATMSPINLLILDE 174
Cdd:PRK09700 360 QNMAISRSlkdggyKGAMGLFHEVDEQRTAENQRELLALKCHSVNQ----NITELSGGNQQKVLISKWLCCCPEVIIFDE 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 175 HTAALDPHSSENVMELTQRVAKEKHVtMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK09700 436 PTRGIDVGAKAEIYKVMRQLADDGKV-ILMVSSELPEIITVCDRIAVFCEGRL 487
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
17-247 |
1.85e-08 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 53.86 E-value: 1.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKE--YERSRFIGRVFQDPSMGTC 94
Cdd:PRK13638 13 DEPVL-KGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDYSKRglLALRQQVATVFQDPEQQIF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PS------LTVLENMALADNKgssflLQRGVNRRRT----QHYREElsllhmgledklgvQVGSLSGGQRQALAMLIATM 164
Cdd:PRK13638 92 YTdidsdiAFSLRNLGVPEAE-----ITRRVDEALTlvdaQHFRHQ--------------PIQCLSHGQKKRVAIAGALV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 165 SPINLLILDEHTAALDPHSSENVMELTQRVAKE-KHVtmLMVTHNLKFAVAYGDRLLMMHRGHIMldAAGEDKKVLDVRD 243
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHV--IISSHDIDLIYEISDAVYVLRQGQIL--THGAPGEVFACTE 228
|
....
gi 1852789824 244 LTNR 247
Cdd:PRK13638 229 AMEQ 232
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
26-206 |
4.13e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 53.48 E-value: 4.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 26 NLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGTcpsLTVLEnmal 105
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKLVSDEWQRNNTDM---LSPGE---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 106 aDNKG--SSFLLQRGV-NRRRTQHYREELsllhmGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPH 182
Cdd:PRK10938 96 -DDTGrtTAEIIQDEVkDPARCEQLAQQF-----GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169
|
170 180
....*....|....*....|....
gi 1852789824 183 SSENVMELTQRVAKEKHVTMLMVT 206
Cdd:PRK10938 170 SRQQLAELLASLHQSGITLVLVLN 193
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
2-180 |
4.98e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.40 E-value: 4.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDrqVTKMKEYERSRf 81
Cdd:TIGR03719 323 IEAENLTKAFG-----DKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE--TVKLAYVDQSR- 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 82 igrvfqdpsMGTCPSLTVLENMAladnkGSSFLLQRGvnrRRTQHYREELSLLHMGLED--KLgvqVGSLSGGQRQALAM 159
Cdd:TIGR03719 395 ---------DALDPNKTVWEEIS-----GGLDIIKLG---KREIPSRAYVGRFNFKGSDqqKK---VGQLSGGERNRVHL 454
|
170 180
....*....|....*....|.
gi 1852789824 160 LIATMSPINLLILDEHTAALD 180
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLD 475
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
1-227 |
7.40e-08 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 52.04 E-value: 7.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvNEVVLfQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIyvgdrqvtkmkEYERSR 80
Cdd:PRK09544 4 LVSLENVSVSFG----QRRVL-SDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-----------KRNGKL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 81 FIGRVFQDPSMGTCPSLTVLENMALADNKGSSFLLQrGVNRRRTQHyreelsLLHMGLEdklgvqvgSLSGGQRQALAML 160
Cdd:PRK09544 68 RIGYVPQKLYLDTTLPLTVNRFLRLRPGTKKEDILP-ALKRVQAGH------LIDAPMQ--------KLSGGETQRVLLA 132
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 161 IATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRgHI 227
Cdd:PRK09544 133 RALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCLNH-HI 198
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
32-241 |
7.52e-08 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 52.82 E-value: 7.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 32 GSFVAV---------------VGSNGSGKTTILNLLCGSLPLGSGEIYV-------GDRQVtkmkeyeRSRfIGRVFQDP 89
Cdd:NF033858 277 GDFTAVdhvsfrirrgeifgfLGSNGCGKSTTMKMLTGLLPASEGEAWLfgqpvdaGDIAT-------RRR-VGYMSQAF 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 90 SMGTcpSLTVLENMALadnkgssfllqrgvnrrrtqHYReelsLLHM----------------GLEDKLGVQVGSLSGGQ 153
Cdd:NF033858 349 SLYG--ELTVRQNLEL--------------------HAR----LFHLpaaeiaarvaemlerfDLADVADALPDSLPLGI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 154 RQ----ALAMLiatMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAvAYGDRLLMMHRGhiml 229
Cdd:NF033858 403 RQrlslAVAVI---HKP-ELLILDEPTSGVDPVARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAG---- 473
|
250
....*....|..
gi 1852789824 230 daagedkKVLDV 241
Cdd:NF033858 474 -------RVLAS 478
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
2-207 |
1.12e-07 |
|
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: 52.11 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 2 VRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCG--SLPLGSGEIYVGDRQVTKMKEYERS 79
Cdd:TIGR03269 1 IEVKNLTKKFD-----GKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGmdQYEPTSGRIIYHVALCEKCGYVERP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 80 RFIGRvfQDPSMGTCPSLTVLENMALAD------NKGSSFLLQRG----------VNRRRTQH---YREE------LSLL 134
Cdd:TIGR03269 76 SKVGE--PCPVCGGTLEPEEVDFWNLSDklrrriRKRIAIMLQRTfalygddtvlDNVLEALEeigYEGKeavgraVDLI 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 135 HM-GLEDKLGVQVGSLSGG--QRQALAMLIATmSPInLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTH 207
Cdd:TIGR03269 154 EMvQLSHRITHIARDLSGGekQRVVLARQLAK-EPF-LFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
24-230 |
1.22e-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: 52.13 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLP-LGSGEIYVGDRQV-TKMKEYERSRFIGRVFQD-PSMGTCPSLTVL 100
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVdIRNPAQAIRAGIAMVPEDrKRHGIVPILGVG 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALADNKGSSFLLQRGvNRRRTQHYREELSLLHMGLEDKLgVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:TIGR02633 358 KNITLSVLKSFCFKMRID-AAAELQIIGSAIQRLKVKTASPF-LPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVD 435
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1852789824 181 PHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLD 230
Cdd:TIGR02633 436 VGAKYEIYKLINQLAQEG-VAIIVVSSELAEVLGLSDRVLVIGEGKLKGD 484
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
20-227 |
1.46e-07 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 52.26 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPsmgtcpsltV 99
Cdd:TIGR00957 1300 LVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDP---------V 1370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMALAdnkgssfllqrgVNRRRTQHYREE-----LSLLHM-----GLEDKLGVQVG----SLSGGQRQALAMLIATMS 165
Cdd:TIGR00957 1371 LFSGSLR------------MNLDPFSQYSDEevwwaLELAHLktfvsALPDKLDHECAeggeNLSVGQRQLVCLARALLR 1438
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1852789824 166 PINLLILDEHTAALDpHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYgDRLLMMHRGHI 227
Cdd:TIGR00957 1439 KTKILVLDEATAAVD-LETDNLIQSTIRTQFED-CTVLTIAHRLNTIMDY-TRVIVLDKGEV 1497
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
16-209 |
1.61e-07 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 51.63 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 16 VNEVVLFQDFNLQIAEGSFVAVVGSNGSGK-TTILNLLcgSLPLGSGEIYVGDRQVTKMKEYE----RSRfIGRVFQDPS 90
Cdd:PRK15134 296 VDHNVVVKNISFTLRPGETLGLVGESGSGKsTTGLALL--RLINSQGEIWFDGQPLHNLNRRQllpvRHR-IQVVFQDPN 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 91 MGTCPSLTVLENMAladnKGssflLQrgVNRRR-TQHYREELSLLHM---GLEDKLGVQV-GSLSGGQRQALAMLIATMS 165
Cdd:PRK15134 373 SSLNPRLNVLQIIE----EG----LR--VHQPTlSAAQREQQVIAVMeevGLDPETRHRYpAEFSGGQRQRIAIARALIL 442
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1852789824 166 PINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNL 209
Cdd:PRK15134 443 KPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDL 486
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
21-226 |
1.92e-07 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.83 E-value: 1.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIyvgdrqvtkmkeyersRFIGRVFQDPSMGTCPSLTVL 100
Cdd:TIGR01271 441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRISFSPQTSWIMPGTIK 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALadnkGSSFLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:TIGR01271 505 DNIIF----GLSYDEYRYTSVIKACQLEEDIALFPEKDKTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1852789824 181 PHSSENVME--LTQRVAKEkhvTMLMVTHNLKFaVAYGDRLLMMHRGH 226
Cdd:TIGR01271 581 VVTEKEIFEscLCKLMSNK---TRILVTSKLEH-LKKADKILLLHEGV 624
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
32-225 |
2.36e-07 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 51.65 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 32 GSFVAVVGSNGSGKTTILNLLCGSLPLG---SGEIYVGDRQVTkmKEYERSrfIGRVFQ-DPSMGTcpsLTVLENMalad 107
Cdd:TIGR00956 789 GTLTALMGASGAGKTTLLNVLAERVTTGvitGGDRLVNGRPLD--SSFQRS--IGYVQQqDLHLPT---STVRESL---- 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 108 nKGSSFLLQ-RGVNRRRTQHYREE-LSLLHM-GLEDKL-GVQVGSLSGGQRQALAM---LIAtmSPINLLILDEHTAALD 180
Cdd:TIGR00956 858 -RFSAYLRQpKSVSKSEKMEYVEEvIKLLEMeSYADAVvGVPGEGLNVEQRKRLTIgveLVA--KPKLLLFLDEPTSGLD 934
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1852789824 181 PHSSENVMELTQRVAkeKHVTMLMVTHNLKFAVAYG--DRLLMMHRG 225
Cdd:TIGR00956 935 SQTAWSICKLMRKLA--DHGQAILCTIHQPSAILFEefDRLLLLQKG 979
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
29-180 |
3.35e-07 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 50.65 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 29 IAEGSFVAVVGSNGSGKTTILNLLCGSLPLGS--GEIYVGDRQVTKmkeyERSRFIGRVFQDPSMgtCPSLTVLENMALA 106
Cdd:PLN03211 91 ASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPTK----QILKRTGFVTQDDIL--YPHLTVRETLVFC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 107 dnkgSSFLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGS-----LSGGQRQALAmlIATMSPIN--LLILDEHTAAL 179
Cdd:PLN03211 165 ----SLLRLPKSLTKQEKILVAESV-ISELGLTKCENTIIGNsfirgISGGERKRVS--IAHEMLINpsLLILDEPTSGL 237
|
.
gi 1852789824 180 D 180
Cdd:PLN03211 238 D 238
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
21-225 |
4.47e-07 |
|
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: 49.86 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIyvgdrqvtkmkeyersRFIGRVFQDPSMGTCPSLTVL 100
Cdd:cd03291 52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------------KHSGRISFSSQFSWIMPGTIK 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 101 ENMALadnkGSSFLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALD 180
Cdd:cd03291 116 ENIIF----GVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLD 191
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1852789824 181 PHSSENVME--LTQRVAKEKHVTMLMVTHNLKFAvaygDRLLMMHRG 225
Cdd:cd03291 192 VFTEKEIFEscVCKLMANKTRILVTSKMEHLKKA----DKILILHEG 234
|
|
| YddA |
COG4178 |
ABC-type uncharacterized transport system, permease and ATPase components [General function ... |
20-207 |
5.47e-07 |
|
ABC-type uncharacterized transport system, permease and ATPase components [General function prediction only];
Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 50.19 E-value: 5.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQvtkmkeyersrfigRVF---QDPSMgtcPS 96
Cdd:COG4178 377 PLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA--------------RVLflpQRPYL---PL 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENMALADnkgssfllqrgvnrRRTQHYREEL-SLLHM-GLE---DKLGV-----QVgsLSGGQRQALA---MLIAt 163
Cdd:COG4178 440 GTLREALLYPA--------------TAEAFSDAELrEALEAvGLGhlaERLDEeadwdQV--LSLGEQQRLAfarLLLH- 502
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1852789824 164 mSPiNLLILDEHTAALDPHSSENVMELTQRvaKEKHVTMLMVTH 207
Cdd:COG4178 503 -KP-DWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
25-228 |
5.63e-07 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 49.58 E-value: 5.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 25 FNLQiaEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVT---KMKEYERSRFIGRVFQDPSMGTCPSLTV-- 99
Cdd:PRK11308 36 FTLE--RGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLkadPEAQKLLRQKIQIVFQNPYGSLNPRKKVgq 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 -LE-----NMALA----DNKGSSFLLQRGVnrrRTQHYREelsLLHMgledklgvqvgsLSGGQRQALAMLIATMSPINL 169
Cdd:PRK11308 114 iLEeplliNTSLSaaerREKALAMMAKVGL---RPEHYDR---YPHM------------FSGGQRQRIAIARALMLDPDV 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1852789824 170 LILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK11308 176 VVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
35-228 |
1.15e-06 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 49.35 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 35 VAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMGtcpSLTVLENMalaD--NKGSS 112
Cdd:PLN03130 1268 VGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLF---SGTVRFNL---DpfNEHND 1341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 113 FLLQRGVNRrrtQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSenvmELTQ 192
Cdd:PLN03130 1342 ADLWESLER---AHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRTD----ALIQ 1414
|
170 180 190
....*....|....*....|....*....|....*...
gi 1852789824 193 RVAKE--KHVTMLMVTHNLKfAVAYGDRLLMMHRGHIM 228
Cdd:PLN03130 1415 KTIREefKSCTMLIIAHRLN-TIIDCDRILVLDAGRVV 1451
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
31-209 |
1.21e-06 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 49.01 E-value: 1.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 31 EGSFVAVVGSNGSGKTTILNLLCGSL-P-LGSGEIYVGDRQV------TKMKEYERS---------------RFIGRVFQ 87
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELkPnLGDYDEEPSWDEVlkrfrgTELQDYFKKlangeikvahkpqyvDLIPKVFK 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 88 dpsmGTCPSLtvLENmalADNKGSSfllqrgvnrrrtQHYREELSLLHMgledkLGVQVGSLSGGQRQALAMLIATMSPI 167
Cdd:COG1245 178 ----GTVREL--LEK---VDERGKL------------DELAEKLGLENI-----LDRDISELSGGELQRVAIAAALLRDA 231
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1852789824 168 NLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNL 209
Cdd:COG1245 232 DFYFFDEPSSYLDIYQRLNVARLIRELAEEGK-YVLVVEHDL 272
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
15-89 |
1.46e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 48.10 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCG--SLPLGSGEIYVGDRQVTKMKEYERSR---FIGrvFQDP 89
Cdd:CHL00131 16 SVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHlgiFLA--FQYP 93
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
24-227 |
2.52e-06 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 48.08 E-value: 2.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRF-IGRVFQDPSM-GTCPSLTVLE 101
Cdd:PRK10762 270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDGLANgIVYISEDRKRdGLVLGMSVKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 102 NMAL-ADNKGSSFLLQrgvnrrrTQHYREelsllHMGLEDKLGV----------QVGSLSGGQRQALAMLIATMSPINLL 170
Cdd:PRK10762 350 NMSLtALRYFSRAGGS-------LKHADE-----QQAVSDFIRLfniktpsmeqAIGLLSGGNQQKVAIARGLMTRPKVL 417
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1852789824 171 ILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK10762 418 ILDEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
20-207 |
4.16e-06 |
|
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: 45.61 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYvgdrqvtkMKEYERSRFIGrvfQDPSMgtcPSLTV 99
Cdd:cd03223 15 VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG--------MPEGEDLLFLP---QRPYL---PLGTL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 lenmaladnkgssfllqrgvnrrrtqhyREELSLLhmgLEDKlgvqvgsLSGGQRQALAMliatmspINLL-------IL 172
Cdd:cd03223 81 ----------------------------REQLIYP---WDDV-------LSGGEQQRLAF-------ARLLlhkpkfvFL 115
|
170 180 190
....*....|....*....|....*....|....*
gi 1852789824 173 DEHTAALDPHSSENVMELtqrvAKEKHVTMLMVTH 207
Cdd:cd03223 116 DEATSALDEESEDRLYQL----LKELGITVISVGH 146
|
|
| ABC_Rad50 |
cd03240 |
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ... |
34-207 |
6.39e-06 |
|
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.
Pssm-ID: 213207 [Multi-domain] Cd Length: 204 Bit Score: 45.68 E-value: 6.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 34 FVAVVGSNGSGKTTILNL----LCGSLPLGSgEIYVGDRQVTKmkEYERSRFIGRVFQDPSMGTCpslTVLENMALADNk 109
Cdd:cd03240 24 LTLIVGQNGAGKTTIIEAlkyaLTGELPPNS-KGGAHDPKLIR--EGEVRAQVKLAFENANGKKY---TITRSLAILEN- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 110 gSSFLLQrgvnrrrtqhyrEELSLLhmgLEDklgvQVGSLSGGQ--------RQALAMLIatMSPINLLILDEHTAALDP 181
Cdd:cd03240 97 -VIFCHQ------------GESNWP---LLD----MRGRCSGGEkvlasliiRLALAETF--GSNCGILALDEPTTNLDE 154
|
170 180
....*....|....*....|....*..
gi 1852789824 182 HSSENVM-ELTQRVAKEKHVTMLMVTH 207
Cdd:cd03240 155 ENIEESLaEIIEERKSQKNFQLIVITH 181
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
2-67 |
7.96e-06 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 46.65 E-value: 7.96e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 2 VRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGD 67
Cdd:PRK11819 325 IEAENLSKSFG-----DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
19-243 |
9.51e-06 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 46.56 E-value: 9.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 19 VVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQ----VTKMKEYErsrfiGRVFQDPSMGTC 94
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRFYDLKNDHHIVFKNEhtndMTNEQDYQ-----GDEEQNVGMKNV 1255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTVLENMALADN----KGSSFLLQRGVN---------RRRTQHYREELSLLHM--------GLED------------- 140
Cdd:PTZ00265 1256 NEFSLTKEGGSGEDstvfKNSGKILLDGVDicdynlkdlRNLFSIVSQEPMLFNMsiyenikfGKEDatredvkrackfa 1335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 141 -----------KLGVQVG----SLSGGQRQALAMLIATMSPINLLILDEHTAALDPhSSENVMELTQRVAKEK-HVTMLM 204
Cdd:PTZ00265 1336 aidefieslpnKYDTNVGpygkSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIEKTIVDIKDKaDKTIIT 1414
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1852789824 205 VTHNLKfAVAYGDRLLMMH---RGHIMLDAAGEDKKVLDVRD 243
Cdd:PTZ00265 1415 IAHRIA-SIKRSDKIVVFNnpdRTGSFVQAHGTHEELLSVQD 1455
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
17-227 |
1.32e-05 |
|
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: 44.56 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLG---SGEIYVGDRQVTKMKEYERSRFIGRVFQDPSMgt 93
Cdd:cd03233 18 SKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF-- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 94 cPSLTVLENMALADN-KGSSFLlqRGVnrrrtqhyreelsllhmgledklgvqvgslSGGQRQALAMLIATMSPINLLIL 172
Cdd:cd03233 96 -PTLTVRETLDFALRcKGNEFV--RGI------------------------------SGGERKRVSIAEALVSRASVLCW 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 173 DEHTAALDPHSSENVMELTQRVAKEKHVTMLM-VTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:cd03233 143 DNSTRGLDSSTALEILKCIRTMADVLKTTTFVsLYQASDEIYDLFDKVLVLYEGRQ 198
|
|
| 3a01203 |
TIGR00954 |
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ... |
17-207 |
1.83e-05 |
|
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 45.51 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 17 NEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRqvtkmkeyersrfiGRVF---QDPSMGT 93
Cdd:TIGR00954 463 NGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK--------------GKLFyvpQRPYMTL 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 94 CpslTVLENMALADNKGSSFllQRGVNRRRTQHYREELSLLHMgLEDKLG---VQVGS--LSGGQRQALAMLIATMSPIN 168
Cdd:TIGR00954 529 G---TLRDQIIYPDSSEDMK--RRGLSDKDLEQILDNVQLTHI-LEREGGwsaVQDWMdvLSGGEKQRIAMARLFYHKPQ 602
|
170 180 190
....*....|....*....|....*....|....*....
gi 1852789824 169 LLILDEHTAALDPHSSENVMELtqrvAKEKHVTMLMVTH 207
Cdd:TIGR00954 603 FAILDECTSAVSVDVEGYMYRL----CREFGITLFSVSH 637
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
15-180 |
2.74e-05 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 43.71 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFqDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKM-KEYerSRFIGRvfqdpSMGT 93
Cdd:PRK13541 10 NIEQKNLF-DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIaKPY--CTYIGH-----NLGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 94 CPSLTVLENMAL-ADNKGSSFLLQRGVnrrrtqHYreelsllhMGLEDKLGVQVGSLSGGQRQ--ALAMLIATMSpiNLL 170
Cdd:PRK13541 82 KLEMTVFENLKFwSEIYNSAETLYAAI------HY--------FKLHDLLDEKCYSLSSGMQKivAIARLIACQS--DLW 145
|
170
....*....|
gi 1852789824 171 ILDEHTAALD 180
Cdd:PRK13541 146 LLDEVETNLS 155
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
27-212 |
4.56e-05 |
|
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: 42.73 E-value: 4.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 27 LQIAEGSFVAVVGSNGSGKTTILNLLCgslpLGsgeiyVGDRQVTKMKEYersrfigrVFQDPSMGTCPSLTVLenmala 106
Cdd:cd03227 16 VTFGEGSLTIITGPNGSGKSTILDAIG----LA-----LGGAQSATRRRS--------GVKAGCIVAAVSAELI------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 107 dnkgsSFLLQrgvnrrrtqhyreelsllhmgledklgvqvgsLSGGQRQ----ALAMLIATMSPINLLILDEHTAALDPH 182
Cdd:cd03227 73 -----FTRLQ--------------------------------LSGGEKElsalALILALASLKPRPLYILDEIDRGLDPR 115
|
170 180 190
....*....|....*....|....*....|
gi 1852789824 183 SSENVMELTQRVAKEKHvTMLMVTHNLKFA 212
Cdd:cd03227 116 DGQALAEAILEHLVKGA-QVIVITHLPELA 144
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-228 |
5.03e-05 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 44.08 E-value: 5.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 18 EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERS---RFIGRVFQDPSMGTC 94
Cdd:PRK10261 336 EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQalrRDIQFIFQDPYASLD 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTV-------LENMALADNKGS----SFLLQR-GVNRRRTQHYREElsllhmgledklgvqvgsLSGGQRQALAMLIA 162
Cdd:PRK10261 416 PRQTVgdsimepLRVHGLLPGKAAaarvAWLLERvGLLPEHAWRYPHE------------------FSGGQRQRICIARA 477
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1852789824 163 TMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIM 228
Cdd:PRK10261 478 LALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIV 543
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
97-209 |
6.71e-05 |
|
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.
Pssm-ID: 433102 [Multi-domain] Cd Length: 303 Bit Score: 43.15 E-value: 6.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 97 LTVLENMALADNKGSSFLLQRGVNRRRTQHYREELSLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPIN---LLILD 173
Cdd:pfam13304 185 LQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALLSALPkggLLLID 264
|
90 100 110
....*....|....*....|....*....|....*.
gi 1852789824 174 EHTAALDPHSSENVMELTqRVAKEKHVTMLMVTHNL 209
Cdd:pfam13304 265 EPESGLHPKLLRRLLELL-KELSRNGAQLILTTHSP 299
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
5-210 |
7.55e-05 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 42.88 E-value: 7.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 5 EHIYKTFNPGSVNEVVL-FQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEI-YVGDRQVTKMkeyersrfi 82
Cdd:PRK13546 22 ERMKDALIPKHKNKTFFaLDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVdRNGEVSVIAI--------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 83 grvfqdpSMGTCPSLTVLENMALAdnkgssfLLQRGVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIA 162
Cdd:PRK13546 93 -------SAGLSGQLTGIENIEFK-------MLCMGFKRKEIKAMTPKI-IEFSELGEFIYQPVKKYSSGMRAKLGFSIN 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1852789824 163 TMSPINLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLK 210
Cdd:PRK13546 158 ITVNPDILVIDEALSVGDQTFAQKCLDKIYEF-KEQNKTIFFVSHNLG 204
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
21-180 |
9.70e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 43.40 E-value: 9.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 21 LFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIyvgdrqvtkmkEYERSRFIGRVFQDPS---------- 90
Cdd:PRK11147 18 LLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRI-----------IYEQDLIVARLQQDPPrnvegtvydf 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 91 ---------------------MGTCPSLTVLENMALADNKGSSFLLQRGVNRrrtqhYREELSLLHMGLEDKLgvqvGSL 149
Cdd:PRK11147 87 vaegieeqaeylkryhdishlVETDPSEKNLNELAKLQEQLDHHNLWQLENR-----INEVLAQLGLDPDAAL----SSL 157
|
170 180 190
....*....|....*....|....*....|..
gi 1852789824 150 SGG-QRQAlAMLIATMSPINLLILDEHTAALD 180
Cdd:PRK11147 158 SGGwLRKA-ALGRALVSNPDVLLLDEPTNHLD 188
|
|
| ABC_SMC_barmotin |
cd03278 |
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ... |
31-225 |
1.06e-04 |
|
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: 42.07 E-value: 1.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 31 EGSFVAVVGSNGSGKTTILNLLCGSLplgsGEiyvgdrqvTKMKEYERSRFIGRVF----QDPSMGTCP-SLTvLENmal 105
Cdd:cd03278 21 PPGLTAIVGPNGSGKSNIIDAIRWVL----GE--------QSAKSLRGEKMSDVIFagseTRKPANFAEvTLT-FDN--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 106 aDNKGSSFLLQRGVNRrrtqhyreelsLLHMGleDKLGVQVGSLSGGQRQ--ALAMLIAT--MSPINLLILDEHTAALDP 181
Cdd:cd03278 85 -SDGRYSIISQGDVSE-----------IIEAP--GKKVQRLSLLSGGEKAltALALLFAIfrVRPSPFCVLDEVDAALDD 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1852789824 182 HSSENVMELTQRVAKEkhVTMLMVTHNlKFAVAYGDRLL---MMHRG 225
Cdd:cd03278 151 ANVERFARLLKEFSKE--TQFIVITHR-KGTMEAADRLYgvtMQESG 194
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
18-237 |
1.59e-04 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 42.41 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 18 EVVLFQDFNLQIAEGSFVAVVGSNGSGKTTilnllcGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRVF---QDPSMGTC 94
Cdd:NF000106 25 EVKAVDGVDLDVREGTVLGVLGP*GAA**R------GALPAHV*GPDAGRRPWRF*TWCANRRALRRTIg*hRPVR*GRR 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 95 PSLTVLENMALAdnkGSSFLLQRGVNRRRTQHYREELSLlhmglEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDE 174
Cdd:NF000106 99 ESFSGRENLYMI---GR*LDLSRKDARARADELLERFSL-----TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1852789824 175 HTAALDPHSSENVMELTQRVAKEKhVTMLMVTHNLKFAVAYGDRLLMMHRGHIMLDAAGEDKK 237
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDG-ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
132-228 |
1.78e-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: 41.15 E-value: 1.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 132 SLLHMGLED-KLGVQVGSLSGG--QRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHN 208
Cdd:cd03238 70 FLIDVGLGYlTLGQKLSTLSGGelQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHN 148
|
90 100
....*....|....*....|....*.
gi 1852789824 209 LKFaVAYGDRLLMM------HRGHIM 228
Cdd:cd03238 149 LDV-LSSADWIIDFgpgsgkSGGKVV 173
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
24-227 |
1.84e-04 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 42.22 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 24 DFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPlG--SGEIYVGDRQVTKMKEYERSRF-IGRVFQD-PSMGTCPSLTV 99
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYP-GrwEGEIFIDGKPVKIRNPQQAIAQgIAMVPEDrKRDGIVPVMGV 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 100 LENMALAdnkgssfLLQRGVNRRRTQHYREELSLLHMglEDKLGVQ-------VGSLSGG--QRQALA-MLIAtmSPiNL 169
Cdd:PRK13549 359 GKNITLA-------ALDRFTGGSRIDDAAELKTILES--IQRLKVKtaspelaIARLSGGnqQKAVLAkCLLL--NP-KI 426
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1852789824 170 LILDEHTAALDPHSSENVMELTQRVAKEkHVTMLMVTHNLKFAVAYGDRLLMMHRGHI 227
Cdd:PRK13549 427 LILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
15-207 |
2.27e-04 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 41.32 E-value: 2.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 15 SVNEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGS--LPLGSGEIYVGDRQVTKMKEYERS-RFIGRVFQDPSm 91
Cdd:PRK09580 10 SVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgEGIFMAFQYPV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 92 gTCPSLTvlenmaladnkgSSFLLQRGVNRRRtqHYR---------------EELSLLHMGlEDKL--GVQVGsLSGGQR 154
Cdd:PRK09580 89 -EIPGVS------------NQFFLQTALNAVR--SYRgqepldrfdfqdlmeEKIALLKMP-EDLLtrSVNVG-FSGGEK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 155 QALAML-IATMSPiNLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTH 207
Cdd:PRK09580 152 KRNDILqMAVLEP-ELCILDESDSGLDIDALKIVADGVNSLRDGKR-SFIIVTH 203
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
20-64 |
2.33e-04 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 42.15 E-value: 2.33e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1852789824 20 VLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIY 64
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF 567
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
32-224 |
2.87e-04 |
|
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: 40.05 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 32 GSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYERSRFIGRvfqdpsmgtcpsltvlenmaladnkgs 111
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYIDGEDILEEVLDQLLLIIV--------------------------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 112 sfllqrgvnrrrtqhyreelsllhmgledklGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELT 191
Cdd:smart00382 55 -------------------------------GGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLE 103
|
170 180 190
....*....|....*....|....*....|....*...
gi 1852789824 192 Q-----RVAKEKHVTMLMVTHNLKFAvaygDRLLMMHR 224
Cdd:smart00382 104 ElrlllLLKSEKNLTVILTTNDEKDL----GPALLRRR 137
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
1-179 |
4.32e-04 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 41.14 E-value: 4.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFnPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEI-YVGDRQVTKMKEYERS 79
Cdd:PRK10762 4 LLQLKGIDKAF-PG----VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVTFNGPKSSQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 80 RFIGRVFQDpsMGTCPSLTVLENMALADNKGSSFllqRGVNRRRTqhYREELSLLHmgledKLGVQ------VGSLSGGQ 153
Cdd:PRK10762 79 AGIGIIHQE--LNLIPQLTIAENIFLGREFVNRF---GRIDWKKM--YAEADKLLA-----RLNLRfssdklVGELSIGE 146
|
170 180
....*....|....*....|....*.
gi 1852789824 154 RQALAMLIATMSPINLLILDEHTAAL 179
Cdd:PRK10762 147 QQMVEIAKVLSFESKVIIMDEPTDAL 172
|
|
| AAA_23 |
pfam13476 |
AAA domain; |
22-56 |
8.95e-04 |
|
AAA domain;
Pssm-ID: 463890 [Multi-domain] Cd Length: 190 Bit Score: 39.40 E-value: 8.95e-04
10 20 30
....*....|....*....|....*....|....*
gi 1852789824 22 FQDFNLQIAEGSFVaVVGSNGSGKTTILNLLCGSL 56
Cdd:pfam13476 9 FRDQTIDFSKGLTL-ITGPNGSGKTTILDAIKLAL 42
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
1-180 |
1.15e-03 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.77 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 1 MVRMEHIYKTFNpgsvnEVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEI---------YVGDRQVt 71
Cdd:PRK10636 312 LLKMEKVSAGYG-----DRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIglakgiklgYFAQHQL- 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 72 kmkEYERSrfigrvfqDPSmgtcpsltVLENMAladnkgssfllqRGVNRRRTQHYREELSllHMGLE-DKLGVQVGSLS 150
Cdd:PRK10636 386 ---EFLRA--------DES--------PLQHLA------------RLAPQELEQKLRDYLG--GFGFQgDKVTEETRRFS 432
|
170 180 190
....*....|....*....|....*....|.
gi 1852789824 151 GGQRQALAM-LIATMSPiNLLILDEHTAALD 180
Cdd:PRK10636 433 GGEKARLVLaLIVWQRP-NLLLLDEPTNHLD 462
|
|
| ABC_SMC_head |
cd03239 |
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural ... |
33-196 |
1.21e-03 |
|
The SMC head domain belongs to the ATP-binding cassette superfamily; The structural maintenance of chromosomes (SMC) proteins are essential for successful chromosome transmission during replication and segregation of the genome in all organisms. SMCs are generally present as single proteins in bacteria, and as at least six distinct proteins in eukaryotes. The proteins range in size from approximately 110 to 170 kDa, and each has five distinct domains: amino- and carboxy-terminal globular domains, which contain sequences characteristic of ATPases, two coiled-coil regions separating the terminal domains , and a central flexible hinge. SMC proteins function together with other proteins in a range of chromosomal transactions, including chromosome condensation, sister-chromatid cohesion, recombination, DNA repair, and epigenetic silencing of gene expression.
Pssm-ID: 213206 [Multi-domain] Cd Length: 178 Bit Score: 38.83 E-value: 1.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 33 SFVAVVGSNGSGKTTILNLLCgslplgsgeiyvgdrqvtkmkeyersrfigrvfqdpsmgtcpslTVLENMALADNKGSS 112
Cdd:cd03239 23 SFNAIVGPNGSGKSNIVDAIC--------------------------------------------FVLGGKAAKLRRGSL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 113 FLLQRGVNRRRTQ------HYREELSLLHMGLEDKLgvqvgsLSGGQRQ--ALAMLIATMS--PINLLILDEHTAALDPH 182
Cdd:cd03239 59 LFLAGGGVKAGINsasveiTFDKSYFLVLQGKVEQI------LSGGEKSlsALALIFALQEikPSPFYVLDEIDAALDPT 132
|
170
....*....|....
gi 1852789824 183 SSENVMELTQRVAK 196
Cdd:cd03239 133 NRRRVSDMIKEMAK 146
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
30-209 |
1.24e-03 |
|
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: 39.27 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 30 AEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVTKMKEYeRSRFIGRVFQDPSMGTCPSLTVLENMALADN- 108
Cdd:cd03236 24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPDWDEILDEF-RGSELQNYFTKLLEGDVKVIVKPQYVDLIPKa 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 109 -KGSSFLLqrgVNRRRTQHYREELsLLHMGLEDKLGVQVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSENV 187
Cdd:cd03236 103 vKGKVGEL---LKKKDERGKLDEL-VDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNA 178
|
170 180
....*....|....*....|..
gi 1852789824 188 MELTQRVAKEKHvTMLMVTHNL 209
Cdd:cd03236 179 ARLIRELAEDDN-YVLVVEHDL 199
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
4-250 |
1.45e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 39.71 E-value: 1.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 4 MEHIYKTFnPGsvneVVLFQDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGSLPLGSGEIYVGDRQVT-KMKEYERSRFI 82
Cdd:PRK10982 1 MSNISKSF-PG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 83 GRVFQDpsMGTCPSLTVLENMALADNKGSSFLLQRGVNRRRTQHYREELsllhmGLEDKLGVQVGSLSGGQRQALAMLIA 162
Cdd:PRK10982 76 SMVHQE--LNLVLQRSVMDNMWLGRYPTKGMFVDQDKMYRDTKAIFDEL-----DIDIDPRAKVATLSVSQMQMIEIAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 163 TMSPINLLILDEHTAALDPHSSENVMELTQRVaKEKHVTMLMVTHNLKFAVAYGDRLLMMHRGHIMldaAGEDKKVLDV- 241
Cdd:PRK10982 149 FSYNAKIVIMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI---ATQPLAGLTMd 224
|
250
....*....|....*..
gi 1852789824 242 --------RDLTNRFDE 250
Cdd:PRK10982 225 kiiammvgRSLTQRFPD 241
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
145-219 |
3.14e-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: 37.55 E-value: 3.14e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1852789824 145 QVGSLSGGQRQALAMLIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHVTMLMVTHNLKFAVAYGDRL 219
Cdd:cd03222 68 QYIDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRI 142
|
|
| PRK00635 |
PRK00635 |
excinuclease ABC subunit A; Provisional |
142-209 |
3.38e-03 |
|
excinuclease ABC subunit A; Provisional
Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 38.66 E-value: 3.38e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1852789824 142 LGVQVGSLSGGQRQALAMLIATMSPI---NLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNL 209
Cdd:PRK00635 803 LGRPLSSLSGGEIQRLKLAYELLAPSkkpTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH-TVVIIEHNM 872
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
149-208 |
4.99e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 38.11 E-value: 4.99e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1852789824 149 LSGGQRQ--ALAMLIATM--SPINLLILDEHTAALDPHSSENVMELTQRVAkeKHVTMLMVTHN 208
Cdd:TIGR02168 1090 LSGGEKAltALALLFAIFkvKPAPFCILDEVDAPLDDANVERFANLLKEFS--KNTQFIVITHN 1151
|
|
| ABC_SMC2_euk |
cd03273 |
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ... |
149-193 |
5.29e-03 |
|
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).
Pssm-ID: 213240 [Multi-domain] Cd Length: 251 Bit Score: 37.28 E-value: 5.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1852789824 149 LSGGQRQALAM-LIATM---SPINLLILDEHTAALDPHSSENVMELTQR 193
Cdd:cd03273 167 LSGGQRSLVALsLILALllfKPAPMYILDEVDAALDLSHTQNIGRMIKT 215
|
|
| ABC_UvrA_II |
cd03271 |
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ... |
23-209 |
6.88e-03 |
|
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins and UvrB having one ATP binding site that is structurally related to that of helicases.
Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 36.82 E-value: 6.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 23 QDFNLQIAEGSFVAVVGSNGSGKTTILNLLCGslPLGSGEIYVGDRQVTKMKEYERSRFIGRVF---QDPSMGT------ 93
Cdd:cd03271 12 KNIDVDIPLGVLTCVTGVSGSGKSSLINDTLY--PALARRLHLKKEQPGNHDRIEGLEHIDKVIvidQSPIGRTprsnpa 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 94 -------------CPS----------LTVL-ENMALAD------NKGSSFLLQRGVNRRRTQhyreelSLLHMGLED-KL 142
Cdd:cd03271 90 tytgvfdeirelfCEVckgkrynretLEVRyKGKSIADvldmtvEEALEFFENIPKIARKLQ------TLCDVGLGYiKL 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 143 GVQVGSLSGG--QRQALAMLIATMSPIN-LLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHNL 209
Cdd:cd03271 164 GQPATTLSGGeaQRIKLAKELSKRSTGKtLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNL 232
|
|
| uvra |
TIGR00630 |
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ... |
133-209 |
7.44e-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: 7.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1852789824 133 LLHMGLED-KLGVQVGSLSGG--QRQALAM-LIATMSPINLLILDEHTAALDPHSSENVMELTQRVAKEKHvTMLMVTHN 208
Cdd:TIGR00630 813 LCDVGLGYiRLGQPATTLSGGeaQRIKLAKeLSKRSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHN 891
|
.
gi 1852789824 209 L 209
Cdd:TIGR00630 892 L 892
|
|
| |
