|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-242 |
4.58e-95 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 278.10 E-value: 4.58e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPE 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 163 GLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQqtglhkQTLDDIYIHVTQGG 242
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKA------RLLEDVFLELTGEE 234
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-237 |
4.15e-74 |
|
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: 225.12 E-value: 4.15e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPES 83
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 PVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLG 163
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 164 LDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTGlhKQTLDDIYIH 237
Cdd:COG4555 163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIG--EENLEDAFVA 234
|
|
| ABC_DR_subfamily_A |
cd03230 |
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ... |
3-211 |
6.60e-73 |
|
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: 219.58 E-value: 6.60e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPE 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEmtamaydidrdeamnrampllktfrlenelkvfpshFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446139018 163 GLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-228 |
1.63e-58 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 187.24 E-value: 1.63e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIeayRRKLSYIP 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLE-------NELkvfpshfSKGMKQKVMIICAFIVNPEL 154
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGdrankkvEEL-------SKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 155 YIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTGLHK 228
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQFGRNT 224
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-212 |
8.81e-57 |
|
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: 180.11 E-value: 8.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIpE 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALI-E 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRdeamNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446139018 163 GLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-225 |
1.69e-53 |
|
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]
Pssm-ID: 130256 [Multi-domain] Cd Length: 302 Bit Score: 174.50 E-value: 1.69e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPESPVIYEELT 91
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQS 171
Cdd:TIGR01188 83 GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 172 MLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTG 225
Cdd:TIGR01188 163 IWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKRRLG 216
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-228 |
5.44e-52 |
|
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: 168.28 E-value: 5.44e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYI 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKkNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 ---PE----SPVIYEEltleehIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:COG1122 81 fqnPDdqlfAPTVEED------VAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGD-LEALRQQTGLHK 228
Cdd:COG1122 155 VLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTpREVFSDYELLEE 230
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-215 |
8.10e-52 |
|
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: 167.46 E-value: 8.10e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIeayRRKLSYIPE 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA---RNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 163 GLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-191 |
1.06e-48 |
|
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: 159.18 E-value: 1.06e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYI 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYDIDRDEAmnRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 446139018 161 FLGLDPLGIQSMLDLMVEKKNEGRTVLMSTH 191
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
9-215 |
4.91e-48 |
|
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: 158.05 E-value: 4.91e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 9 TGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKhML-GLLTPMEGSLSISDININDDIEAYRRKLSYIPESPVIY 87
Cdd:cd03263 9 TYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLK-MLtGELRPTSGTAYINGYSIRTDRKAARQSLGYCPQFDALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 EELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPL 167
Cdd:cd03263 88 DELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446139018 168 GIQSMLDLMVEKKnEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03263 168 SRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-210 |
5.41e-48 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 157.63 E-value: 5.41e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGY--GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYI 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 ---PESPVIyeELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:cd03225 81 fqnPDDQFF--GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGE 210
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-220 |
2.45e-45 |
|
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: 158.53 E-value: 2.45e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKR-----PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIEAY 73
Cdd:COG1123 261 LEVRNLSKRYPVRgkggvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKlsrrSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 74 RRKLSYIPESPV--IYEELTLEEHIEMTAMAYDI-DRDEAMNRAMPLLKTFRLENELK-VFPSHFSKGMKQKVMIICAFI 149
Cdd:COG1123 341 RRRVQMVFQDPYssLNPRMTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLPPDLAdRYPHELSGGQRQRVAIARALA 420
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 150 VNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:COG1123 421 LEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-220 |
5.63e-45 |
|
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: 157.37 E-value: 5.63e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MT--VKVEQLTGGY--GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP---MEGSLSISDININDDIEAY 73
Cdd:COG1123 1 MTplLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHggrISGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 74 R-RKLSYIPESP-VIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVN 151
Cdd:COG1123 81 RgRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 152 PELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEI 230
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-221 |
1.42e-44 |
|
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: 149.06 E-value: 1.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPE 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 163 GLDP---LGIQSMLDLMveKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALR 221
Cdd:cd03265 161 GLDPqtrAHVWEYIEKL--KEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-215 |
3.61e-44 |
|
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: 147.90 E-value: 3.61e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYG--KRPV--IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLS 78
Cdd:cd03266 2 ITADALTKRFRdvKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 159 EPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-210 |
8.72e-44 |
|
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 145.08 E-value: 8.72e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPE 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 spviyeeltleehiemtamaydidrdeamnrampllktfrlenelkvfpshFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd00267 81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446139018 163 GLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGE 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-235 |
1.49e-43 |
|
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];
Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 147.50 E-value: 1.49e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIP 81
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlSRRELARRIAYVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPVIYEELTLEEHIEM------TAMAYDIDRDEAM-NRAMPLLKTFRLE----NELkvfpshfSKGMKQKVMIICAFIV 150
Cdd:COG1120 82 QEPPAPFGLTVRELVALgryphlGLFGRPSAEDREAvEEALERTGLEHLAdrpvDEL-------SGGERQRVLIARALAQ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 151 NPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALrqqtgLHKQ 229
Cdd:COG1120 155 EPPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV-----LTPE 229
|
....*.
gi 446139018 230 TLDDIY 235
Cdd:COG1120 230 LLEEVY 235
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-228 |
6.80e-43 |
|
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.62 E-value: 6.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininDDIEAYRRKLSYIPE 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEE--LTLEEHIEMTAMAY--------DIDRDEAMNrampLLKTFRLE-------NELkvfpshfSKGMKQKVMII 145
Cdd:COG1121 83 RAEVDWDfpITVRDVVLMGRYGRrglfrrpsRADREAVDE----ALERVGLEdladrpiGEL-------SGGQQQRVLLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 146 CAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDeGEVVAFGDLEALRQQTG 225
Cdd:COG1121 152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLN-RGLVAHGPPEEVLTPEN 230
|
...
gi 446139018 226 LHK 228
Cdd:COG1121 231 LSR 233
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-215 |
5.37e-42 |
|
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: 142.29 E-value: 5.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDieayRRKLSYIPES 83
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 PVIYEE--LTLEEHIEMTAMAY----DIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:cd03235 77 RSIDRDfpISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDeGEVVAFG 215
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
8.15e-42 |
|
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: 142.19 E-value: 8.15e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSlsisdININD-DIEAY------RRK 76
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGS-----IRFDGrDITGLppheraRAG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 77 LSYIPESPVIYEELTLEEHIEMTAMAYDIDRDEAmnrampllktfRLENELKVFP----------SHFSKGMKQKVMIIC 146
Cdd:cd03224 77 IGYVPEGRRIFPELTVEENLLLGAYARRRAKRKA-----------RLERVYELFPrlkerrkqlaGTLSGGEQQMLAIAR 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 147 AFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQ 222
Cdd:cd03224 146 ALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-215 |
1.02e-41 |
|
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: 141.87 E-value: 1.02e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLT----GGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIEAYR 74
Cdd:cd03257 2 LEVKNLSvsfpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 75 RKLSYIPESPviYEEL----TLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKV---FPSHFSKGMKQKVMIICA 147
Cdd:cd03257 82 KEIQMVFQDP--MSSLnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEEVlnrYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 148 FIVNPELYIIDEPFLGLDPLgIQS-MLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03257 160 LALNPKLLIADEPTSALDVS-VQAqILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-222 |
1.38e-41 |
|
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440744 [Multi-domain] Cd Length: 241 Bit Score: 142.04 E-value: 1.38e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ----DDIEAYRRKLS 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITglseKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHI-----EMTamayDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:COG1127 86 MLFQGGALFDSLTVFENVafplrEHT----DLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDPE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQ 222
Cdd:COG1127 162 ILLYDEPTAGLDPITSAVIDELIRElRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-215 |
3.18e-40 |
|
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: 136.41 E-value: 3.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPE 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SpviyeeltleehIEMTAMAYDIDRDeamnrampllktFrleNELkvfpshfSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03214 81 A------------LELLGLAHLADRP------------F---NEL-------SGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 163 GLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03214 127 HLDIAHQIELLELLRRlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-215 |
3.38e-40 |
|
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: 137.71 E-value: 3.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGeIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPE 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 163 GLDPLGIQSMLDLMVEkKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03264 160 GLDPEERIRFRNLLSE-LGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
1-223 |
3.53e-40 |
|
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein family are exclusive to the Bacteroidetes phylum (previously Cytophaga-Flavobacteria-Bacteroides). GldA is an ABC transporter ATP-binding protein (pfam00005) linked to a type of rapid surface gliding motility found in certain Bacteroidetes, such as Flavobacterium johnsoniae and Cytophaga hutchinsonii. Knockouts of GldA abolish the gliding phenotype. Gliding motility appears closely linked to chitin utilization in the model species Flavobacterium johnsoniae. Bacteroidetes with members of this protein family appear to have all of the genes associated with gliding motility.
Pssm-ID: 132561 [Multi-domain] Cd Length: 301 Bit Score: 140.29 E-value: 3.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYI 80
Cdd:TIGR03522 1 MSIRVSSLTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:TIGR03522 81 PEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 161 FLGLDPLGIQSMLDLMvekKNEG--RTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQ 223
Cdd:TIGR03522 161 TTGLDPNQLVEIRNVI---KNIGkdKTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAA 222
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-222 |
1.35e-39 |
|
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: 136.86 E-value: 1.35e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEA----YRRKLS 78
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAelyrLRRRMG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHI-----EMTAMaydiDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:cd03261 81 MLFQSGALFDSLTVFENVafplrEHTRL----SEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQ 222
Cdd:cd03261 157 LLLYDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-210 |
4.60e-39 |
|
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: 133.47 E-value: 4.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD---DIEAYRRKLSY 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEELTLEEhiemtamaydidrdeamNRAMPLlktfrlenelkvfpshfSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLE-----------------NIALGL-----------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446139018 160 PFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGE 210
Cdd:cd03229 127 PTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-239 |
7.58e-39 |
|
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.
Pssm-ID: 163452 [Multi-domain] Cd Length: 223 Bit Score: 134.45 E-value: 7.58e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIsdininDDIEAYRRKLSYIP-- 81
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIF------DGHPWTRKDLHKIGsl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 -ESPVIYEELTLEEHIEMTAMAYDIDRdeamNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:TIGR03740 76 iESPPLYENLTARENLKVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 161 FLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEvvafgdleaLRQQTGLHK-QTLDDIYIHVT 239
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGV---------LGYQGKINKsENLEKLFVEVV 222
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-235 |
2.25e-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: 133.85 E-value: 2.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYG-KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIEAYRRKLS 78
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkALRQLRRQIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHIEMTAMAY------------DIDRdeamNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIIC 146
Cdd:cd03256 82 MIFQQFNLIERLSVLENVLSGRLGRrstwrslfglfpKEEK----QRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 147 AFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEK-KNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQqtg 225
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTD--- 234
|
250
....*....|
gi 446139018 226 lhkQTLDDIY 235
Cdd:cd03256 235 ---EVLDEIY 241
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-161 |
3.65e-38 |
|
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: 130.46 E-value: 3.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ-DDIEAYRRKLSYIPESPVIYEELTLEEHI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 97 EMTAMAYDIDRDEAMNRAMPLLKTFRLENELK----VFPSHFSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-221 |
1.45e-37 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid transport and metabolism];
Pssm-ID: 440179 [Multi-domain] Cd Length: 236 Bit Score: 131.26 E-value: 1.45e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINInDDIEAY---RRKLSYI 80
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDI-TGLPPHriaRLGIGYV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAM-----PLLKTFR--LENELkvfpshfSKGMKQKVMIICAFIVNPE 153
Cdd:COG0410 84 PEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERvyelfPRLKERRrqRAGTL-------SGGEQQMLAIGRALMSRPK 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALR 221
Cdd:COG0410 157 LLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELL 224
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
3-220 |
1.75e-37 |
|
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: 131.13 E-value: 1.75e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGslsisDININD-DIEAY------RR 75
Cdd:cd03218 1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSG-----KILLDGqDITKLpmhkraRL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 76 KLSYIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELY 155
Cdd:cd03218 76 GIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFL 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 156 IIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTH----ILATaeryCDRFIILDEGEVVAFGDLEAL 220
Cdd:cd03218 156 LLDEPFAGVDPIAVQDIQKIIKILKDRGIGVLITDHnvreTLSI----TDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-215 |
2.91e-37 |
|
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: 129.95 E-value: 2.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDdIEAYRRKLSYIPE 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTG-VPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIemtamAY-----DIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:cd03259 80 DYALFPHLTVAENI-----AFglklrGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03259 155 DEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-211 |
1.83e-36 |
|
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: 127.99 E-value: 1.83e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLT----GGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ----DDIEAYR 74
Cdd:cd03255 1 IELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklseKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 75 RK-LSYIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:cd03255 81 RRhIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILaTAERYCDRFIILDEGEV 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-225 |
2.45e-36 |
|
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: 134.50 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIEMTAMAYDidrDEAMNRAmplLKTFRLENELKVFP-----------SHFSKGMKQKVMIICAF 148
Cdd:COG4988 416 VPQNPYLFAG-TIRENLRLGRPDAS---DEELEAA---LEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARAL 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 149 IVNPELYIIDEPFLGLDPLG----IQSMLDLMvekknEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQT 224
Cdd:COG4988 489 LRDAPLLLLDEPTAHLDAETeaeiLQALRRLA-----KGRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAKN 562
|
.
gi 446139018 225 G 225
Cdd:COG4988 563 G 563
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-220 |
3.22e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 130.72 E-value: 3.22e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYI 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 161 FLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-229 |
5.78e-36 |
|
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: 134.58 E-value: 5.78e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKR--PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:COG2274 474 IELENVSFRYPGDspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIemTAMAYDIDrDEAMNRAmplLKTFRLENELKVFP-----------SHFSKGMKQKVMIICAF 148
Cdd:COG2274 554 VLQDVFLFSG-TIRENI--TLGDPDAT-DEEIIEA---ARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLAIARAL 626
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 149 IVNPELYIIDEPFLGLDPLG---IQSMLdlmvEKKNEGRTVLMSTHILATAeRYCDRFIILDEGEVVAFGDLEALRQQTG 225
Cdd:COG2274 627 LRNPRILILDEATSALDAETeaiILENL----RRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARKG 701
|
....
gi 446139018 226 LHKQ 229
Cdd:COG2274 702 LYAE 705
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-232 |
5.91e-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: 128.34 E-value: 5.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGK-----RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIEAY 73
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 74 RRKLSYI---PESPvIYEElTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELK-VFPSHFSKGMKQKVMIICAFI 149
Cdd:TIGR04521 81 RKKVGLVfqfPEHQ-LFEE-TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLeRSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 150 VNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGD-LEALRQQTGLH 227
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTpREVFSDVDELE 238
|
....*
gi 446139018 228 KQTLD 232
Cdd:TIGR04521 239 KIGLD 243
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-229 |
9.51e-36 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 129.05 E-value: 9.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSY--------IPESPVIyEE 89
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVvfgqrsqlWWDLPAI-DS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 90 LTLEEHIemtamaYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGI 169
Cdd:COG4586 117 FRLLKAI------YRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 170 QSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTGLHKQ 229
Cdd:COG4586 191 EAIREFLKEyNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKT 251
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-220 |
1.59e-35 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 128.00 E-value: 1.59e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPE 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 163 GLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-211 |
1.64e-35 |
|
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: 125.33 E-value: 1.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD---DIEAYRRKLSY 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDdkkNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEELTLEEHIEMTAM-AYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 159 EPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-212 |
1.10e-34 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 123.62 E-value: 1.10e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ----DDIEAYRRKL 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSrlkrREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:COG2884 82 GVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:COG2884 162 DEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-220 |
5.04e-34 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 122.45 E-value: 5.04e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININdDIEAYRRK---L 77
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDIT-HLPMHKRArlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVIYEELTLEEHI----EMTamayDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:COG1137 81 GYLPQEASIFRKLTVEDNIlavlELR----KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTH----ILATaeryCDRFIILDEGEVVAFGDLEAL 220
Cdd:COG1137 157 FILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHnvreTLGI----CDRAYIISEGKVLAEGTPEEI 223
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
16-215 |
9.96e-34 |
|
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: 121.67 E-value: 9.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYI--PESPVIYeELTLE 93
Cdd:cd03267 35 EALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfgQKTQLWW-DLPVI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 94 EHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLD---PLGIQ 170
Cdd:cd03267 114 DSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDvvaQENIR 193
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 446139018 171 SMLDLMVEKKneGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03267 194 NFLKEYNRER--GTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-235 |
2.21e-33 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 120.93 E-value: 2.21e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIEAYRRKL 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgrALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVIYEELTLeehIE---------------MTAMAYDIDRDEAMNrampLLKTFRLENELKVFPSHFSKGMKQKV 142
Cdd:COG3638 83 GMIFQQFNLVPRLSV---LTnvlagrlgrtstwrsLLGLFPPEDRERALE----ALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 143 MIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEK-KNEGRTVLMSTHILATAERYCDRFIILDEGEVVaFgDLEAlr 221
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVV-F-DGPP-- 231
|
250
....*....|....
gi 446139018 222 qqTGLHKQTLDDIY 235
Cdd:COG3638 232 --AELTDAVLREIY 243
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-210 |
3.06e-33 |
|
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: 118.25 E-value: 3.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYG--KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIemtamaydidrdeamnrampllktfrlenelkvfpshFSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 160 PFLGLDPLG----IQSMLDLMvekknEGRTVLMSTHILATAERyCDRFIILDEGE 210
Cdd:cd03228 123 ATSALDPETealiLEALRALA-----KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-237 |
2.49e-32 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 118.58 E-value: 2.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMlSSRQLARRLAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEELTLEEHIEMTAMAYD------IDRDEA-MNRAMPLLKTFRLENELKvfpSHFSKGMKQKVMIICAFIVNP 152
Cdd:PRK11231 81 LPQHHLTPEGITVRELVAYGRSPWLslwgrlSAEDNArVNQAMEQTRINHLADRRL---TDLSGGQRQRAFLAMVLAQDT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 153 ELYIIDEPFLGLDpLGIQ-SMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQtGLHKQTL 231
Cdd:PRK11231 158 PVVLLDEPTTYLD-INHQvELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP-GLLRTVF 235
|
....*..
gi 446139018 232 D-DIYIH 237
Cdd:PRK11231 236 DvEAEIH 242
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-206 |
3.55e-32 |
|
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: 117.19 E-value: 3.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKR----PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISdiniNDDIEAYRRKLS 78
Cdd:cd03293 1 LEVRNVSKTYGGGggavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVD----GEPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446139018 159 EPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIIL 206
Cdd:cd03293 157 EPFSALDALTREQLQEELLDiWRETGKTVLLVTHDIDEAVFLADRVVVL 205
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-215 |
6.85e-32 |
|
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding component of a bacterial solute transporter that serves a protective role to cells growing in a hyperosmolar environment. ABC (ATP-binding cassette) transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition, to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 117.02 E-value: 6.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGK-RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYI 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENE--LKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 159 EPFLGLDPLGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVG 218
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-224 |
6.20e-31 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 114.34 E-value: 6.20e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKhMLGLL-TPMEGSLSISDININ-------DDIEA 72
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLeTPDSGQLNIAGHQFDfsqkpseKAIRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 73 YRRKLSYIPESPVIYEELTLEEH-IEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVN 151
Cdd:COG4161 80 LRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 152 PELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQ-QT 224
Cdd:COG4161 160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDASHFTQpQT 233
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
10-215 |
1.13e-30 |
|
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: 113.40 E-value: 1.13e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 10 GGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIsdininddieayRRKLSYIPESPV-IYE 88
Cdd:cd03220 30 GEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTV------------RGRVSSLLGLGGgFNP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 89 ELTLEEHIEMTAMAYDIDRDEaMNRAMPLLKTFrleNELKVF---P-SHFSKGMKQKVMIICAFIVNPELYIIDEPFLGL 164
Cdd:cd03220 98 ELTGRENIYLNGRLLGLSRKE-IDEKIDEIIEF---SELGDFidlPvKTYSSGMKARLAFAIATALEPDILLIDEVLAVG 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446139018 165 DPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03220 174 DAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
8-220 |
1.63e-30 |
|
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: 113.06 E-value: 1.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 8 LTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI----NDDIEAYRRKLSYIPES 83
Cdd:cd03258 11 FGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLtllsGKELRKARRRIGMIFQH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 PVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLG 163
Cdd:cd03258 91 FNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSA 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 164 LDPLGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:cd03258 171 LDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-220 |
3.62e-30 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 112.29 E-value: 3.62e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininDDI------EAYRR 75
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDD----EDIsllplhARARR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 76 KLSYIPESPVIYEELTLEEHI-EMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPEL 154
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNLmAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKF 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 155 YIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-218 |
3.69e-30 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 112.48 E-value: 3.69e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 11 GYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSlsisdININDDIeayrrklsyipeSPVI---- 86
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGR-----VEVNGRV------------SALLelga 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 87 --YEELTLEEHIEMTAMAYDIDRDEaMNRAMPLLKTFrleNELKVF---P-SHFSKGMKQKVMIICAFIVNPELYIIDE- 159
Cdd:COG1134 98 gfHPELTGRENIYLNGRLLGLSRKE-IDEKFDEIVEF---AELGDFidqPvKTYSSGMRARLAFAVATAVDPDILLVDEv 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 160 ------PFLgldplgiQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:COG1134 174 lavgdaAFQ-------KKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
17-216 |
3.93e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 114.18 E-value: 3.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPESPVIYEEL------ 90
Cdd:PRK13631 41 ALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELITNPYSKKIKNFKELrrrvsm 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 91 ------------TLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENE-LKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:PRK13631 121 vfqfpeyqlfkdTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILAIQPEILIF 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGD 216
Cdd:PRK13631 201 DEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-229 |
6.39e-30 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 116.80 E-value: 6.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIemtamAY---DIDRDEAMnRAmplLKTFRLENELKVFP-----------SHFSKGMKQKVMII 145
Cdd:COG1132 419 VPQDTFLFSG-TIRENI-----RYgrpDATDEEVE-EA---AKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIA 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 146 CAFIVNPELYIIDEPFLGLDP---LGIQSMLD-LMvekknEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALR 221
Cdd:COG1132 489 RALLKDPPILILDEATSALDTeteALIQEALErLM-----KGRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEELL 562
|
....*...
gi 446139018 222 QQTGLHKQ 229
Cdd:COG1132 563 ARGGLYAR 570
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
17-222 |
6.71e-30 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 112.48 E-value: 6.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI---NDDIEAYRRKLSYIPESPviYEEL--- 90
Cdd:PRK13639 17 ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkydKKSLLEVRKTVGIVFQNP--DDQLfap 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 91 TLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQ 170
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 171 SMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA-------FGDLEALRQ 222
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKegtpkevFSDIETIRK 233
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-231 |
7.79e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 111.64 E-value: 7.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKhMLGLL-TPMEGSLSISDININ-------DDIEA 72
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLeMPRSGTLNIAGNHFDfsktpsdKAIRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 73 YRRKLSYIPESPVIYEELT-LEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVN 151
Cdd:PRK11124 80 LRRNVGMVFQQYNLWPHLTvQQNLIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMME 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 152 PELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQ-QTGLHKQT 230
Cdd:PRK11124 160 PQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASCFTQpQTEAFKNY 239
|
.
gi 446139018 231 L 231
Cdd:PRK11124 240 L 240
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-235 |
9.10e-30 |
|
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: 111.24 E-value: 9.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGK-RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIEAYRRKL 77
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVIYEELTLEEHIEMTAMAYD---------IDRDEAMnRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAF 148
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgrFSEEDKE-RALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 149 IVNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQqtglh 227
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRiNKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDD----- 235
|
....*...
gi 446139018 228 kQTLDDIY 235
Cdd:TIGR02315 236 -EVLRHIY 242
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
5-212 |
9.74e-30 |
|
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: 110.42 E-value: 9.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRP-VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDdiEAYRRKLSYIPES 83
Cdd:cd03226 2 IENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA--KERRKSIGYVMQD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 P--VIYEElTLEEHIEMTAMAYDidrdEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:cd03226 80 VdyQLFTD-SVREELLLGLKELD----AGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446139018 162 LGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:cd03226 155 SGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
15-215 |
1.03e-29 |
|
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: 117.04 E-value: 1.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPESPVIYEELTLEE 94
Cdd:TIGR01257 943 RPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAE 1022
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLD 174
Cdd:TIGR01257 1023 HILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWD 1102
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446139018 175 LMVeKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:TIGR01257 1103 LLL-KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-213 |
1.24e-29 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 111.33 E-value: 1.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLT----GGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininDDIEAYRRKLS 78
Cdd:COG1116 8 LELRGVSkrfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 159 EPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDE--GEVVA 213
Cdd:COG1116 164 EPFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.26e-29 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 112.49 E-value: 1.26e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKR-----PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEA--- 72
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlptelKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkek 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 73 ------------YRRKLSYIPE----SPVIYE-------ELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRL-ENELK 128
Cdd:PRK13651 81 ekvleklviqktRFKKIKKIKEirrrVGVVFQfaeyqlfEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 129 VFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDE 208
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKD 240
|
....*...
gi 446139018 209 GEVVAFGD 216
Cdd:PRK13651 241 GKIIKDGD 248
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
13-215 |
1.89e-29 |
|
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: 111.20 E-value: 1.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ-----DDIEAYRRKLSYIPESPVIY 87
Cdd:cd03294 35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAamsrkELRELRRKKISMVFQSFALL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 EELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPL 167
Cdd:cd03294 115 PHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446139018 168 GIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03294 195 IRREMQDELLRlQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVG 243
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-221 |
4.08e-29 |
|
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: 109.45 E-value: 4.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDdIEAYRRKLSYIPES 83
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITG-LPPHEIARLGIGRT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 ---PVIYEELTLEEHIEMTAMAYDI----------DRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIV 150
Cdd:cd03219 81 fqiPRLFPELTVLENVMVAAQARTGsglllararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 151 NPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALR 221
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVR 231
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
13-220 |
1.25e-28 |
|
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: 110.14 E-value: 1.25e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP---MEGSLSISDININD----DIEAYR-RKLSYIPES- 83
Cdd:COG0444 16 GVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELRKIRgREIQMIFQDp 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 -----PViyeeLTLEEHIEMTAMAY-DIDRDEAMNRAMPLLKTFRL---ENELKVFPSHFSKGMKQKVMIICAFIVNPEL 154
Cdd:COG0444 96 mtslnPV----MTVGDQIAEPLRIHgGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVMIARALALEPKL 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 155 YIIDEPFLGLDPLgIQ-SMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:COG0444 172 LIADEPTTALDVT-IQaQILNLLKDlQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-236 |
4.49e-28 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 112.14 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKSTTIKhML-GLLTPMEGSLSI--SDININdDIEAyRRKLSYIPESPVIYEELTLEEHI 96
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMK-MLtGLLPASEGEAWLfgQPVDAG-DIAT-RRRVGYMSQAFSLYGELTVRQNL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 97 EMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLM 176
Cdd:NF033858 361 ELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRLL 440
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 177 VE-KKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQTGlhKQTLDDIYI 236
Cdd:NF033858 441 IElSREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG--AATLEEAFI 498
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-229 |
6.16e-28 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 111.40 E-value: 6.16e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGY--GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLS 78
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEElTLEEHIemtAMAY-DIDrDEAMNRAmplLKTFRLENELKVFP-----------SHFSKGMKQKVMIIC 146
Cdd:COG4987 413 VVPQRPHLFDT-TLRENL---RLARpDAT-DEELWAA---LERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALAR 484
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 147 AFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEkKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQTGL 226
Cdd:COG4987 485 ALLRDAPILLLDEPTEGLDAATEQALLADLLE-ALAGRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQNGR 562
|
...
gi 446139018 227 HKQ 229
Cdd:COG4987 563 YRQ 565
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-225 |
8.50e-28 |
|
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213221 [Multi-domain] Cd Length: 229 Bit Score: 105.77 E-value: 8.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYI 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEElTLEEHIemtAMAYDIDRDEAMNRAMPLLK--TF--RLENELKVFPSH----FSKGMKQKVMIICAFIVNP 152
Cdd:cd03254 83 LQDTFLFSG-TIMENI---RLGRPNATDEEVIEAAKEAGahDFimKLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDP 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 153 ELYIIDEPFLGLDP---LGIQSMLdlmvEKKNEGRTVLMSTHILATAeRYCDRFIILDEGEVVAFGDLEALRQQTG 225
Cdd:cd03254 159 KILILDEATSNIDTeteKLIQEAL----EKLMKGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLAKKG 229
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-215 |
1.11e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 107.06 E-value: 1.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGK-----RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD---DIEA 72
Cdd:PRK13637 1 MSIKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDkkvKLSD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 73 YRRKLSYIPESP--VIYEElTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHF--SKGMKQKVMIICAF 148
Cdd:PRK13637 81 IRKKVGLVFQYPeyQLFEE-TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYEDYKDKSPFelSGGQKRRVAIAGVV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 149 IVNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKElHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQG 227
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-213 |
1.65e-27 |
|
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: 103.28 E-value: 1.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSI--SDININDDIEAYRRKLSYI 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVdgKEVSFASPRDARRAGIAMV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPViyeeltleehiemtamaydidrdeamnrampllktfrlenelkvfpshfskGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:cd03216 81 YQLSV---------------------------------------------------GERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 161 FLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
20-212 |
2.27e-27 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 106.07 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI-----NDDIEAYRRKLSYI---PESPvIYEELT 91
Cdd:PRK13641 25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNLKKLRKKVSLVfqfPEAQ-LFENTV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEhIEMTAMAYDIDRDEAMNRAMPLLKTFRLENEL-KVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQ 170
Cdd:PRK13641 104 LKD-VEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 446139018 171 SMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-238 |
7.41e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 104.43 E-value: 7.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY--GKRpVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAY-RRKLSY 79
Cdd:PRK13647 5 IEVEDLHFRYkdGTK-ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWvRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 I---PESPVIyeELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:PRK13647 84 VfqdPDDQVF--SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 157 IDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDL-----EALRQQTGLHKQTL 231
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKslltdEDIVEQAGLRLPLV 241
|
....*..
gi 446139018 232 DDIYIHV 238
Cdd:PRK13647 242 AQIFEDL 248
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-216 |
1.43e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 103.53 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYG--KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDD-IEAYRRKLSY 79
Cdd:PRK13632 8 IKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 I---PESPVIyeELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:PRK13632 88 IfqnPDNQFI--GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 157 IDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMS-TH-----ILAtaerycDRFIILDEGEVVAFGD 216
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHdmdeaILA------DKVIVFSEGKLIAQGK 225
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-220 |
1.57e-26 |
|
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: 102.64 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLL-----TPMEGSLSISDININD---DIEAYR 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 75 RKLSYIPESPVIYeELTLEEHIEMTAMAYDI-DRDEAMNRAMPLLKTFRLENELK--VFPSHFSKGMKQKVMIICAFIVN 151
Cdd:cd03260 81 RRVGMVFQKPNPF-PGSIYDNVAYGLRLHGIkLKEELDERVEEALRKAALWDEVKdrLHALGLSGGQQQRLCLARALANE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 152 PELYIIDEPFLGLDPLGIQSMLDLMVEKKNEgRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-220 |
2.70e-26 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 102.52 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDD---------IEA 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTArslsqqkglIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 73 YRRKLSYIPESPVIYEELT-LEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVN 151
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTvLENIIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 152 PELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-222 |
3.19e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 102.94 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGK-----RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI-----NDDI 70
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 71 EAYRRKLSYI---PESPVIyeELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLE-NELKVFPSHFSKGMKQKVMIIC 146
Cdd:PRK13646 81 RPVRKRIGMVfqfPESQLF--EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 147 AFIVNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA-------FGDLE 218
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSqtspkelFKDKK 238
|
....
gi 446139018 219 ALRQ 222
Cdd:PRK13646 239 KLAD 242
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
3.54e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 106.22 E-value: 3.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIEM-TAMAYDIDRDEAMNRA--MPLLKTFR--LENELKVFPSHFSKGMKQKVMIICAFIVNPEL 154
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLaRPDASDAEIREALERAglDEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRDAPL 479
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446139018 155 YIIDEPFLGLDPLGIQSMLDLMvEKKNEGRTVLMSTHILATAERyCDRFIIL 206
Cdd:TIGR02857 480 LLLDEPTAHLDAETEAEVLEAL-RALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
15-215 |
3.95e-26 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 102.79 E-value: 3.95e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI-----NDDIEAYRRKLSYI---PESPvI 86
Cdd:PRK13634 20 RRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkkNKKLKPLRKKVGIVfqfPEHQ-L 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 87 YEElTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENE-LKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLD 165
Cdd:PRK13634 99 FEE-TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEElLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446139018 166 PLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK13634 178 PKGRKEMMEMFYKlHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-228 |
4.13e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.89 E-value: 4.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-----DIEAYRRKLSYI---PESPvIYEELT 91
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSStskqkEIKPVRKKVGVVfqfPESQ-LFEETV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEhIEMTAMAYDIDRDEAMNRAMPLLKTFRLENEL-KVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQ 170
Cdd:PRK13643 103 LKD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 171 SMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTGLHK 228
Cdd:PRK13643 182 EMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQEVDFLK 239
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-215 |
1.02e-25 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 101.63 E-value: 1.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY--GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIeayRRK 76
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvwDV---RRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 77 LSYIPESP-VIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELY 155
Cdd:PRK13635 83 VGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 156 IIDEPFLGLDPLGIQSMLDLMVEKKNEGR-TVLMSTHILATAERyCDRFIILDEGEVVAFG 215
Cdd:PRK13635 163 ILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
16-211 |
2.26e-25 |
|
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: 99.02 E-value: 2.26e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIEAYRRKLSYIPESPVIYEELT 91
Cdd:cd03292 15 AALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDlrgrAIPYLRRKIGVVFQDFRLLPDRN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQS 171
Cdd:cd03292 95 VYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWE 174
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446139018 172 MLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:cd03292 175 IMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
12-220 |
2.67e-25 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 99.78 E-value: 2.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD---DIEAYRRklsyipESPVIYE 88
Cdd:PRK09493 11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDpkvDERLIRQ------EAGMVFQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 89 ELTLEEHieMTAM---------AYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:PRK09493 85 QFYLFPH--LTALenvmfgplrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDE 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 160 PFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK09493 163 PTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-221 |
3.31e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 100.31 E-value: 3.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ---DDIEAYRRKLSYIPESP-------VIY 87
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDysrKGLMKLRESVGMVFQDPdnqlfsaSVY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 EEltleehIEMTAMAYDIDRDEAMNRAMPLLKTFRLENeLKVFPSH-FSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP 166
Cdd:PRK13636 102 QD------VSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 167 LGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVV-------AFGDLEALR 221
Cdd:PRK13636 175 MGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVIlqgnpkeVFAEKEMLR 237
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-220 |
5.40e-25 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 98.67 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPviKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINInDDIEAYRRKLSyipes 83
Cdd:COG3840 3 RLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDL-TALPPAERPVS----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 pVIYEE------LTLEEHIemtAMAYDID---RDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPEL 154
Cdd:COG3840 75 -MLFQEnnlfphLTVAQNI---GLGLRPGlklTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPI 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 155 YIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:COG3840 151 LLLDEPFSALDPALRQEMLDLVDElCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-191 |
5.56e-25 |
|
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: 97.49 E-value: 5.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ---DDIEAYRRKLSYI---PESPVIYEel 90
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDysrKGLLERRQRVGLVfqdPDDQLFAA-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 91 TLEEHIEMTAMAYDIDRDEAMNR---AMPLLKTFRLENELkvfPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPL 167
Cdd:TIGR01166 85 DVDQDVAFGPLNLGLSEAEVERRvreALTAVGASGLRERP---THCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPA 161
|
170 180
....*....|....*....|....
gi 446139018 168 GIQSMLDLMVEKKNEGRTVLMSTH 191
Cdd:TIGR01166 162 GREQMLAILRRLRAEGMTVVISTH 185
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-222 |
7.56e-25 |
|
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid transport and metabolism];
Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 98.57 E-value: 7.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINInDDIEAYRR-KL----S 78
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDI-TGLPPHRIaRLgiarT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 Y-IPEspvIYEELTLEEHIEMTAMA---------------YDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKV 142
Cdd:COG0411 85 FqNPR---LFPELTVLENVLVAAHArlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 143 MIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALR 221
Cdd:COG0411 162 EIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVR 241
|
.
gi 446139018 222 Q 222
Cdd:COG0411 242 A 242
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-215 |
4.67e-24 |
|
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: 95.78 E-value: 4.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININdDIEAYRRKLSYIPE 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-DLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 163 GLDP-LGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03301 160 NLDAkLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
13-209 |
8.56e-24 |
|
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];
Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 95.19 E-value: 8.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKR-PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD----ININD----DIEAYRRK------- 76
Cdd:COG4778 21 GKRlPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHdggwVDLAQasprEILALRRRtigyvsq 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 77 -LSYIPESP---VIYEELtleehIEMTamaydIDRDEAMNRAMPLLKTFRLENEL-KVFPSHFSKGMKQKVMIICAFIVN 151
Cdd:COG4778 101 fLRVIPRVSaldVVAEPL-----LERG-----VDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIAD 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 152 PELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEG 209
Cdd:COG4778 171 PPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
13-230 |
9.67e-24 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 96.41 E-value: 9.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ-DDIEAYRRKLSYIPESP--VIYEE 89
Cdd:PRK13652 15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITkENIREVRKFVGLVFQNPddQIFSP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 90 lTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGI 169
Cdd:PRK13652 95 -TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 170 QSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTGLHKQT 230
Cdd:PRK13652 174 KELIDFLNDlPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPDLLARV 235
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-212 |
1.22e-23 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 95.33 E-value: 1.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEA--YRRKLSYI 80
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAkiMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAmaYDIDRDEAMNRAMPLLKTF-RLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGG--FFAERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 160 PFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
|
|
| ABC_ModC_like |
cd03299 |
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ... |
3-218 |
1.87e-23 |
|
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: 94.71 E-value: 1.87e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRpVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDdIEAYRRKLSYIPE 82
Cdd:cd03299 1 LKVENLSKDWKEF-KLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITN-LPPEKRDISYVPQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03299 79 NYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 163 GLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:cd03299 159 ALDVRTKEKLREELKKiRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPE 215
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-211 |
2.17e-23 |
|
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: 92.88 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGygkrPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSI--SDININDDIEAYRRKLSYI 80
Cdd:cd03215 5 LEVRGLSVK----GAVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLdgKPVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PEspviyeeltleehiemtamaydiDR-DEAMNRAMPLlktfrLENelKVFPSHFSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:cd03215 81 PE-----------------------DRkREGLVLDLSV-----AEN--IALSSLLSGGNQQKVVLARWLARDPRVLILDE 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446139018 160 PFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:cd03215 131 PTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-215 |
2.26e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.22 E-value: 2.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI-NDDIEAYRRKLSY 79
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVeALSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEELTLEEHIEMT--------AMAYDIDR---DEAMNRAMPLLKTFRLENELkvfpshfSKGMKQKVMIICAF 148
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGrtphrsrfDTWTETDRaavERAMERTGVAQFADRPVTSL-------SGGERQRVLLARAL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 149 IVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK09536 155 AQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
6-215 |
4.28e-23 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 96.64 E-value: 4.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 6 EQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ-----DDIEAYRRKLSYI 80
Cdd:PRK10070 32 EQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAkisdaELREVRRKKIAMV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:PRK10070 112 FQSFALMPHMTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 161 FLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK10070 192 FSALDPLIRTEMQDELVKlQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVG 247
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-215 |
5.09e-23 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 94.38 E-value: 5.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD--DIEAYRRKLSYIPESPVIYEELTL 92
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDeeNLWDIRNKAGMVFQNPDNQIVATI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 93 -EEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLEnELKVFPSH-FSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQ 170
Cdd:PRK13633 103 vEEDVAFGPENLGIPPEEIRERVDESLKKVGMY-EYRRHAPHlLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRR 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446139018 171 SMLDLMVE-KKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFG 215
Cdd:PRK13633 182 EVVNTIKElNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEG 226
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-215 |
5.53e-23 |
|
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: 93.07 E-value: 5.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININdDIEAYRRKLSYIPE 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 163 GLDPLGIQSM-LDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03300 160 ALDLKLRKDMqLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIG 213
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
12-220 |
6.99e-23 |
|
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: 93.23 E-value: 6.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGslsiSDINI------NDDIEAYRRKLSYIpeSPV 85
Cdd:COG1119 13 RGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYG----NDVRLfgerrgGEDVWELRKRIGLV--SPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 86 IYEELTLEEHIE---MTAmAYD-IDR-----DEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:COG1119 87 LQLRFPRDETVLdvvLSG-FFDsIGLyreptDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELLI 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 157 IDEPFLGLDPLGIQSMLDLMvEK--KNEGRTVLMSTH----ILAtaeryC-DRFIILDEGEVVAFGDLEAL 220
Cdd:COG1119 166 LDEPTAGLDLGARELLLALL-DKlaAEGAPTLVLVTHhveeIPP-----GiTHVLLLKDGRVVAAGPKEEV 230
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
5-220 |
8.08e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 93.49 E-value: 8.08e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ--------------DDI 70
Cdd:PRK10619 8 VIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkNQL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 71 EAYRRKLSYIPESPVIYEELT-LEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKV-FPSHFSKGMKQKVMIICAF 148
Cdd:PRK10619 88 RLLRTRLTMVFQHFNLWSHMTvLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARAL 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 149 IVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
5-191 |
8.24e-23 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 91.94 E-value: 8.24e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPESP 84
Cdd:PRK13540 4 VIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 85 VIYEELTLEEHIemtamAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGL 164
Cdd:PRK13540 84 GINPYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVAL 158
|
170 180
....*....|....*....|....*..
gi 446139018 165 DPLGIQSMLDLMVEKKNEGRTVLMSTH 191
Cdd:PRK13540 159 DELSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
3-215 |
9.56e-23 |
|
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: 92.17 E-value: 9.56e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFElnKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDdIEAYRRKLSYIPE 82
Cdd:cd03298 1 VRLDKIRFSYGEQPMHFDLTFA--QGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTA-APPADRPVSMLFQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03298 78 ENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 163 GLDPLGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03298 158 ALDPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-215 |
1.23e-22 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 91.46 E-value: 1.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRpVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP--MEGSLSISDINIndDIEAYRRKLS 78
Cdd:cd03213 9 LTVTVKSSPSKSGKQ-LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPL--DKRSFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHIEMTAmaydidrdeamnrampllktfrlenELKVfpshFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAA-------------------------KLRG----LSGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 159 EPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHiLATAERY--CDRFIILDEGEVVAFG 215
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTGRTIICSIH-QPSSEIFelFDKLLLLSQGRVIYFG 194
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-225 |
1.27e-22 |
|
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: 96.62 E-value: 1.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYG--KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYI 80
Cdd:TIGR01257 1938 LRLNELTKVYSgtSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYC 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:TIGR01257 2018 PQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEP 2097
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 161 FLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTG 225
Cdd:TIGR01257 2098 TTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSKFG 2162
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-215 |
2.85e-22 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 91.11 E-value: 2.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 14 KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYEElTL 92
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 93 EEHIEMTAMAYDidrDEAMNRAMPL--LKTFR------LENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPflgl 164
Cdd:cd03245 95 RDNITLGAPLAD---DERILRAAELagVTDFVnkhpngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEP---- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 165 dplgiQSMLDLMVEKK--------NEGRTVLMSTHILAtAERYCDRFIILDEGEVVAFG 215
Cdd:cd03245 168 -----TSAMDMNSEERlkerlrqlLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
2-245 |
6.40e-22 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 91.48 E-value: 6.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININddiEAYRRKL-SY 79
Cdd:PRK15056 6 GIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR---QALQKNLvAY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPES-------PVIYEELTLEE---HIEMTAMAYDIDR---DEAMNRAMPLLKTFRLENELkvfpshfSKGMKQKVMIIC 146
Cdd:PRK15056 83 VPQSeevdwsfPVLVEDVVMMGrygHMGWLRRAKKRDRqivTAALARVDMVEFRHRQIGEL-------SGGQKKRVFLAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 147 AFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDrFIILDEGEVVAFGDLEALRQQTGL 226
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFTAENL 234
|
250 260
....*....|....*....|
gi 446139018 227 hKQTLDDIYIHVT-QGGDVH 245
Cdd:PRK15056 235 -ELAFSGVLRHVAlNGSEES 253
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-237 |
8.28e-22 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 94.04 E-value: 8.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTtikhMLGLLT----PMEGSLSISDININDdiEAYRRKLS 78
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIAgarkIQQGRVEVLGGDMAD--ARHRRAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 yipesPVI-----------YEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENelkvFPS----HFSKGMKQKVM 143
Cdd:NF033858 76 -----PRIaympqglgknlYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP----FADrpagKLSGGMKQKLG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 144 IICAFIVNPELYIIDEPFLGLDPLGIQSMLDLM--VEKKNEGRTVLMSTHILATAERYcDRFIILDEGEVVAFGDLEALR 221
Cdd:NF033858 147 LCCALIHDPDLLILDEPTTGVDPLSRRQFWELIdrIRAERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELL 225
|
250
....*....|....*.
gi 446139018 222 QQTGlhKQTLDDIYIH 237
Cdd:NF033858 226 ARTG--ADTLEAAFIA 239
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-229 |
1.03e-21 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 89.98 E-value: 1.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGK--RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:cd03251 1 VEFKNVTFRYPGdgPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIemtamAY---DIDRDEAMNRA-----------MPL-LKTFRLENELKVfpshfSKGMKQKVMI 144
Cdd:cd03251 81 VSQDVFLFND-TVAENI-----AYgrpGATREEVEEAAraanahefimeLPEgYDTVIGERGVKL-----SGGQRQRIAI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 145 ICAFIVNPELYIIDEPFLGLDPLG---IQSMLD-LMvekknEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEAL 220
Cdd:cd03251 150 ARALLKDPPILILDEATSALDTESerlVQAALErLM-----KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
....*....
gi 446139018 221 RQQTGLHKQ 229
Cdd:cd03251 224 LAQGGVYAK 232
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-229 |
1.13e-21 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 93.25 E-value: 1.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 14 KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYEElTL 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLFSG-SV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 93 EEHIemtamAYDIDR---DEAMNRA---------MPLLKTFRLENELKvfPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:TIGR00958 572 RENI-----AYGLTDtpdEEIMAAAkaanahdfiMEFPNGYDTEVGEK--GSQLSGGQKQRIAIARALVRKPRVLILDEA 644
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 161 FLGLDplgIQSMLDLMVEKKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQTGLHKQ 229
Cdd:TIGR00958 645 TSALD---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGCYKH 709
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-215 |
1.58e-21 |
|
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: 88.89 E-value: 1.58e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNkGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIS-----DININDDIEAYRRKLSYIPESPVIYEELTLEE 94
Cdd:cd03297 16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNgtvlfDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIE--MTAMAYDIDRDeamnRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLD-PLGIQS 171
Cdd:cd03297 95 NLAfgLKRKRNREDRI----SVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDrALRLQL 170
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446139018 172 MLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03297 171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
16-215 |
1.95e-21 |
|
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: 88.70 E-value: 1.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYEElTLEE 94
Cdd:cd03244 18 PVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISIIPQDPVLFSG-TIRS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIEMTAMAYDIDRDEAMNRAmpLLKTF------RLENELKVFPSHFSKGMKQkvmIIC---AFIVNPELYIIDEPFLGLD 165
Cdd:cd03244 97 NLDPFGEYSDEELWQALERV--GLKEFveslpgGLDTVVEEGGENLSVGQRQ---LLClarALLRKSKILVLDEATASVD 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 166 PLG---IQSMLdlmvekKNE--GRTVLMSTHILAT-AEryCDRFIILDEGEVVAFG 215
Cdd:cd03244 172 PETdalIQKTI------REAfkDCTVLTIAHRLDTiID--SDRILVLDKGRVVEFD 219
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-229 |
5.03e-21 |
|
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213220 [Multi-domain] Cd Length: 236 Bit Score: 88.06 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYG-KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYI 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTL-----------EEHIEMTAMAYDIDrDEAMNraMPL-LKTFRLENELKVfpshfSKGMKQKVMIICAF 148
Cdd:cd03253 81 PQDTVLFNDTIGynirygrpdatDEEVIEAAKAAQIH-DKIMR--FPDgYDTIVGERGLKL-----SGGEKQRVAIARAI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 149 IVNPELYIIDEPFLGLDPLGIQSMLDLMvEKKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQTGLHK 228
Cdd:cd03253 153 LKNPPILLLDEATSALDTHTEREIQAAL-RDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELLAKGGLYA 230
|
.
gi 446139018 229 Q 229
Cdd:cd03253 231 E 231
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-218 |
8.09e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 89.37 E-value: 8.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLT----GGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKhMLGLL-TPMEGSLSISDININD----DIEAY 73
Cdd:COG1135 2 IELENLSktfpTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIR-CINLLeRPTSGSVLVDGVDLTAlserELRAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 74 RRKLSYIPESPVIYEELTLEEHIemtamAY-----DIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAF 148
Cdd:COG1135 81 RRKIGMIFQHFNLLSSRTVAENV-----ALpleiaGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARAL 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 149 IVNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:COG1135 156 ANNPKVLLCDEATSALDPETTRSILDLLKDiNRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVL 226
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
5-211 |
9.91e-21 |
|
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: 85.73 E-value: 9.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYG--KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIP 81
Cdd:cd03246 3 VENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESpVIYEELTLEEHIemtamaydidrdeamnrampllktfrlenelkvfpshFSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:cd03246 83 QD-DELFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446139018 162 LGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERyCDRFIILDEGEV 211
Cdd:cd03246 125 SHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
5-220 |
1.06e-20 |
|
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: 90.51 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLT----GGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP----MEGSLSISDININDDIEAYRRK 76
Cdd:COG4172 9 VEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLLGLSERELRR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 77 L-----SYI---PES---PV------IYEelTLEEHIEMTamaydidRDEAMNRAMPLLKTFRL---ENELKVFPSHFSK 136
Cdd:COG4172 89 IrgnriAMIfqePMTslnPLhtigkqIAE--VLRLHRGLS-------GAAARARALELLERVGIpdpERRLDAYPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 137 GMKQKVMIICAFIVNPELYIIDEPFLGLDpLGIQS-MLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAF 214
Cdd:COG4172 160 GQRQRVMIAMALANEPDLLIADEPTTALD-VTVQAqILDLLKDlQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQ 238
|
....*.
gi 446139018 215 GDLEAL 220
Cdd:COG4172 239 GPTAEL 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
15-223 |
1.20e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 87.88 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI-----NDDIEAYRRKLSYI---PESPVi 86
Cdd:PRK13649 20 GRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDIKQIRKKVGLVfqfPESQL- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 87 YEELTLEEhIEMTAMAYDIDRDEAMNRAMPLLKTFRLENEL-KVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLD 165
Cdd:PRK13649 99 FEETVLKD-VAFGPQNFGVSQEEAEALAREKLALVGISESLfEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLD 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 166 PLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQ 223
Cdd:PRK13649 178 PKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-211 |
3.53e-20 |
|
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: 85.60 E-value: 3.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRP---VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLS 78
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEElTLEEHIemtamAYDIdRDEAMNRAMPLLKTFRLENELKVFP-----------SHFSKGMKQKVMIICA 147
Cdd:cd03248 92 LVGQEPVLFAR-SLQDNI-----AYGL-QSCSFECVKEAAQKAHAHSFISELAsgydtevgekgSQLSGGQKQRVAIARA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 148 FIVNPELYIIDEPFLGLDpLGIQSMLDLMVEKKNEGRTVLMSTHILATAERyCDRFIILDEGEV 211
Cdd:cd03248 165 LIRNPQVLILDEATSALD-AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
3-220 |
7.51e-20 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 87.77 E-value: 7.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSI--SDININDDIEAYRRKLSYI 80
Cdd:COG1129 5 LEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLdgEPVRFRSPRDAQAAGIAII 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHI----EMTAMAYdIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:COG1129 85 HQELNLVPNLSVAENIflgrEPRRGGL-IDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLI 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 157 IDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:COG1129 164 LDEPTASLTEREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-217 |
7.97e-20 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.92 E-value: 7.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ--DDIEAYRRKLSYI 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNklDHKLAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYD-------IDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDL 217
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMV 229
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
8-212 |
8.78e-20 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 85.51 E-value: 8.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 8 LTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ----DDIEAYRRKLSYI--- 80
Cdd:PRK10419 18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklnrAQRKAFRRDIQMVfqd 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 ------PESPV---IYEELtleEHIemtamaYDIDRDEAMNRAMPLLKTFRLENE-LKVFPSHFSKGMKQKVMIICAFIV 150
Cdd:PRK10419 98 sisavnPRKTVreiIREPL---RHL------LSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAV 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 151 NPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTV-LMSTHILATAERYCDRFIILDEGEVV 212
Cdd:PRK10419 169 EPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIV 231
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-218 |
9.30e-20 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 86.32 E-value: 9.30e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP---MEGSLSISDININDDIEAYRRKL-----SYIPESPV---- 85
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILNLPEKELNKLraeqiSMIFQDPMtsln 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 86 ----IYEELTleehiEMTAMAYDIDRDEAMNRAMPLLKTFRL---ENELKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:PRK09473 112 pymrVGEQLM-----EVLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 159 EPFLGLDpLGIQS-MLDLMVEKKNEGRT-VLMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:PRK09473 187 EPTTALD-VTVQAqIMTLLNELKREFNTaIIMITHDLGVVAGICDKVLVMYAGRTMEYGNAR 247
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
9.39e-20 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 85.21 E-value: 9.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwSPAELARRRAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEELTLEEHIEMTAMAYDIDRDEAMN---RAMPLLKTFRLENELkvFPShFSKGMKQKVMI------ICAFIV 150
Cdd:PRK13548 81 LPQHSSLSFPFTVEEVVAMGRAPHGLSRAEDDAlvaAALAQVDLAHLAGRD--YPQ-LSGGEQQRVQLarvlaqLWEPDG 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 151 NPELYIIDEPFLGLDPLGIQSMLDLMVEK-KNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGD-LEALRQQT 224
Cdd:PRK13548 158 PPRWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTpAEVLTPET 233
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-240 |
1.32e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 85.24 E-value: 1.32e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY--GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP---MEGSLSISDININDD-IEAYRRK 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKtVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 77 LSYIPESP-VIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELY 155
Cdd:PRK13640 86 VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKII 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 156 IIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAErYCDRFIILDEGEVVA-------FGDLEALrQQTGLH 227
Cdd:PRK13640 166 ILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAqgspveiFSKVEML-KEIGLD 243
|
250 260
....*....|....*....|
gi 446139018 228 -------KQTLDDIYIHVTQ 240
Cdd:PRK13640 244 ipfvyklKNKLKEKGISVPQ 263
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-229 |
1.99e-19 |
|
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: 84.07 E-value: 1.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYEElTLEEH 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 96 IEMTAMAYDIDRDEAMNR---AMPLLKTFRLENELKVFP--SHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLG-- 168
Cdd:cd03252 96 IALADPGMSMERVIEAAKlagAHDFISELPEGYDTIVGEqgAGLSGGQRQRIAIARALIHNPRILIFDEATSALDYESeh 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 169 --IQSMLDLMvekknEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQTGLHKQ 229
Cdd:cd03252 176 aiMRNMHDIC-----AGRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLAENGLYAY 232
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-215 |
3.56e-19 |
|
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: 83.16 E-value: 3.56e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDdIEAYRRKLSYI 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATD-VPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHI----EMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:cd03296 80 FQHYALFRHMTVFDNVafglRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 157 IDEPFLGLDPlGIQSMLDLMVEKKNE--GRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:cd03296 160 LDEPFGALDA-KVRKELRRWLRRLHDelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVG 219
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-198 |
3.76e-19 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 82.94 E-value: 3.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSL-----SISDININDDIEAYRRKLSYIPESPVIYEELT 91
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqPMSKLSSAAKAELRNQKLGFIYQFHHLLPDFT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQS 171
Cdd:PRK11629 104 ALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183
|
170 180
....*....|....*....|....*...
gi 446139018 172 MLDLMVE-KKNEGRTVLMSTHILATAER 198
Cdd:PRK11629 184 IFQLLGElNRLQGTAFLVVTHDLQLAKR 211
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-213 |
4.77e-19 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 85.46 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 19 KDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD--ININDDIEAYRRKLSYIPESPVIYEELTLEEHI 96
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIALGIGMVHQHFMLVPNLTVAENI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 97 ----EMTAMAYdIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSM 172
Cdd:COG3845 102 vlglEPTKGGR-LDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLTPQEADEL 180
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446139018 173 LDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:COG3845 181 FEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVG 221
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
12-229 |
6.64e-19 |
|
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: 82.59 E-value: 6.64e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRP---VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIY 87
Cdd:cd03249 10 YPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGLVSQEPVLF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 eELTLEEHIEMTamAYDIDRDEAMNRAmpllKTFRLENELKVFP-----------SHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:cd03249 90 -DGTIAENIRYG--KPDATDEEVEEAA----KKANIHDFIMSLPdgydtlvgergSQLSGGQKQRIAIARALLRNPKILL 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 157 IDEPFLGLD---PLGIQSMLDlmveKKNEGRTVLMSTHILATAeRYCDRFIILDEGEVVAFGDLEALRQQTGLHKQ 229
Cdd:cd03249 163 LDEATSALDaesEKLVQEALD----RAMKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQGTHDELMAQKGVYAK 233
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-211 |
7.45e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 82.75 E-value: 7.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLT---------PMEGSLSISDININDDIEAY 73
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksagshiELLGRTVQREGRLARDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 74 RRKLSYIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHF--------SKGMKQKVMII 145
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFahqrvstlSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 146 CAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-216 |
8.47e-19 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 82.75 E-value: 8.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ---DDIEAYRRKLSYI---PESPV 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLDyskRGLLALRQQVATVfqdPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 86 IYEELtlEEHIEMTAMAYDIDRDEAMNR---AMPLLKTFRLENELKVFPSHfskGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:PRK13638 91 FYTDI--DSDIAFSLRNLGVPEAEITRRvdeALTLVDAQHFRHQPIQCLSH---GQKKRVAIAGALVLQARYLLLDEPTA 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 163 GLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGD 216
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGA 219
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-215 |
9.77e-19 |
|
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 81.30 E-value: 9.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKR--PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIEmtamAYDIDRDEAMNRAMpllktfrlenELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLD----PFDEYSDEEIYGAL----------RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 160 PFLGLDpLGIQSMLDLMVEKKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFG 215
Cdd:cd03369 152 ATASID-YATDALIQKTIREEFTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-216 |
1.08e-18 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 82.20 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 21 INFELNKGEIVGLIGLNGAGKSTTIKHMLGLLtPMEGSLSISDININD-DIEAYRRKLSYIPES-------PViYEELTL 92
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELARHRAYLSQQqsppfamPV-FQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 93 eeHIEMTAMAYDIDRdeAMNRampLLKTFRLENELKVFPSHFSKGMKQKVMIICAFI-----VNPE--LYIIDEPFLGLD 165
Cdd:COG4138 93 --HQPAGASSEAVEQ--LLAQ---LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446139018 166 pLGIQSMLD-LMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGD 216
Cdd:COG4138 166 -VAQQAALDrLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-210 |
1.78e-18 |
|
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.
Pssm-ID: 213188 [Multi-domain] Cd Length: 144 Bit Score: 79.03 E-value: 1.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininddieayRRKLSYIPe 82
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGS----------TVKIGYFE- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 spviyeeltleehiemtamaydidrdeamnrampllktfrlenelkvfpsHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03221 70 --------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPTN 99
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446139018 163 GLDPLGIQSMLDLMVEKKnegRTVLMSTHILATAERYCDRFIILDEGE 210
Cdd:cd03221 100 HLDLESIEALEEALKEYP---GTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
3-212 |
2.00e-18 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 81.07 E-value: 2.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI----NDDIEAYRRKL 77
Cdd:PRK10908 2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:PRK10908 82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-218 |
2.11e-18 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 82.96 E-value: 2.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININdDIEAYRRKLSYIPE 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLS-HVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 163 GLD-PLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:PRK11607 179 ALDkKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE 235
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
5-192 |
2.28e-18 |
|
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: 80.23 E-value: 2.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPESP 84
Cdd:cd03231 3 ADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 85 VIYEELTLEEHIEMTAmayDIDRDEAMNRAmplLKTFRLeNELKVFPSH-FSKGMKQKVMIICAFIVNPELYIIDEPFLG 163
Cdd:cd03231 83 GIKTTLSVLENLRFWH---ADHSDEQVEEA---LARVGL-NGFEDRPVAqLSAGQQRRVALARLLLSGRPLWILDEPTTA 155
|
170 180
....*....|....*....|....*....
gi 446139018 164 LDPLGIQSMLDLMVEKKNEGRTVLMSTHI 192
Cdd:cd03231 156 LDKAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
5-215 |
4.50e-18 |
|
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: 78.89 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYG--KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPE 82
Cdd:cd03247 3 INNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVLNQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEElTLEEHIEmtamaydidrdeamnrampllktfrlenelkvfpSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:cd03247 83 RPYLFDT-TLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTV 127
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 163 GLDPLGIQSMLDLMVEKKnEGRTVLMSTHILATAERYcDRFIILDEGEVVAFG 215
Cdd:cd03247 128 GLDPITERQLLSLIFEVL-KDKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-211 |
4.95e-18 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 80.62 E-value: 4.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI--------------N 67
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvpadR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 68 DDIEAYRRKLSYIPESPVIYEELT-LEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIIC 146
Cdd:COG4598 88 RQLQRIRTRLGMVFQSFNLWSHMTvLENVIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRAAIAR 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 147 AFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:COG4598 168 ALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-220 |
5.61e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 80.80 E-value: 5.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD--DIEAYRRKLSYIPESP-VIYEELTL 92
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLVGIVFQNPeTQFVGRTV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 93 EEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSM 172
Cdd:PRK13644 96 EEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAV 175
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446139018 173 LDLMVEKKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK13644 176 LERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV 222
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-191 |
6.87e-18 |
|
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: 82.41 E-value: 6.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIEMTAMAYDidrDEAMNRAmplLKTFRLENELKVFP-----------SHFSKGMKQKVMIICAF 148
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLARPDAT---DEELWAA---LERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 446139018 149 IVNPELYIIDEPFLGLDPLGIQSMLDLMVeKKNEGRTVLMSTH 191
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLL-AALSGRTVVLITH 528
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
13-212 |
8.14e-18 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 81.00 E-value: 8.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVI--KDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI----NDDIEAYRRKLSYIPE---- 82
Cdd:PRK11153 14 GGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalsEKELRKARRQIGMIFQhfnl 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 --SPVIYEE--LTLEehiemtamAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:PRK11153 94 lsSRTVFDNvaLPLE--------LAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 159 EPFLGLDPLGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:PRK11153 166 EATSALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
21-231 |
9.49e-18 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 81.81 E-value: 9.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 21 INFELNKGEIVGLIGLNGAGKSTTIKHMLGLLtPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYEElTLEEHIEM- 98
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLSWVGQNPQLPHG-TLRDNVLLg 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 99 TAMAYDIDRDEAMNRA-----MPLLkTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP----LGI 169
Cdd:PRK11174 447 NPDASDEQLQQALENAwvsefLPLL-PQGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAhseqLVM 525
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 170 QSMLDLMvekknEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQTGLHKQTL 231
Cdd:PRK11174 526 QALNAAS-----RRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQAGGLFATLL 581
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-216 |
9.75e-18 |
|
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: 81.77 E-value: 9.75e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIkHML-GL--LTPMEG---------------------- 57
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLM-HVLrGMdqYEPTSGriiyhvalcekcgyverpskvg 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 58 --------SLSISDININDDIEAYRRKLS-----YIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLE 124
Cdd:TIGR03269 80 epcpvcggTLEPEEVDFWNLSDKLRRRIRkriaiMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 125 NELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEK-KNEGRTVLMSTHILATAERYCDRF 203
Cdd:TIGR03269 160 HRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDLSDKA 239
|
250
....*....|...
gi 446139018 204 IILDEGEVVAFGD 216
Cdd:TIGR03269 240 IWLENGEIKEEGT 252
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-242 |
1.14e-17 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 80.93 E-value: 1.14e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAG--KSTTIKHMLGlltPMEGSLSISDININDDIEAYRRKLS-Y 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:NF000106 91 RPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 160 PFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTG--------LHKQTL 231
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGgrtlqirpAHAAEL 250
|
250
....*....|.
gi 446139018 232 DDIYIHVTQGG 242
Cdd:NF000106 251 DRMVGAIAQAG 261
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-233 |
1.23e-17 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 81.95 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIsdininddieaYRRKLSYIPESPVIYEElTLEE 94
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVV-----------IRGSVAYVPQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIeMTAMAYDIDRdeaMNRAMPLLKtfrLENELKVFPSH-----------FSKGMKQKVMIICAFIVNPELYIIDEPFLG 163
Cdd:PLN03232 698 NI-LFGSDFESER---YWRAIDVTA---LQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 164 LDPLGIQSMLDLMVEKKNEGRTVLMST---HILATAerycDRFIILDEGEVVAFGDLEALRQQTGLHKQTLDD 233
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLM----DRIILVSEGMIKEEGTFAELSKSGSLFKKLMEN 839
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
1.25e-17 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 78.38 E-value: 1.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINIndDIEAYRRKLSYI 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI--DDPDVAEACHYL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAmayDIdRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:PRK13539 79 GHRNAMKPALTVAENLEFWA---AF-LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 446139018 161 FLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHI 192
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-212 |
1.31e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 79.75 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDIN---FELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ-DDIEAYRRKLS 78
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESP-VIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVEKKNEGR-TVLMSTHILATAERyCDRFIILDEGEVV 212
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-213 |
1.38e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 81.22 E-value: 1.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGgygkRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD--ININDDIEAYRRKLSYIP 81
Cdd:COG1129 258 EVEGLSV----GGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 E---SPVIYEELTLEEHIEMTAMAYD-----IDRDEAMNRAMPLLKTFRL---ENELKVfpSHFSKGMKQKVMIICAFIV 150
Cdd:COG1129 334 EdrkGEGLVLDLSIRENITLASLDRLsrgglLDRRRERALAEEYIKRLRIktpSPEQPV--GNLSGGNQQKVVLAKWLAT 411
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 151 NPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:COG1129 412 DPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
5-192 |
1.41e-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: 78.17 E-value: 1.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPESP 84
Cdd:TIGR01189 3 ARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 85 VIYEELTLEEHIEMtamaYDIDRDEAMNRAMPLLKTFRLeNELKVFPSHF-SKGMKQKVMIICAFIVNPELYIIDEPFLG 163
Cdd:TIGR01189 83 GLKPELSALENLHF----WAAIHGGAQRTIEDALAAVGL-TGFEDLPAAQlSAGQQRRLALARLWLSRRPLWILDEPTTA 157
|
170 180
....*....|....*....|....*....
gi 446139018 164 LDPLGIQSMLDLMVEKKNEGRTVLMSTHI 192
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGIVLLTTHQ 186
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
18-232 |
1.55e-17 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 79.67 E-value: 1.55e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ------DDIEAYRRKLSYIPESP--VIYEE 89
Cdd:PRK13645 27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPanlkkiKEVKRLRKEIGLVFQFPeyQLFQE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 90 lTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENE-LKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLG 168
Cdd:PRK13645 107 -TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKG 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 169 IQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGD-LEALRQQTGLHKQTLD 232
Cdd:PRK13645 186 EEDFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSpFEIFSNQELLTKIEID 251
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
3-220 |
1.81e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 78.47 E-value: 1.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVikDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAyRRKLSYIPE 82
Cdd:PRK10771 2 LKLTDITWLYHHLPM--RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS-RRPVSMLFQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIE------MTAMAYDIDRDEAMNRAMpllktfRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:PRK10771 79 ENNLFSHLTVAQNIGlglnpgLKLNAAQREKLHAIARQM------GIEDLLARLPGQLSGGQRQRVALARCLVREQPILL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 157 IDEPFLGLDPLGIQSMLDLMVEKKNEGR-TVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK10771 153 LDEPFSALDPALRQEMLTLVSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-243 |
2.61e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 78.20 E-value: 2.61e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIP 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPVIYEELTLEEHIE----------MTAmaydIDRdEAMNRAMPLLKTFRLEN----ELkvfpshfSKGMKQKV---MI 144
Cdd:COG4604 82 QENHINSRLTVRELVAfgrfpyskgrLTA----EDR-EIIDEAIAYLDLEDLADryldEL-------SGGQRQRAfiaMV 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 145 ICAfivNPElYII-DEPFLGLDP---LGIQSMLDLMVEKKneGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:COG4604 150 LAQ---DTD-YVLlDEPLNNLDMkhsVQMMKLLRRLADEL--GKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223
|
250 260
....*....|....*....|....*.
gi 446139018 221 rqqtgLHKQTLDDIY---IHVTQGGD 243
Cdd:COG4604 224 -----ITPEVLSDIYdtdIEVEEIDG 244
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
12-215 |
3.17e-17 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 78.35 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLL-----TPMEGSLSISDINI-NDDIEA--YRRKLSYIPES 83
Cdd:PRK14267 14 YGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIySPDVDPieVRREVGMVFQY 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 PVIYEELTLEEHIEMTAMAYDI--DRDEAMNRAMPLLKTFRL----ENELKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:PRK14267 94 PNPFPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLM 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVEKKNEgRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK14267 174 DEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
13-191 |
3.17e-17 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 77.15 E-value: 3.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPESPVIYEELTL 92
Cdd:PRK13538 12 DERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQPGIKTELTA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 93 EEHIEMTAMAYDIDRDEAMNRAmplLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSM 172
Cdd:PRK13538 92 LENLRFYQRLHGPGDDEALWEA---LAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVARL 168
|
170
....*....|....*....
gi 446139018 173 LDLMVEKKNEGRTVLMSTH 191
Cdd:PRK13538 169 EALLAQHAEQGGMVILTTH 187
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
5-215 |
5.38e-17 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 77.46 E-value: 5.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPES 83
Cdd:COG4559 4 AENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELARRRAVLPQH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 PVIYEELTLEEHIEMTAMAY---DIDRDEAMNRAMPL--LKTF--RLENELkvfpshfSKGMKQKVMI--ICAFIVNPE- 153
Cdd:COG4559 84 SSLAFPFTVEEVVALGRAPHgssAAQDRQIVREALALvgLAHLagRSYQTL-------SGGEQQRVQLarVLAQLWEPVd 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 154 ----LYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:COG4559 157 ggprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-214 |
6.03e-17 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.34 E-value: 6.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininddieayRRKLSYIPESP 84
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK----------GLRIGYLPQEP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 85 VIYEELTLEEHIEM-------------TAMAYDIDRDEAMNRAMPLLKTFR------LENELKV------FP-------- 131
Cdd:COG0488 71 PLDDDLTVLDTVLDgdaelraleaeleELEAKLAEPDEDLERLAELQEEFEalggweAEARAEEilsglgFPeedldrpv 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 132 SHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDplgIQSMLDLmvEK--KNEGRTVLMSTHilataERY-----CDRFI 204
Cdd:COG0488 151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD---LESIEWL--EEflKNYPGTVLVVSH-----DRYfldrvATRIL 220
|
250
....*....|
gi 446139018 205 ILDEGEVVAF 214
Cdd:COG0488 221 ELDRGKLTLY 230
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-226 |
8.64e-17 |
|
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: 79.22 E-value: 8.64e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYeeltlEEH 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiGLHDLRFKITIIPQDPVLF-----SGS 1375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 96 IEMTAMAYDIDRDEAMNRAMPL--LKTF------RLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDpL 167
Cdd:TIGR00957 1376 LRMNLDPFSQYSDEEVWWALELahLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD-L 1454
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 168 GIQSMLDLMVEKKNEGRTVLMSTHILATAERYCdRFIILDEGEVVAFGDLEALRQQTGL 226
Cdd:TIGR00957 1455 ETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQRGI 1512
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-209 |
9.03e-17 |
|
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: 76.74 E-value: 9.03e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIeayrrklsyiPESPVIYEE------LT 91
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPG----------PDRMVVFQNysllpwLT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEHIEMTAMAYDIDRDEAMNRAM--PLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGI 169
Cdd:TIGR01184 71 VRENIALAVDRVLPDLSKSERRAIveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446139018 170 QSMLDLMVEKKNEGR-TVLMSTHILATAERYCDRFIILDEG 209
Cdd:TIGR01184 151 GNLQEELMQIWEEHRvTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-213 |
9.77e-17 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 79.00 E-value: 9.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTtIKHMLGLL-TPMEGSLSISDINI----NDDIEAYRRK-LSYIPESPVIYEEL 90
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKST-LMNILGCLdKPTSGTYRVAGQDVatldADALAQLRREhFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 91 TLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQ 170
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446139018 171 SMLDLMVEKKNEGRTVLMSTH---ILATAErycdRFIILDEGEVVA 213
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTHdpqVAAQAE----RVIEIRDGEIVR 223
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-234 |
1.88e-16 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 76.34 E-value: 1.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI----NDDIEAYRRKLS 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHI-----EMTAMAYDIDRDEAMNRamplLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVayplrEHTQLPAPLLHSTVMMK----LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTGLH-KQTL 231
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISElNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPRvRQFL 243
|
...
gi 446139018 232 DDI 234
Cdd:PRK11831 244 DGI 246
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-233 |
1.97e-16 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 76.12 E-value: 1.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSI-----SDININDDIEAYRRKLS 78
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrdgQLRDLYALSEAERRRLL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 -----YIPESPV------------IYEEL--TLEEH---IEMTAMAY----DIDRDeamnrampllktfRLENelkvFPS 132
Cdd:PRK11701 88 rtewgFVHQHPRdglrmqvsaggnIGERLmaVGARHygdIRATAGDWlervEIDAA-------------RIDD----LPT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 133 HFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDpLGIQS-MLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGE 210
Cdd:PRK11701 151 TFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQArLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
|
250 260
....*....|....*....|...
gi 446139018 211 VVafgdlealrqQTGLHKQTLDD 233
Cdd:PRK11701 230 VV----------ESGLTDQVLDD 242
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-211 |
2.10e-16 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 75.87 E-value: 2.10e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSL---SISDININDDIEAYRRKLSYIP 81
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELlagTAPLAEAREDTRLMFQDARLLP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPVIYE-ELTLEEHIemtamaydidRDEAMnRAmplLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:PRK11247 95 WKKVIDNvGLGLKGQW----------RDAAL-QA---LAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446139018 161 FLGLDPLGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:PRK11247 161 LGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-223 |
2.50e-16 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 77.41 E-value: 2.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDiNInddieayrrKLSYIP- 81
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLGE-TV---------KIGYFDq 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPVIYEELTLEEHI--------EMTAMAY----DIDRDEAMNRAmpllktfrlenelkvfpSHFSKGMKQKVMIICAFI 149
Cdd:COG0488 386 HQEELDPDKTVLDELrdgapggtEQEVRGYlgrfLFSGDDAFKPV-----------------GVLSGGEKARLALAKLLL 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 150 VNPELYIIDEPFLGLDPLGIQSMLDLMVEKknEGrTVLMSTHilataERY-----CDRFIILDEGEVVAF-GDLEALRQQ 223
Cdd:COG0488 449 SPPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSH-----DRYfldrvATRILEFEDGGVREYpGGYDDYLEK 520
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-215 |
3.70e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 75.41 E-value: 3.70e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 6 EQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISdiniNDDIEAY-----RRKLSYI 80
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLD----GEHIQHYaskevARRIGLL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHI-------EMTAMAYDIDRDEAMNRAMPLLKTFRLENElkvFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:PRK10253 87 AQNATTPGDITVQELVargryphQPLFTRWRKEDEEAVTKAMQATGITHLADQ---SVDTLSGGQRQRAWIAMVLAQETA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK10253 164 IMLLDEPTTWLDISHQIDLLELLSElNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
14-212 |
3.71e-16 |
|
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: 74.61 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 14 KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTpmEGSLSISDININD---DIEAYRRKLSYIPESPVIYEEL 90
Cdd:cd03234 19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVE--GGGTTSGQILFNGqprKPDQFQKCVAYVRQDDILLPGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 91 TLEEHIEMTAM---------AYDIDRDEAMnrAMPLLKTFRLENELKvfpSHFSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:cd03234 97 TVRETLTYTAIlrlprkssdAIRKKRVEDV--LLRDLALTRIGGNLV---KGISGGERRRVSIAVQLLWDPKVLILDEPT 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 162 LGLDPLGIQSMLDLMVEKKNEGRTVLMSTHiLATAE--RYCDRFIILDEGEVV 212
Cdd:cd03234 172 SGLDSFTALNLVSTLSQLARRNRIVILTIH-QPRSDlfRLFDRILLLSSGEIV 223
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
5-191 |
5.50e-16 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 74.74 E-value: 5.50e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDdieayrrklsyiP--E 82
Cdd:PRK11248 4 ISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEG------------PgaE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTL------EEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:PRK11248 72 RGVVFQNEGLlpwrnvQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 446139018 157 IDEPFLGLDPLGIQSMLDLMVEKKNE-GRTVLMSTH 191
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITH 187
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-193 |
6.49e-16 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 74.77 E-value: 6.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininddieayRRKLSYIPE 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------KLRIGYVPQ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SpvIYEELTLEEHIEMTAMAYDIDRDEAMnraMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:PRK09544 75 K--LYLDTTLPLTVNRFLRLRPGTKKEDI---LPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQ 149
|
170 180 190
....*....|....*....|....*....|..
gi 446139018 163 GLDPLGIQSMLDLMVEKKNE-GRTVLMSTHIL 193
Cdd:PRK09544 150 GVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
12-215 |
6.97e-16 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 75.84 E-value: 6.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININdDIEAYRRKLSYIPESPVIYEELT 91
Cdd:PRK11000 13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVFQSYALYPHLS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEHIEM---TAMAYDIDRDEAMNRAMPLLKtfrLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP-L 167
Cdd:PRK11000 92 VAENMSFglkLAGAKKEEINQRVNQVAEVLQ---LAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAaL 168
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446139018 168 GIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK11000 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVG 216
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
16-210 |
1.16e-15 |
|
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This subfamily is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.
Pssm-ID: 213217 [Multi-domain] Cd Length: 204 Bit Score: 72.89 E-value: 1.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISdininddieayrRKLSYIPESPVIYEElTLEEH 95
Cdd:cd03250 19 FTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVP------------GSIAYVSQEPWIQNG-TIREN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 96 IEMTAmAYDIDR-DEAmnramplLKTFRLENELKVFPSH-----------FSKGMKQKVMIICAFIVNPELYIIDEPFLG 163
Cdd:cd03250 86 ILFGK-PFDEERyEKV-------IKACALEPDLEILPDGdlteigekginLSGGQKQRISLARAVYSDADIYLLDDPLSA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 164 LDPL--------GIQSMLdlmvekkNEGRTVLMSTHILATAeRYCDRFIILDEGE 210
Cdd:cd03250 158 VDAHvgrhifenCILGLL-------LNNKTRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-217 |
1.38e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 75.70 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIsdininddieayRRKLSYIPESPVIYEELTLEEHIE 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI------------KGSAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 98 MTAMAYDIDRdEAMNRAMPLLKTFRLENELKVFP-SHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLM 176
Cdd:PRK13545 108 LKGLMMGLTK-EKIKEIIPEIIEFADIGKFIYQPvKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446139018 177 VEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDL 217
Cdd:PRK13545 187 NEFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDI 227
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
3-215 |
1.39e-15 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 74.78 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYG--KRP--VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLT-P---MEGSLSISDININDDIEAYR 74
Cdd:PRK11022 4 LNVDKLSVHFGdeSAPfrAVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKER 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 75 RKLSYiPESPVIYEEltleehiEMTAM------AYDI----------DRDEAMNRAMPLLKTFRL---ENELKVFPSHFS 135
Cdd:PRK11022 84 RNLVG-AEVAMIFQD-------PMTSLnpcytvGFQImeaikvhqggNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 136 KGMKQKVMIICAFIVNPELYIIDEPFLGLDpLGIQS-MLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:PRK11022 156 GGMSQRVMIAMAIACRPKLLIADEPTTALD-VTIQAqIIELLLElQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVE 234
|
..
gi 446139018 214 FG 215
Cdd:PRK11022 235 TG 236
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
15-212 |
1.51e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 73.58 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYR-RKLSYIPESPVI--YEELT 91
Cdd:COG1101 19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRaKYIGRVFQDPMMgtAPSMT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEHIemtAMAYdiDRDEAMNRAMPLLKTFR-------------LENELKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:COG1101 99 IEENL---ALAY--RRGKRRGLRRGLTKKRRelfrellatlglgLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLLD 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 159 EPFLGLDPLGIQSMLDL---MVEKKNegRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:COG1101 174 EHTAALDPKTAALVLELtekIVEENN--LTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
15-220 |
3.65e-15 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 72.42 E-value: 3.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP----MEGSLSISDININDdiEAYR-RKLSYI---PES--- 83
Cdd:PRK10418 16 QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAP--CALRgRKIATImqnPRSafn 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 PViyeeLTLEEHIEMTAMAYDIDRDEAmnRAMPLLKTFRLENE---LKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:PRK10418 94 PL----HTMHTHARETCLALGKPADDA--TLTAALEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 161 FLGLDPLGIQSMLDLM---VEKKNEGrtVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK10418 168 TTDLDVVAQARILDLLesiVQKRALG--MLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETL 228
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-218 |
3.98e-15 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 72.54 E-value: 3.98e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLS----ISDININDDIEAyrrklsyipespviyeELTLE 93
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDrngeVSVIAISAGLSG----------------QLTGI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 94 EHIEMTAMAYDIDRDEaMNRAMPLLKTFRLENELKVFP-SHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSM 172
Cdd:PRK13546 104 ENIEFKMLCMGFKRKE-IKAMTPKIIEFSELGEFIYQPvKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKC 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446139018 173 LDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:PRK13546 183 LDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELD 228
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-235 |
6.76e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 6.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 28 GEIVGLIGLNGAGKSTTIKhMLGL-LTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYEELTLEEHIEMT------ 99
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLK-MLGRhQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVAIGrypwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 100 AMA-YDIDRDEAMNRAMPL--LKTF--RLENELkvfpshfSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLD 174
Cdd:PRK10575 116 ALGrFGAADREKVEEAISLvgLKPLahRLVDSL-------SGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 175 LMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQTglhkqTLDDIY 235
Cdd:PRK10575 189 LVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGE-----TLEQIY 245
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
5-225 |
8.05e-15 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 73.32 E-value: 8.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGYGKR--PVIKDINFELNKGEIVGLIGLNGAGKSTtikhMLGLLT----PMEGSLSISDININD-DIEAYRRKL 77
Cdd:PRK11160 341 LNNVSFTYPDQpqPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTrawdPQQGEILLNGQPIADySEAALRQAI 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVIYEElTLEEHIemtAMAYDIDRDEAMNRAmplLKTFRLENELKVFPS----------HFSKGMKQKVMIICA 147
Cdd:PRK11160 417 SVVSQRVHLFSA-TLRDNL---LLAAPNASDEALIEV---LQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRRLGIARA 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 148 FIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKnEGRTVLMSTHILATAERYcDRFIILDEGEVVAFGDLEALRQQTG 225
Cdd:PRK11160 490 LLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLAQQG 565
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-165 |
1.00e-14 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 72.42 E-value: 1.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDdIEAYRRKLSYI 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-LHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIemtamAYDID---RDEAMNRA------MPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVN 151
Cdd:PRK10851 80 FQHYALFRHMTVFDNI-----AFGLTvlpRRERPNAAaikakvTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170
....*....|....
gi 446139018 152 PELYIIDEPFLGLD 165
Cdd:PRK10851 155 PQILLLDEPFGALD 168
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-215 |
1.53e-14 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 70.94 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ-DDIEAYRRKLSYIPESP--------VIYE 88
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITdDNFEKLRKHIGIVFQNPdnqfvgsiVKYD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 89 -ELTLEEHiemtAMAYDidrdeAMNRAMP-LLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP 166
Cdd:PRK13648 105 vAFGLENH----AVPYD-----EMHRRVSeALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446139018 167 LGIQSMLDLMVEKKNEGRTVLMS-THILATAERyCDRFIILDEGEVVAFG 215
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTVYKEG 224
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
17-220 |
2.78e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 71.66 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLtPMEGSLSISDININD----DIEAYRRKLSYIPESP-------- 84
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDGQPLHNlnrrQLLPVRHRIQVVFQDPnsslnprl 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 85 ----VIYEELTLEeHIEMTAMAydidRDEAMNRAMpllKTFRLENELKV-FPSHFSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:PRK15134 380 nvlqIIEEGLRVH-QPTLSAAQ----REQQVIAVM---EEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 160 PFLGLDPLGIQSMLDLMVEKKNEGR-TVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
13-225 |
2.95e-14 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 71.53 E-value: 2.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIkhmlGLL----TPMEGSLSISDININD-DIEAYRRKLSYIPESPVIY 87
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLqrvfDPQSGRILIDGTDIRTvTRASLRRNIAVVFQDAGLF 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 EElTLEEHIEM-TAMAYDIDRDEAMNRAMPLLKTFRLENELKVFP----SHFSKGMKQKVMIICAFIVNPELYIIDEPfl 162
Cdd:PRK13657 422 NR-SIEDNIRVgRPDATDEEMRAAAERAQAHDFIERKPDGYDTVVgergRQLSGGERQRLAIARALLKDPPILILDEA-- 498
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 163 gldplgiQSMLDLMVEKK--------NEGRTVLMSTHILATAeRYCDRFIILDEGEVVAFGDLEALRQQTG 225
Cdd:PRK13657 499 -------TSALDVETEAKvkaaldelMKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDELVARGG 561
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-201 |
3.55e-14 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 69.81 E-value: 3.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIK--HMLGLLTP---MEGSLSISDININD---DIEAYR 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfNRLNDLIPgfrVEGKVTFHGKNLYApdvDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 75 RKLSYIPESP-----VIYEELTLEEHIEmtamAYDIDRDEAMNRAmplLKTFRLENE----LKVFPSHFSKGMKQKVMII 145
Cdd:PRK14243 91 RRIGMVFQKPnpfpkSIYDNIAYGARIN----GYKGDMDELVERS---LRQAALWDEvkdkLKQSGLSLSGGQQQRLCIA 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 146 CAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKnEGRTVLMSTHILATAERYCD 201
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSD 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-218 |
4.08e-14 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 71.42 E-value: 4.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD----------ININDDIEAYRRK-----LSYI 80
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrgadMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPV--IYEELTLEEHI-EMTAMAYDIDRDEAMNRAMPLLKTFRL---ENELKVFPSHFSKGMKQKVMIICAFIVNPEL 154
Cdd:PRK10261 110 FQEPMtsLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIpeaQTILSRYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 155 YIIDEPFLGLDpLGIQS-MLDLM-VEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:PRK10261 190 LIADEPTTALD-VTIQAqILQLIkVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVE 254
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-221 |
4.83e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 71.09 E-value: 4.83e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininddieayrrKLSYIPESPVIYEElTLEEH 95
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 96 IeMTAMAYDidrdeaMNRAMPLLKTFRLENELKVFPSH-----------FSKGMKQKVMIICAFIVNPELYIIDEPFlgl 164
Cdd:TIGR01271 507 I-IFGLSYD------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPF--- 576
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 165 dplgiqSMLDLMVEKKNEGRTV--LMS--THILATAE----RYCDRFIILDEGEVV---AFGDLEALR 221
Cdd:TIGR01271 577 ------THLDVVTEKEIFESCLckLMSnkTRILVTSKlehlKKADKILLLHEGVCYfygTFSELQAKR 638
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-229 |
7.78e-14 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 70.43 E-value: 7.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGY-GK-RPVIKDINFELNKGEIVGLIGLNGAGKSTtikhMLGLLTP----MEGSLSISDININD-DIEAYRR 75
Cdd:PRK11176 342 IEFRNVTFTYpGKeVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRDyTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 76 KLSYIPESPVIY-------------EELTLEEHIEMTAMAYDIDRDEAMNRAmplLKTFRLENELKVfpshfSKGMKQKV 142
Cdd:PRK11176 418 QVALVSQNVHLFndtianniayartEQYSREQIEEAARMAYAMDFINKMDNG---LDTVIGENGVLL-----SGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 143 MIICAFIVNPELYIIDEPFLGLD---PLGIQSMLDLMveKKNegRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEA 219
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDtesERAIQAALDEL--QKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
250
....*....|
gi 446139018 220 LRQQTGLHKQ 229
Cdd:PRK11176 565 LLAQNGVYAQ 574
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-218 |
1.18e-13 |
|
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: 69.83 E-value: 1.18e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYG--KRPVIK---DINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLsisDININDD-------- 69
Cdd:TIGR03269 280 IKVRNVSKRYIsvDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEV---NVRVGDEwvdmtkpg 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 70 IEAYRRKLSYIpesPVIYEELTLEEHIEM-----TAMAYDIDRDEAMNRAMPLLKTFRLENE-----LKVFPSHFSKGMK 139
Cdd:TIGR03269 357 PDGRGRAKRYI---GILHQEYDLYPHRTVldnltEAIGLELPDELARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGER 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 140 QKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:TIGR03269 434 HRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEmEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-211 |
1.60e-13 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 68.22 E-value: 1.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGK---RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIS-DININDDIEAYRRKLS 78
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgDLLTEENVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESP-VIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAErYCDRFIILDEGEV 211
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGiRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
16-220 |
1.68e-13 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 69.62 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYEElTLEE 94
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKfGLTDLRRVLSIIPQSPVLFSG-TVRF 1328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIEMTAMAYDIDRDEAMNRAMplLK------TFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDpLG 168
Cdd:PLN03232 1329 NIDPFSEHNDADLWEALERAH--IKdvidrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD-VR 1405
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446139018 169 IQSMLDLMVEKKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEAL 220
Cdd:PLN03232 1406 TDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQEL 1456
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-231 |
1.73e-13 |
|
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: 69.55 E-value: 1.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKveQLTGGY--GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTpMEGSLSISDININD-DIEAYRRKL 77
Cdd:TIGR01271 1218 MDVQ--GLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVI-----------YEELTLEEHIEMTamaydidrDEAMNRAM----PLLKTFRLENELKVFpshfSKGMKQKV 142
Cdd:TIGR01271 1295 GVIPQKVFIfsgtfrknldpYEQWSDEEIWKVA--------EEVGLKSVieqfPDKLDFVLVDGGYVL----SNGHKQLM 1362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 143 MIICAFIVNPELYIIDEPFLGLDPLGIQsMLDLMVEKKNEGRTVLMSTH-ILATAEryCDRFIILDEGEVVAFGDLEALR 221
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQ-IIRKTLKQSFSNCTVILSEHrVEALLE--CQQFLVIEGSSVKQYDSIQKLL 1439
|
250
....*....|
gi 446139018 222 QQTGLHKQTL 231
Cdd:TIGR01271 1440 NETSLFKQAM 1449
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-216 |
2.96e-13 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 67.37 E-value: 2.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGL--LTP---MEGSLSISDININD---DIEAYR 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYDpdvDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 75 RKLSYIPESPV-----IYEELT-------------LEEHIEmtamaydidrdEAMNRAMpllktfrLENE----LKVFPS 132
Cdd:COG1117 92 RRVGMVFQKPNpfpksIYDNVAyglrlhgikskseLDEIVE-----------ESLRKAA-------LWDEvkdrLKKSAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 133 HFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEgRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:COG1117 154 GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELV 232
|
....
gi 446139018 213 AFGD 216
Cdd:COG1117 233 EFGP 236
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
18-215 |
3.24e-13 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 68.54 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPmeGSLSISDININD---DIEAYRRKLSYIPESPVIYEELTLEE 94
Cdd:TIGR00955 41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPK--GVKGSGSVLLNGmpiDAKEMRAISAYVQQDDLFIPTLTVRE 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIEMTA---MAYDIDRDEAMNRAMPLLKTFRL----------ENELKVFpshfSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:TIGR00955 119 HLMFQAhlrMPRRVTKKEKRERVDEVLQALGLrkcantrigvPGRVKGL----SGGERKRLAFASELLTDPPLLFCDEPT 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 162 LGLDPLGIQSMLDLMVEKKNEGRTVLMSTHiLATAERYC--DRFIILDEGEVVAFG 215
Cdd:TIGR00955 195 SGLDSFMAYSVVQVLKGLAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLG 249
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-231 |
3.25e-13 |
|
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.
Pssm-ID: 213256 [Multi-domain] Cd Length: 275 Bit Score: 67.57 E-value: 3.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKveQLTGGY--GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTpMEGSLSISDININD-DIEAYRRKL 77
Cdd:cd03289 3 MTVK--DLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSvPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVIYEElTLEEHIEmtamAYDIDRDEAMNRampLLKTFRLENELKVFPSH-----------FSKGMKQKVMIIC 146
Cdd:cd03289 80 GVIPQKVFIFSG-TFRKNLD----PYGKWSDEEIWK---VAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLAR 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 147 AFIVNPELYIIDEPFLGLDPLGIQsMLDLMVEKKNEGRTVLMSTHILaTAERYCDRFIILDEGEVVAFGDLEALRQQTGL 226
Cdd:cd03289 152 SVLSKAKILLLDEPSAHLDPITYQ-VIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNEKSH 229
|
....*
gi 446139018 227 HKQTL 231
Cdd:cd03289 230 FKQAI 234
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-215 |
4.17e-13 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 66.88 E-value: 4.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 21 INFELNKGEIVGLIGLNGAGKSTTIKHMLGLLtPMEGSLSISDININD----DIEAYRRKLSYiPESPVI------YEEL 90
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAwsaaELARHRAYLSQ-QQTPPFampvfqYLTL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 91 TLEEHIEMTAMAYDIDRdeamnrampLLKTFRLENELKVFPSHFSKGMKQKVMIICAFI-----VNPE--LYIIDEPFLG 163
Cdd:PRK03695 93 HQPDKTRTEAVASALNE---------VAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLLDEPMNS 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446139018 164 LDpLGIQSMLD-LMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK03695 164 LD-VAQQAALDrLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-234 |
4.50e-13 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 66.72 E-value: 4.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHM--LGLLTP---MEGSLSISDINI---NDDIEAYR 74
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIyspRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 75 RKLSYIPESP-----VIYEEL-------------TLEEHIEMT---AMAYDIDRDEAMNRAMPLlktfrlenelkvfpsh 133
Cdd:PRK14239 86 KEIGMVFQQPnpfpmSIYENVvyglrlkgikdkqVLDEAVEKSlkgASIWDEVKDRLHDSALGL---------------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 134 fSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEgRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:PRK14239 150 -SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIE 227
|
250 260
....*....|....*....|.
gi 446139018 214 FGDLEALRQQTGlHKQTLDDI 234
Cdd:PRK14239 228 YNDTKQMFMNPK-HKETEDYI 247
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
14-220 |
4.81e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 67.96 E-value: 4.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 14 KRPV--IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD----DIEAYRRKLSYIPESPviY 87
Cdd:PRK10261 334 TREVhaVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQDP--Y 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 EELTLEEHIEMTAMA-----YDIDRDEAMNRAMPLLKTFRLENELKV-FPSHFSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:PRK10261 412 ASLDPRQTVGDSIMEplrvhGLLPGKAAAARVAWLLERVGLLPEHAWrYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 162 LGLDPLGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-220 |
5.09e-13 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 67.42 E-value: 5.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSI--SDININDDIE--AYRRKLSYIPESPV--IYEELT 91
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWlgKDLLGMKDDEwrAVRSDIQMIFQDPLasLNPRMT 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LEEHIEMTAMAY--DIDRDEAMNR--AMpLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDpL 167
Cdd:PRK15079 117 IGEIIAEPLRTYhpKLSRQEVKDRvkAM-MLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD-V 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 168 GIQS-MLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK15079 195 SIQAqVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEV 249
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
12-221 |
5.30e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 5.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ--DDIEAYRRKLSYIPESPVIYEE 89
Cdd:PRK15439 21 YSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCArlTPAKAHQLGIYLVPQEPLLFPN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 90 LTLEEHIemtamAYDIDRDEAMNRampllktfRLENELKVFPSHFSKGMK---------QKVMIICAFIVNPELYIIDEP 160
Cdd:PRK15439 101 LSVKENI-----LFGLPKRQASMQ--------KMKQLLAALGCQLDLDSSagslevadrQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 161 FLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALR 221
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLS 228
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-63 |
9.41e-13 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 67.27 E-value: 9.41e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD 63
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGE 383
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-213 |
9.58e-13 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 67.12 E-value: 9.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRpvIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIS--DININDDIEAYRRKLSYIP 81
Cdd:PRK09700 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNgkDISPRSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPV---IYEELTLEEHIEMT----------AMAYDIDRDEAM----NRAMPLLKTFRLENELkvfpSHFSKGMKQKVMI 144
Cdd:PRK09700 345 ESRRdngFFPNFSIAQNMAISrslkdggykgAMGLFHEVDEQRtaenQRELLALKCHSVNQNI----TELSGGNQQKVLI 420
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 145 ICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQ 489
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-207 |
9.93e-13 |
|
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 65.51 E-value: 9.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 24 ELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGslsisdinindDIEAYRRKLSYIPEspviyeelTLEEHIEMT--AM 101
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEG-----------DIEIELDTVSYKPQ--------YIKADYEGTvrDL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 102 AYDIDRD---------EAMNramPLLKTFRLENELkvfpSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDplgiqSM 172
Cdd:cd03237 82 LSSITKDfythpyfktEIAK---PLQIEQILDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLD-----VE 149
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 446139018 173 LDLMVEK------KNEGRTVLMSTHILATAERYCDRFIILD 207
Cdd:cd03237 150 QRLMASKvirrfaENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-222 |
1.27e-12 |
|
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: 64.47 E-value: 1.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGL--LTPMEGSLSISDININdDIEAYRRKLSYI- 80
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDIT-DLPPEERARLGIf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 --PESPVIYEELTLEEHIemtamaydidrdeamnrampllktfRLENElkvfpsHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:cd03217 81 laFQYPPEIPGVKNADFL-------------------------RYVNE------GFSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 159 EPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTH---ILATAERycDRFIILDEGEVVAFGDLEALRQ 222
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqrLLDYIKP--DRVHVLYDGRIVKSGDKELALE 194
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-211 |
1.31e-12 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 66.51 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININdDIEAYRRKLSYIPE 82
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIT-HVPAENRHVNTVFQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:PRK09452 94 SYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446139018 163 GLD-PLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:PRK09452 174 ALDyKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-223 |
1.57e-12 |
|
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: 65.65 E-value: 1.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininddieayrrKLSYIPESPVIYEElTLEEH 95
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 96 IeMTAMAYDidrdeaMNRAMPLLKTFRLENELKVFPSH-----------FSKGMKQKVMIICAFIVNPELYIIDEPFLGL 164
Cdd:cd03291 118 I-IFGVSYD------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 165 DPLGIQSMLDLMVEKknegrtvLMS--THILATAE----RYCDRFIILDEGEVVAFGDLEALRQQ 223
Cdd:cd03291 191 DVFTEKEIFESCVCK-------LMAnkTRILVTSKmehlKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-220 |
1.68e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 66.47 E-value: 1.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD-----ININDDIEAyrrklsyipESPVIYEELTLEE 94
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTAALAA---------GVAIIYQELHLVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 hiEMTAM-----------AYDIDRDEAMNRAMPLLKTF--RLENELKVfpSHFSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:PRK11288 93 --EMTVAenlylgqlphkGGIVNRRLLNYEAREQLEHLgvDIDPDTPL--KYLSIGQRQMVEIAKALARNARVIAFDEPT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 162 LGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA-FGDLEAL 220
Cdd:PRK11288 169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVAtFDDMAQV 228
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-215 |
2.14e-12 |
|
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: 63.82 E-value: 2.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 11 GYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP---MEGSLSISDININDDIEAYRRKLSYIPESPVIY 87
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGnvsVEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 EELTLEEHIEmtamaydidrdeamnrampllktFRLE---NElkvFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGL 164
Cdd:cd03233 96 PTLTVRETLD-----------------------FALRckgNE---FVRGISGGERKRVSIAEALVSRASVLCWDNSTRGL 149
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 165 DP---LGIQSMLDLMVekKNEGRTVLMSthILATAERYCDRF---IILDEGEVVAFG 215
Cdd:cd03233 150 DSstaLEILKCIRTMA--DVLKTTTFVS--LYQASDEIYDLFdkvLVLYEGRQIYYG 202
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
8-220 |
2.58e-12 |
|
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: 65.62 E-value: 2.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 8 LTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLT--PMEGSL--SISDININDDIEAYRRKLSYIPES 83
Cdd:TIGR02633 7 IVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIywSGSPLKASNIRDTERAGIVIIHQE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 PVIYEELTLEEHI----EMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFP-SHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:TIGR02633 87 LTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQARLLILD 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 159 EPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:TIGR02633 167 EPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTM 228
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
15-212 |
2.77e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 65.88 E-value: 2.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDD--IEAYRRKLSYIPESPV--IYEE- 89
Cdd:PRK15134 22 RTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPPVVYPSGDIRFHGEslLHASEQTLRGVRGNKIamIFQEp 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 90 -------LTLEEHI-EMTAMAYDIDRDEAMNRAMPLLKTFRLEN---ELKVFPSHFSKGMKQKVMIICAFIVNPELYIID 158
Cdd:PRK15134 102 mvslnplHTLEKQLyEVLSLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALLTRPELLIAD 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 159 EPFLGLDpLGIQS-MLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:PRK15134 182 EPTTALD-VSVQAqILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCV 236
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
13-233 |
2.88e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.91 E-value: 2.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIsdininddieaYRRKLSYIPESPVIYEElTL 92
Cdd:PLN03130 628 AERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV-----------IRGTVAYVPQVSWIFNA-TV 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 93 EEHIeMTAMAYDIDRdeaMNRAmplLKTFRLENELKVFPSH-----------FSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:PLN03130 696 RDNI-LFGSPFDPER---YERA---IDVTALQHDLDLLPGGdlteigergvnISGGQKQRVSMARAVYSNSDVYIFDDPL 768
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 162 LGLDPLGIQSMLDLMVEKKNEGRTVLMST---HILAtaerYCDRFIILDEGEVVAFGDLEALRQQTGLHKQTLDD 233
Cdd:PLN03130 769 SALDAHVGRQVFDKCIKDELRGKTRVLVTnqlHFLS----QVDRIILVHEGMIKEEGTYEELSNNGPLFQKLMEN 839
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-222 |
2.97e-12 |
|
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: 65.59 E-value: 2.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 21 INFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDD-IEAYRRKLSyipespVIYEELTLEEHIemt 99
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADnREAYRQLFS------AVFSDFHLFDRL--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 100 amaYDIDRDEAMNRAMPLLKTFRLENELKVFPSHF-----SKGMKQKVMIICAFIVNPELYIIDE------P-----Flg 163
Cdd:COG4615 422 ---LGLDGEADPARARELLERLELDHKVSVEDGRFsttdlSQGQRKRLALLVALLEDRPILVFDEwaadqdPefrrvF-- 496
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 164 ldplgiqsMLDLMVEKKNEGRTVLMSTHilatAERY---CDRFIILDEGEVVAFGDLEALRQ 222
Cdd:COG4615 497 --------YTELLPELKARGKTVIAISH----DDRYfdlADRVLKMDYGKLVELTGPAALAA 546
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-191 |
3.13e-12 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 63.65 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP---MEGSLSISDINInDDIEAYRRKLSYI 80
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-TALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMtAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:COG4136 82 FQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190
....*....|....*....|....*....|..
gi 446139018 161 FLGLDPLGIQSMLDLMVEK-KNEGRTVLMSTH 191
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQiRQRGIPALLVTH 192
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
4.33e-12 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 63.78 E-value: 4.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIK--HMLGLLTP---MEGSLSISDINI-NDDIEAYRRK 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRvfNRLIELYPearVSGEVYLDGQDIfKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 77 LSYIPESPVIYEELTLEEHIemtAMAYDIDR-----DEAMNRAMPLLKTFRLENELK----VFPSHFSKGMKQKVMIICA 147
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENV---ALGLKLNRlvkskKELQERVRWALEKAQLWDEVKdrldAPAGKLSGGQQQRLCIARA 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 148 FIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEgRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG 227
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-223 |
6.23e-12 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 64.36 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEayRRKLSYIP 81
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrSIQ--QRDICMVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:PRK11432 85 QSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 162 LGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQ 223
Cdd:PRK11432 165 SNLDANLRRSMREKIRElQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQ 227
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-213 |
1.20e-11 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 63.89 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLT-GGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDINI-NDDIEAYRRK-LSYI 80
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItGLSPRERRRLgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESP-----VIyeELTLEEHIEMTamAYD---------IDRDEAMNRAMPLLKTF--RLEN-ELKVfpSHFSKGMKQKVM 143
Cdd:COG3845 339 PEDRlgrglVP--DMSVAENLILG--RYRrppfsrggfLDRKAIRAFAEELIEEFdvRTPGpDTPA--RSLSGGNQQKVI 412
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 144 IICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLmsthiLATAE-----RYCDRFIILDEGEVVA 213
Cdd:COG3845 413 LARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVL-----LISEDldeilALSDRIAVMYEGRIVG 482
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-215 |
1.39e-11 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 62.50 E-value: 1.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYR-RKLSYIPESPV--------IYE 88
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRsQRIRMIFQDPStslnprqrISQ 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 89 --ELTLEEHIEMTAMAydidRDEAMNRAmpLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP 166
Cdd:PRK15112 109 ilDFPLRLNTDLEPEQ----REKQIIET--LRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDM 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446139018 167 LGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK15112 183 SMRSQLINLMLElQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERG 232
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-220 |
1.93e-11 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 63.60 E-value: 1.93e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYE---ELT 91
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKfGLMDLRKVLGIIPQAPVLFSgtvRFN 1332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 92 LE---EHiemtamaYDIDRDEAMNRAMplLK------TFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:PLN03130 1333 LDpfnEH-------NDADLWESLERAH--LKdvirrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 163 GLDpLGIQSMLDLMVEKKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEAL 220
Cdd:PLN03130 1404 AVD-VRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-63 |
2.93e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.83 E-value: 2.93e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD 63
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE 385
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-218 |
3.00e-11 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 62.20 E-value: 3.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDD-----IEAYRRKLSYIpespviYEELTLEE 94
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAekgicLPPEKRRIGYV------FQDARLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIEMTA-MAYdidrdeAMNRAMP-----LLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDplg 168
Cdd:PRK11144 90 HYKVRGnLRY------GMAKSMVaqfdkIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD--- 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 169 iqsmldlmVEKKNE--------GRTV----LMSTHILATAERYCDRFIILDEGEVVAFGDLE 218
Cdd:PRK11144 161 --------LPRKREllpylerlAREInipiLYVSHSLDEILRLADRVVVLEQGKVKAFGPLE 214
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-211 |
4.27e-11 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 62.33 E-value: 4.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGgygkrPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIS--DININDDIEAYRRKLSYIP 81
Cdd:PRK10762 259 KVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDghEVVTRSPQDGLANGIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESP-----VIyeELTLEEHIEMTAMAY------DIDRDEAMNRAMPLLKTFRLENelkvfPSH------FSKGMKQKVMI 144
Cdd:PRK10762 334 EDRkrdglVL--GMSVKENMSLTALRYfsraggSLKHADEQQAVSDFIRLFNIKT-----PSMeqaiglLSGGNQQKVAI 406
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446139018 145 ICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGrtvlMSThILATAER-----YCDRFIILDEGEV 211
Cdd:PRK10762 407 ARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG----LSI-ILVSSEMpevlgMSDRILVMHEGRI 473
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
15-225 |
6.00e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.65 E-value: 6.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSYIPESPVIYEElTLE 93
Cdd:PRK10789 328 HPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQTPFLFSD-TVA 406
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 94 EHIEM---TAMAYDIdrDEAMNRAMPLLKTFRL----ENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP 166
Cdd:PRK10789 407 NNIALgrpDATQQEI--EHVARLASVHDDILRLpqgyDTEVGERGVMLSGGQKQRISIARALLLNAEILILDDALSAVDG 484
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 167 LGIQSMLDlMVEKKNEGRTVLMSTHILaTAERYCDRFIILDEGEVVAFGDLEALRQQTG 225
Cdd:PRK10789 485 RTEHQILH-NLRQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHDQLAQQSG 541
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-211 |
6.13e-11 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 60.18 E-value: 6.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 28 GEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYRRKL-----SYIPESPVIYEELTLEEHIEMTAMA 102
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLrakhvGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 103 YDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKN 181
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSlNRE 195
|
170 180 190
....*....|....*....|....*....|
gi 446139018 182 EGRTVLMSTHILATAERyCDRFIILDEGEV 211
Cdd:PRK10584 196 HGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-211 |
7.28e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 61.61 E-value: 7.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTG-GYgkrpviKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYR--RKLSYI 80
Cdd:PRK15439 270 TVEDLTGeGF------RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlaRGLVYL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PE----------SPVIYEELTLEEHiEM---TAMAYDIDRDEAMNRAMPlLKTFRLENELKVfpshFSKGMKQKVMIICA 147
Cdd:PRK15439 344 PEdrqssglyldAPLAWNVCALTHN-RRgfwIKPARENAVLERYRRALN-IKFNHAEQAART----LSGGNQQKVLIAKC 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 148 FIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:PRK15439 418 LEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-220 |
8.01e-11 |
|
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: 61.24 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 19 KDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLtPMEGSLSISDININD----DIEAYRRKL---------SYipeSPv 85
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGlsrrALRPLRRRMqvvfqdpfgSL---SP- 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 86 iyeELTLEEHIE--MTAMAYDIDRDEAMNRAMPLLKTFRLENE-LKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:COG4172 378 ---RMTVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLDPAaRHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 163 GLDpLGIQS-MLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:COG4172 455 ALD-VSVQAqILDLLRDlQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
18-191 |
1.28e-10 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 59.98 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIvgLIGLNGAGKSTTIKHMLGLL----------------TPMEGSLSISDININDD-----IEAYRRK 76
Cdd:COG4938 12 FKEAELELKPLTL--LIGPNGSGKSTLIQALLLLLqsnfiylpaersgparLYPSLVRELSDLGSRGEytadfLAELENL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 77 LSYIPESPVIYEELT--LEEHIEmTAMAYDIDRDEamnramPLLKTFRLENELKVFPSHFSKGMKQKVMII--CAFIVNP 152
Cdd:COG4938 90 EILDDKSKELLEQVEewLEKIFP-GKVEVDASSDL------VRLVFRPSGNGKRIPLSNVGSGVSELLPILlaLLSAAKP 162
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 446139018 153 -ELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTH 191
Cdd:COG4938 163 gSLLIIEEPEAHLHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-225 |
1.53e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 60.73 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIsdininddieayRRKLSYI 80
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHM------------KGSVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIyEELTLEEHIeMTAMAYDIDRDEAMNRAMPLLKtfrlenELKVFPS-----------HFSKGMKQKVMIICAFI 149
Cdd:TIGR00957 705 PQQAWI-QNDSLRENI-LFGKALNEKYYQQVLEACALLP------DLEILPSgdrteigekgvNLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 150 VNPELYIIDEPFLGLDPLGIQSMLDLMVEKKN--EGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQTG 225
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQRDG 853
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
20-220 |
2.07e-10 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 59.59 E-value: 2.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKStTIKHMLGLL-TPMEGSLSISDINI----NDDIEAYRRKLSYIPESPviYEEL---- 90
Cdd:PRK11308 33 GVSFTLERGKTLAVVGESGCGKS-TLARLLTMIeTPTGGELYYQGQDLlkadPEAQKLLRQKIQIVFQNP--YGSLnprk 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 91 ----TLEEHIEMTAmayDIDRDEAMNRAMPLLKTFRLENE-LKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLD 165
Cdd:PRK11308 110 kvgqILEEPLLINT---SLSAAERREKALAMMAKVGLRPEhYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALD 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 166 pLGIQS-MLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK11308 187 -VSVQAqVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQI 242
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-211 |
3.03e-10 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 59.74 E-value: 3.03e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 1 MTVKVEQLTGGygKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ--DDIEAYRRKLS 78
Cdd:PRK10982 249 VILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhNANEAINHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPE---SPVIYEELTleehIEMTAMAYDIDRdeaMNRAMPLLKTFRLENELKVF--------PSH------FSKGMKQK 141
Cdd:PRK10982 327 LVTEerrSTGIYAYLD----IGFNSLISNIRN---YKNKVGLLDNSRMKSDTQWVidsmrvktPGHrtqigsLSGGNQQK 399
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 142 VMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:PRK10982 400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-229 |
3.38e-10 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 59.80 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGslsisDININDDIeayrrKLSYIPE 82
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSG-----EIGLAKGI-----KLGYFAQ 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 83 SPVIYeeltleehiemtamaydIDRDEAMNRAMPLLKTFRLENELKVF--------------PSHFSKGmkQKVMIICAF 148
Cdd:PRK10636 383 HQLEF-----------------LRADESPLQHLARLAPQELEQKLRDYlggfgfqgdkvteeTRRFSGG--EKARLVLAL 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 149 IV--NPELYIIDEPFLGLDPLGIQSMLDLMVEkkNEGRTVLMS--THILATAErycDRFIILDEGEVVAF-GDLEALRQQ 223
Cdd:PRK10636 444 IVwqRPNLLLLDEPTNHLDLDMRQALTEALID--FEGALVVVShdRHLLRSTT---DDLYLVHDGKVEPFdGDLEDYQQW 518
|
....*..
gi 446139018 224 -TGLHKQ 229
Cdd:PRK10636 519 lSDVQKQ 525
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
8-220 |
4.61e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 58.57 E-value: 4.61e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 8 LTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-------DIEAYRRKLSYI 80
Cdd:PRK14271 27 LTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGrsifnyrDVLEFRRRVGML 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRL----ENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:PRK14271 107 FQRPNPFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLL 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 157 IDEPFLGLDPLGIQSmLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK14271 187 LDEPTSALDPTTTEK-IEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-215 |
7.60e-10 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 57.75 E-value: 7.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSI--------SDININDDIEaYRRKLSYIPESPVI 86
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVdgkvlyfgKDIFQIDAIK-LRKEVGMVFQQPNP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 87 YEELTLEEHIEMTAMAYDIDRDEAMNRAMP-LLKTFRLENE----LKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPF 161
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKEKREIKKIVEeCLRKVGLWKEvydrLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 162 LGLDPLGIQSMLDLMVEKKNEGRTVLMStHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVADYVAFLYNGELVEWG 234
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
17-191 |
8.28e-10 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 56.80 E-value: 8.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAYrrkLSYIPESPVIYEELTLEEHI 96
Cdd:PRK13541 15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIGHNLGLKLEMTVFENL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 97 EMTAMAYdiDRDEAMNRAmplLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLM 176
Cdd:PRK13541 92 KFWSEIY--NSAETLYAA---IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
|
170
....*....|....*
gi 446139018 177 VEKKNEGRTVLMSTH 191
Cdd:PRK13541 167 VMKANSGGIVLLSSH 181
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
14-213 |
1.45e-09 |
|
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: 57.53 E-value: 1.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 14 KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLT-PMEGSLSIS--DININDDIEAYRRKLSYIPESPV---IY 87
Cdd:TIGR02633 272 HRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINgkPVDIRNPAQAIRAGIAMVPEDRKrhgIV 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 EELTLEEHIEMTAMAY--------DIDRDEAMNRAMPLLKTFRLENELKVfpSHFSKGMKQKVMIICAFIVNPELYIIDE 159
Cdd:TIGR02633 352 PILGVGKNITLSVLKSfcfkmridAAAELQIIGSAIQRLKVKTASPFLPI--GRLSGGNQQKAVLAKMLLTNPRVLILDE 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 160 PFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-174 |
1.58e-09 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 56.26 E-value: 1.58e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDininDDI-----EAYRRKLSYIPESPV-- 85
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG----EDIstlkpEIYRQQVSYCAQTPTlf 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 86 ---IYEELTL-----EEHIEMTAMAYDIDRdeamnrampllktFRL-ENELKVFPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:PRK10247 94 gdtVYDNLIFpwqirNQQPDPAIFLDDLER-------------FALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160
|
170
....*....|....*...
gi 446139018 157 IDEpflgldplgIQSMLD 174
Cdd:PRK10247 161 LDE---------ITSALD 169
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-226 |
2.03e-09 |
|
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: 57.14 E-value: 2.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:COG5265 357 EVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEElTLEEHIemtamAY---DIDRDEAMNRA-MPLLKTF--RL---------ENELKVfpshfSKGMKQKVMI 144
Cdd:COG5265 437 VPQDTVLFND-TIAYNI-----AYgrpDASEEEVEAAArAAQIHDFieSLpdgydtrvgERGLKL-----SGGEKQRVAI 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 145 ICAFIVNPELYIIDEPFLGLDP---LGIQSMLDLMvekkNEGRTVLMSTHILATAeRYCDRFIILDEGEVVAFGDLEALR 221
Cdd:COG5265 506 ARTLLKNPPILIFDEATSALDSrteRAIQAALREV----ARGRTTLVIAHRLSTI-VDADEILVLEAGRIVERGTHAELL 580
|
....*
gi 446139018 222 QQTGL 226
Cdd:COG5265 581 AQGGL 585
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
4-215 |
2.47e-09 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 57.20 E-value: 2.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLL--TPMEGSLSISDININDDIeayRRKLSYIP 81
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIqgNNFTGTILANNRKPTKQI---LKRTGFVT 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPVIYEELTLEEHIEMTAM---AYDIDRDEAMNRAMPLLKTFRL---ENEL--KVFPSHFSKGMKQKVMIICAFIVNPE 153
Cdd:PLN03211 147 QDDILYPHLTVRETLVFCSLlrlPKSLTKQEKILVAESVISELGLtkcENTIigNSFIRGISGGERKRVSIAHEMLINPS 226
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 154 LYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILAT-AERYCDRFIILDEGEVVAFG 215
Cdd:PLN03211 227 LLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSrVYQMFDSVLVLSEGRCLFFG 289
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-63 |
2.59e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.59e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD 63
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSE 380
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
2.68e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 56.20 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKhMLGLLTPMEGSL-----------SISDININddIE 71
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK-CLNRMNELESEVrvegrveffnqNIYERRVN--LN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 72 AYRRKLSYIPESPVIYEELTLEE---HIEMTAMAYDIDRDEAMNRAmplLKTFRLENELK--VFPS--HFSKGMKQKVMI 144
Cdd:PRK14258 85 RLRRQVSMVHPKPNLFPMSVYDNvayGVKIVGWRPKLEIDDIVESA---LKDADLWDEIKhkIHKSalDLSGGQQQRLCI 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 145 ICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGR-TVLMSTHILATAERYCD--RFIILDE---GEVVAFG 215
Cdd:PRK14258 162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSDftAFFKGNEnriGQLVEFG 238
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-165 |
6.49e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 55.59 E-value: 6.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 24 ELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISdininddieayrRKLSYIPESPVIYEELTLEEHIEMTAMAY 103
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------LKISYKPQYIKPDYDGTVEDLLRSITDDL 428
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 104 D---IDRDeamnrampLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLD 165
Cdd:PRK13409 429 GssyYKSE--------IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 485
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
20-213 |
7.04e-09 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 55.71 E-value: 7.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTpmEGSLSiSDININDDieayRRKLSYIPESP-----VIYEELTLEE 94
Cdd:PRK13549 23 NVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYP--HGTYE-GEIIFEGE----ELQASNIRDTEragiaIIHQELALVK 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HI----------EMTAMAYdIDRDEAMNRAMPLLKTFRLE--NELKVfpSHFSKGMKQKVMIICAFIVNPELYIIDEPFL 162
Cdd:PRK13549 96 ELsvleniflgnEITPGGI-MDYDAMYLRAQKLLAQLKLDinPATPV--GNLGLGQQQLVEIAKALNKQARLLILDEPTA 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 446139018 163 GLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:PRK13549 173 SLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
17-210 |
7.84e-09 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.81 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDI-NIND-DIEAYRRKLSYIPESPVIYE------ 88
Cdd:PTZ00265 400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShNLKDiNLKWWRSKIGVVSQDPLLFSnsiknn 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 89 -----------ELTLEEHIEMTAMAYD----------------------IDRDEAM-----------NRAMPLLKTFRLE 124
Cdd:PTZ00265 480 ikyslyslkdlEALSNYYNEDGNDSQEnknkrnscrakcagdlndmsntTDSNELIemrknyqtikdSEVVDVSKKVLIH 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 125 NELKVFP-----------SHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLG---IQSMLDLMveKKNEGRTVLMST 190
Cdd:PTZ00265 560 DFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylVQKTINNL--KGNENRITIIIA 637
|
250 260
....*....|....*....|
gi 446139018 191 HILATAeRYCDRFIILDEGE 210
Cdd:PTZ00265 638 HRLSTI-RYANTIFVLSNRE 656
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
12-188 |
1.46e-08 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 54.64 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 12 YGKRPVIKDINFELNKGEIVGLIGLNGAGKSTtikhMLGLLT---PM------------EGS-LSISDIninddieayRR 75
Cdd:PRK10938 270 YNDRPILHNLSWQVNPGEHWQIVGPNGAGKST----LLSLITgdhPQgysndltlfgrrRGSgETIWDI---------KK 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 76 KLSYIPESpviyeeLTLEEHIEMTAM------------AYDIDRDEAMNRAMPLLKTFRLENELKVFPSH-FSKGMKQKV 142
Cdd:PRK10938 337 HIGYVSSS------LHLDYRVSTSVRnvilsgffdsigIYQAVSDRQQKLAQQWLDILGIDKRTADAPFHsLSWGQQRLA 410
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 446139018 143 MIICAFIVNPELYIIDEPFLGLDPLG---IQSMLDLMVekkNEGRTVLM 188
Cdd:PRK10938 411 LIVRALVKHPTLLILDEPLQGLDPLNrqlVRRFVDVLI---SEGETQLL 456
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-223 |
2.08e-08 |
|
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.
Pssm-ID: 213255 [Multi-domain] Cd Length: 257 Bit Score: 53.37 E-value: 2.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 3 VKVEQLTGGYGK--RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVIYEeltleehiemTAMAYDIDRDEAM--NRAMPLLKTFRLENELKVFP-----------SHFSKGMKQKVMIIC 146
Cdd:cd03288 100 ILQDPILFS----------GSIRFNLDPECKCtdDRLWEALEIAQLKNMVKSLPggldavvteggENFSVGQRQLFCLAR 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 147 AFIVNPELYIIDEPFLGLDpLGIQSMLDLMVEKKNEGRTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEALRQQ 223
Cdd:cd03288 170 AFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQ 244
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-222 |
2.21e-08 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 53.15 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGL--LTPMEGSLSISDININD-DIE--AyRRKLS 78
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILElSPDerA-RAGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 79 YIPESPVIYEELTLEEHIEMtamAYDIDRDEAMNrAMPLLKTFR-LENELKVFPSH--------FSKGMKQKVMIICAFI 149
Cdd:COG0396 81 LAFQYPVEIPGVSVSNFLRT---ALNARRGEELS-AREFLKLLKeKMKELGLDEDFldryvnegFSGGEKKRNEILQMLL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 150 VNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTH---ILataeRY--CDRFIILDEGEVVAFGDLEALRQ 222
Cdd:COG0396 157 LEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrIL----DYikPDFVHVLVDGRIVKSGGKELALE 230
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
16-191 |
2.49e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 2.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 16 PVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLsisDININDDIEAYR-RKLSYIPESPVIYEELTLEE 94
Cdd:PRK13543 25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQI---QIDGKTATRGDRsRFMAYLGHLPGLKADLSTLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIEMTAMAYDIDRDEAMNRAMPLLKTFRLENELKvfpSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLD 174
Cdd:PRK13543 102 NLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTLV---RQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGITLVNR 178
|
170
....*....|....*..
gi 446139018 175 LMVEKKNEGRTVLMSTH 191
Cdd:PRK13543 179 MISAHLRGGGAALVTTH 195
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
7-193 |
2.55e-08 |
|
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: 52.72 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 7 QLTGGY----GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININDDIEAY-----RRKL 77
Cdd:cd03290 2 QVTNGYfswgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYSV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESPVIYEElTLEEHIEMTAmAYDIDRDEAMNRAMPL-----LKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNP 152
Cdd:cd03290 82 AYAAQKPWLLNA-TVEENITFGS-PFNKQRYKAVTDACSLqpdidLLPFGDQTEIGERGINLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446139018 153 ELYIIDEPFLGL-----DPLGIQSMLDLMVEKKnegRTVLMSTHIL 193
Cdd:cd03290 160 NIVFLDDPFSALdihlsDHLMQEGILKFLQDDK---RTLVLVTHKL 202
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-98 |
2.61e-08 |
|
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.
Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 2.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGslsisdininddiEAYRR---KLSYIPESPVIYEE 89
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG-------------EARPQpgiKVGYLPQEPQLDPT 82
|
....*....
gi 446139018 90 LTLEEHIEM 98
Cdd:TIGR03719 83 KTVRENVEE 91
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
14-167 |
3.02e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 52.65 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 14 KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLL--TPMEGSLSISDINinddieayrrklsyipespvIYEELT 91
Cdd:COG2401 42 ERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQ--------------------FGREAS 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 92 LEEHiemtamaydIDRDEAMNRAMPLLKTFRLeNELKVF---PSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPL 167
Cdd:COG2401 102 LIDA---------IGRKGDFKDAVELLNAVGL-SDAVLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-212 |
6.38e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 52.48 E-value: 6.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLtPmEGSLSiSDININDDIEAYRRklsyIPESP-----VIYEELTL-- 92
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-P-HGSYE-GEILFDGEVCRFKD----IRDSEalgivIIHQELALip 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 93 ----EEHIEM---TAMAYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLD 165
Cdd:NF040905 92 ylsiAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAALN 171
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446139018 166 PLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:NF040905 172 EEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
21-80 |
6.38e-08 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 52.67 E-value: 6.38e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446139018 21 INFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ-DDIEAYRRKLSYI 80
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaEQPEDYRKLFSAV 402
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-222 |
6.90e-08 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 51.91 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININ--DDIEAYRRKLSYIP 81
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEglPGHQIARMGVVRTF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 82 ESPVIYEELTLEE--------HIEMTAM-------AYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIIC 146
Cdd:PRK11300 87 QHVRLFREMTVIEnllvaqhqQLKTGLFsgllktpAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIAR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 147 AFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNE-GRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQ 222
Cdd:PRK11300 167 CMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
13-215 |
1.02e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 50.70 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTtikhMLGLLTP------MEGSLSISDININddiEAYRRKLSYIPESPVI 86
Cdd:cd03232 18 GKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGrktagvITGEILINGRPLD---KNFQRSTGYVEQQDVH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 87 YEELTLEEHIEMTAmaydidrdeamnrampLLKTFRLENelkvfpshfskgmKQKVMIICAFIVNPELYIIDEPFLGLDP 166
Cdd:cd03232 91 SPNLTVREALRFSA----------------LLRGLSVEQ-------------RKRLTIGVELAAKPSILFLDEPTSGLDS 141
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 167 LGIQSMLDLMVEKKNEGRTVLMSTH-----ILAtaerYCDRFIILDE-GEVVAFG 215
Cdd:cd03232 142 QAAYNIVRFLKKLADSGQAILCTIHqpsasIFE----KFDRLLLLKRgGKTVYFG 192
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
21-223 |
1.36e-07 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 51.44 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 21 INFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP----MEGSLSISDININDDIEAYRRKL-----SYIPESPVIYEE-- 89
Cdd:COG4170 26 VSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDLLKLSPRERRKIigreiAMIFQEPSSCLDps 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 90 LTLEEHIEmtamaydidrdEAM-----------------NRAMPLLKTFRLENE---LKVFPSHFSKGMKQKVMIICAFI 149
Cdd:COG4170 106 AKIGDQLI-----------EAIpswtfkgkwwqrfkwrkKRAIELLHRVGIKDHkdiMNSYPHELTEGECQKVMIAMAIA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 150 VNPELYIIDEPFLGLDP---LGIQSMLDLMveKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEALRQQ 223
Cdd:COG4170 175 NQPRLLIADEPTNAMESttqAQIFRLLARL--NQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKS 249
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
24-160 |
1.41e-07 |
|
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: 51.71 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 24 ELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSlsisdinINDDIeayrrKLSYIPESPVIYEELTLEEHIEMTAmay 103
Cdd:COG1245 362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGE-------VDEDL-----KISYKPQYISPDYDGTVEEFLRSAN--- 426
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 104 didrdeamNRAMP-------LLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:COG1245 427 --------TDDFGssyykteIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-212 |
7.84e-07 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 49.03 E-value: 7.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 5 VEQLTGGyGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLltpMEGSLSIS-DININDDIEAY------RRKL 77
Cdd:PRK15093 11 IEFKTSD-GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTaDRMRFDDIDLLrlspreRRKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 78 SYIPESpVIYEE----LTLEEHIEMTAM------AYDIDRDEAMN----RAMPLLKTFRLENE---LKVFPSHFSKGMKQ 140
Cdd:PRK15093 87 VGHNVS-MIFQEpqscLDPSERVGRQLMqnipgwTYKGRWWQRFGwrkrRAIELLHRVGIKDHkdaMRSFPYELTEGECQ 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 141 KVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVE-KKNEGRTVLMSTHILATAERYCDRFIILDEGEVV 212
Cdd:PRK15093 166 KVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-98 |
8.61e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 49.35 E-value: 8.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 13 GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGslsisdininddiEAYRR---KLSYIPESPVIYEE 89
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG-------------EARPApgiKVGYLPQEPQLDPE 84
|
....*....
gi 446139018 90 LTLEEHIEM 98
Cdd:PRK11819 85 KTVRENVEE 93
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-218 |
2.09e-06 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 47.33 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 4 KVEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLG--LLTPMEGSLSISDININdDIEAYRRK----- 76
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESIL-DLEPEERAhlgif 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 77 LSYipESPViyeELTLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRLENE-LKV------FPSH-----FSKGMKQKVMI 144
Cdd:CHL00131 88 LAF--QYPI---EIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEIINEkLKLvgmdpsFLSRnvnegFSGGEKKRNEI 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 145 ICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHIlataERYCDRFI-----ILDEGEVVAFGDLE 218
Cdd:CHL00131 163 LQMALLDSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITHY----QRLLDYIKpdyvhVMQNGKIIKTGDAE 237
|
|
| YbjD |
COG3593 |
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ... |
18-191 |
8.48e-06 |
|
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];
Pssm-ID: 442812 [Multi-domain] Cd Length: 359 Bit Score: 46.15 E-value: 8.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGeIVGLIGLNGAGKSTTIKHMLGLLTPMEG-SLSISDININDD-----------IEAYRRKLSYIPESPV 85
Cdd:COG3593 14 IKDLSIELSDD-LTVLVGENNSGKSSILEALRLLLGPSSSrKFDEEDFYLGDDpdlpeieieltFGSLLSRLLRLLLKEE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 86 IYEEL--------------------TLEEHIEMTAMAYDIDRDEAMNRAMPLLKTFRL--ENELKVFPSHFSKGMKQKVM 143
Cdd:COG3593 93 DKEELeealeelneelkealkalneLLSEYLKELLDGLDLELELSLDELEDLLKSLSLriEDGKELPLDRLGSGFQRLIL 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 144 IICAFIV-------NPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTH 191
Cdd:COG3593 173 LALLSALaelkrapANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
61-191 |
1.02e-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: 45.84 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 61 ISDININDDIEAYRRKLSYIPESPVIYEELTLEEHIEMTAMAYDIDRDEAMNRAMplLKTFRLENELKVFPSHFSKGMKQ 140
Cdd:pfam13304 166 WAVLDLAADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERG--LILLENGGGGELPAFELSDGTKR 243
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 141 kvmiICAFIV-------NPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTH 191
Cdd:pfam13304 244 ----LLALLAallsalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
22-234 |
1.30e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.78 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 22 NFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISdininddieaYRR--KLSYIPESPVIYEELT------LE 93
Cdd:PRK10938 23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQ----------FSHitRLSFEQLQKLVSDEWQrnntdmLS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 94 EHIEMTA-MAYDIDRDEAMN--RAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQ 170
Cdd:PRK10938 93 PGEDDTGrTTAEIIQDEVKDpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQ 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 171 SMLDLMVEKKNEGRTVLMsthILataERYCD--RFI----ILDEGEVVAFGDLEALRQQTGL----HKQTLDDI 234
Cdd:PRK10938 173 QLAELLASLHQSGITLVL---VL---NRFDEipDFVqfagVLADCTLAETGEREEILQQALVaqlaHSEQLEGV 240
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
5-59 |
1.33e-05 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 45.71 E-value: 1.33e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 5 VEQLTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSL 59
Cdd:PRK11147 322 MENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRI 376
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-165 |
1.35e-05 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 45.22 E-value: 1.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGY-GKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININdDIEAYRRKLSYI 80
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVN-ELEPADRDIAMV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 81 PESPVIYEELTLEEHiemtaMAY-----DIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELY 155
Cdd:PRK11650 82 FQNYALYPHMSVREN-----MAYglkirGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156
|
170
....*....|
gi 446139018 156 IIDEPFLGLD 165
Cdd:PRK11650 157 LFDEPLSNLD 166
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
14-211 |
1.55e-05 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 45.31 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 14 KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPM-EGSLSIS--DININDDIEAYRRKLSYIPESPV---IY 87
Cdd:PRK13549 274 HIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRwEGEIFIDgkPVKIRNPQQAIAQGIAMVPEDRKrdgIV 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 88 EELTLEEHIemTAMAYD-------IDRDE---AMNRAMPLLKTFRLENELKVfpSHFSKGMKQKVMIICAFIVNPELYII 157
Cdd:PRK13549 354 PVMGVGKNI--TLAALDrftggsrIDDAAelkTILESIQRLKVKTASPELAI--ARLSGGNQQKAVLAKCLLLNPKILIL 429
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 158 DEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEV 211
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-229 |
1.58e-05 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 45.48 E-value: 1.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 2 TVKVEQLTGGYGK-RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISDININD-DIEAYRRKLSY 79
Cdd:PRK10790 340 RIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 80 IPESPVI-----YEELTLEEHIemtamaydidRDEAMNRAmplLKTFRLENELKVFP-----------SHFSKGMKQKVM 143
Cdd:PRK10790 420 VQQDPVVladtfLANVTLGRDI----------SEEQVWQA---LETVQLAELARSLPdglytplgeqgNNLSVGQKQLLA 486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 144 IICAFIVNPELYIIDEPFLGLDP---LGIQSMLDLMVEKKnegrTVLMSTHILATAERyCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK10790 487 LARVLVQTPQILILDEATANIDSgteQAIQQALAAVREHT----TLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
....*....
gi 446139018 221 RQQTGLHKQ 229
Cdd:PRK10790 562 LAAQGRYWQ 570
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
17-191 |
5.90e-05 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 5.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTP--MEGSLSISDININDdiEAYRRKLSYIPESPVIYEELTLEE 94
Cdd:PLN03140 895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQ--ETFARISGYCEQNDIHSPQVTVRE 972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 95 HIEMTA---MAYDIDRDEAMN---RAMPLLKTFRLENELKVFP--SHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP 166
Cdd:PLN03140 973 SLIYSAflrLPKEVSKEEKMMfvdEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDA 1052
|
170 180
....*....|....*....|....*
gi 446139018 167 LGIQSMLDLMVEKKNEGRTVLMSTH 191
Cdd:PLN03140 1053 RAAAIVMRTVRNTVDTGRTVVCTIH 1077
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-210 |
6.33e-05 |
|
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: 42.56 E-value: 6.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 24 ELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEgslsisdininDDIEAYRRKLSYIPEspviYEELtleehiemtamay 103
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNG-----------DNDEWDGITPVYKPQ----YIDL------------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 104 didrdeamnrampllktfrlenelkvfpshfSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP---LGIQSMLDLMVEKK 180
Cdd:cd03222 73 -------------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIeqrLNAARAIRRLSEEG 121
|
170 180 190
....*....|....*....|....*....|
gi 446139018 181 NegRTVLMSTHILATAERYCDRFIILdEGE 210
Cdd:cd03222 122 K--KTALVVEHDLAVLDYLSDRIHVF-EGE 148
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
28-215 |
6.80e-05 |
|
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: 43.12 E-value: 6.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 28 GEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSiSDININDDIEAYR-------------------RKLSYIPESPVIYE 88
Cdd:cd03236 26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFD-DPPDWDEILDEFRgselqnyftkllegdvkviVKPQYVDLIPKAVK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 89 ELTLEehiemtamayDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLG 168
Cdd:cd03236 105 GKVGE----------LLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 446139018 169 IQSMLDLMVEKKNEGRTVLMSTHILATAErYCDRFIILDEGEVVAFG 215
Cdd:cd03236 175 RLNAARLIRELAEDDNYVLVVEHDLAVLD-YLSDYIHCLYGEPGAYG 220
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
21-223 |
8.08e-05 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 43.36 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 21 INFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISD--ININDDIEAYRRKLSYIPE---SPVIYEELTLEEH 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCPEdrkAEGIIPVHSVADN 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 96 IEMTAMAYDI-------DRDEAMN-----RAMPlLKTfrlenelkvfPSH------FSKGMKQKVmIICAFIVNP-ELYI 156
Cdd:PRK11288 352 INISARRHHLragclinNRWEAENadrfiRSLN-IKT----------PSReqlimnLSGGNQQKA-ILGRWLSEDmKVIL 419
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446139018 157 IDEPFLGLDpLGIQS-MLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAfgdlEALRQQ 223
Cdd:PRK11288 420 LDEPTRGID-VGAKHeIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG----ELAREQ 482
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-213 |
8.45e-05 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 43.07 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 28 GEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSI--SDININDDIEAYRRKLSYIPESPVIYEELTLEEHI----EMTAM 101
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYlgKEVTFNGPKSSQEAGIGIIHQELNLIPQLTIAENIflgrEFVNR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 102 AYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKN 181
Cdd:PRK10762 110 FGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKS 189
|
170 180 190
....*....|....*....|....*....|..
gi 446139018 182 EGRTVLMSTHILATAERYCDRFIILDEGEVVA 213
Cdd:PRK10762 190 QGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
27-147 |
9.15e-05 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.59 E-value: 9.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 27 KGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIsdININDDIEAYRRKLSYIPESPVIYEELTLEEHIEMTAMAYDID 106
Cdd:smart00382 1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLK 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 446139018 107 R-----DEAMNraMPLLKTFRLENELKVFPSHFSKGMKQKVMIICA 147
Cdd:smart00382 79 PdvlilDEITS--LLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
|
|
| PRK15177 |
PRK15177 |
Vi polysaccharide ABC transporter ATP-binding protein VexC; |
17-229 |
1.03e-04 |
|
Vi polysaccharide ABC transporter ATP-binding protein VexC;
Pssm-ID: 185099 [Multi-domain] Cd Length: 213 Bit Score: 42.35 E-value: 1.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGslsisdinindDIEAYRRKLSYIPESPVIYEELTLEEHI 96
Cdd:PRK15177 2 VLDKTDFVMGYHEHIGILAAPGSGKTTLTRLLCGLDAPDEG-----------DFIGLRGDALPLGANSFILPGLTGEENA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 97 EMTAMAYDIDRDEAMNRAMPLLKtfrLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIID-EPFLGLDPLGIQSMLDL 175
Cdd:PRK15177 71 RMMASLYGLDGDEFSHFCYQLTQ---LEQCYTDRVSEYSVTMKTHLAFAINLLLPCRLYIADgKLYTGDNATQLRMQAAL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 446139018 176 MVEKKNEGRTVLmsTHILATAERYCDRFIILDEGEVVAfgdLEALRQQTGLHKQ 229
Cdd:PRK15177 148 ACQLQQKGLIVL--THNPRLIKEHCHAFGVLLHGKITM---CEDLAQATALFEQ 196
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-88 |
1.29e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 42.84 E-value: 1.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTikhmlgLLTPMEG-SLSISDININD-DIEAY-----RRKLSYIPESPVIYE 88
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTL------LLTFMRMvEVCGGEIRVNGrEIGAYglrelRRQFSMIPQDPVLFD 1397
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
15-40 |
1.63e-04 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 42.47 E-value: 1.63e-04
10 20
....*....|....*....|....*.
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAG 40
Cdd:NF040905 273 RKVVDDVSLNVRRGEIVGIAGLMGAG 298
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-216 |
1.72e-04 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 42.40 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 14 KRPVIKDINFELNKGEIVGLIGLNGAGKSTTIK----HMLGLLTPMEGSLSISDININDDIEAYRRKLSYIPESPVIYEE 89
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKtiasNTDGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 90 LTLEEHIEMTAMA------YD-IDRDEAMNRAMPL-LKTFRLEN--ELKV---FPSHFSKGMKQKVMIICAFIVNPELYI 156
Cdd:TIGR00956 153 LTVGETLDFAARCktpqnrPDgVSREEYAKHIADVyMATYGLSHtrNTKVgndFVRGVSGGERKRVSIAEASLGGAKIQC 232
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446139018 157 IDEPFLGLDP---LGIQSMLDLMVEKKNEgrTVLMSthILATAERYCDRF---IILDEGEVVAFGD 216
Cdd:TIGR00956 233 WDNATRGLDSataLEFIRALKTSANILDT--TPLVA--IYQCSQDAYELFdkvIVLYEGYQIYFGP 294
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
15-215 |
1.76e-04 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 41.74 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 15 RPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLT---PMEGSLSISDININDD----IEAYR--RKLSYIPES-- 83
Cdd:PRK13547 14 RAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTgggAPRGARVTGDVTLNGEplaaIDAPRlaRLRAVLPQAaq 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 84 ---PVIYEELTL---EEHIEMTAMAYDIDRD---EAMNR--AMPLLK---TFRLENEL----------KVFPSHFSkgmk 139
Cdd:PRK13547 94 pafAFSAREIVLlgrYPHARRAGALTHRDGEiawQALALagATALVGrdvTTLSGGELarvqfarvlaQLWPPHDA---- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446139018 140 qkvmiicafIVNPELYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRT-VLMSTHILATAERYCDRFIILDEGEVVAFG 215
Cdd:PRK13547 170 ---------AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHG 237
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-220 |
2.50e-04 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 41.64 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 20 DINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIS--DININDDIEAYRRKLSyipespVIYEELTL-EEHI 96
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQgkEIDFKSSKEALENGIS------MVHQELNLvLQRS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 97 EMTAM--------AYDIDRDEAMNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDPLG 168
Cdd:PRK10982 90 VMDNMwlgryptkGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446139018 169 IQSMLDLMVEKKNEGRTVLMSTHILATAERYCDRFIILDEGEVVAFGDLEAL 220
Cdd:PRK10982 170 VNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-204 |
4.34e-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: 40.00 E-value: 4.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 18 IKDINFELNKGEIVGLIGLNGAGKSTTIKhmlglltpmEGSLSISDININDDIEAYRR-------KLSYIPESPVIYeeL 90
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN---------EGLYASGKARLISFLPKFSRnklifidQLQFLIDVGLGY--L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 91 TLeehiemtamaydidrdeamNRAMPLLktfrlenelkvfpshfSKGMKQKVMIICAFIVNPE--LYIIDEPFLGLDPLG 168
Cdd:cd03238 80 TL-------------------GQKLSTL----------------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
|
170 180 190
....*....|....*....|....*....|....*.
gi 446139018 169 IQSMLDLMVEKKNEGRTVLMSTHILATAErYCDRFI 204
Cdd:cd03238 125 INQLLEVIKGLIDLGNTVILIEHNLDVLS-SADWII 159
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
8-62 |
4.37e-04 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 41.03 E-value: 4.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 8 LTGGYGKRPVIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSIS 62
Cdd:PRK15064 7 ITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLD 61
|
|
| ABC_Class2 |
cd03227 |
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ... |
135-215 |
4.82e-04 |
|
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: 39.65 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 135 SKGMKQKVMIICAFI---VNPE-LYIIDEPFLGLDPLGIQSMLDLMVEKKNEGRTVLMSTHILATAERYcDRFIILdeGE 210
Cdd:cd03227 79 SGGEKELSALALILAlasLKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELA-DKLIHI--KK 155
|
....*
gi 446139018 211 VVAFG 215
Cdd:cd03227 156 VITGV 160
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
27-165 |
6.71e-04 |
|
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];
Pssm-ID: 440858 [Multi-domain] Cd Length: 592 Bit Score: 40.54 E-value: 6.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 27 KGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSiSDININDDIEAYR--------RKLsYIPESPVIYEeltlEEHIEM 98
Cdd:COG1245 98 KGKVTGILGPNGIGKSTALKILSGELKPNLGDYD-EEPSWDEVLKRFRgtelqdyfKKL-ANGEIKVAHK----PQYVDL 171
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446139018 99 TAMAYD------IDR-DEAMnRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLD 165
Cdd:COG1245 172 IPKVFKgtvrelLEKvDERG-KLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-222 |
6.98e-04 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 40.53 E-value: 6.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 17 VIKDINFELNKGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSISdininddieayrRKLSYIPESPVIYEElTLEEHI 96
Cdd:PTZ00243 675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE------------RSIAYVPQQAWIMNA-TVRGNI 741
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 97 -----EMTAMAYDIDRDEAMNRAMPLLKTfRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEPFLGLDP-LGIQ 170
Cdd:PTZ00243 742 lffdeEDAARLADAVRVSQLEADLAQLGG-GLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSALDAhVGER 820
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 446139018 171 SMLDLMVEKKnEGRTVLMST---HILATAerycDRFIILDEGEVVAFGDLEALRQ 222
Cdd:PTZ00243 821 VVEECFLGAL-AGKTRVLAThqvHVVPRA----DYVVALGDGRVEFSGSSADFMR 870
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
27-160 |
1.31e-03 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 39.41 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446139018 27 KGEIVGLIGLNGAGKSTTIKHMLGLLTPMEGSLSiSDININDDIEAYR-------------------RKLSYIPESPVIY 87
Cdd:PRK13409 98 EGKVTGILGPNGIGKTTAVKILSGELIPNLGDYE-EEPSWDEVLKRFRgtelqnyfkklyngeikvvHKPQYVDLIPKVF 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446139018 88 EElTLEEHIEMTamaydidrDEAmNRAMPLLKTFRLENELKVFPSHFSKGMKQKVMIICAFIVNPELYIIDEP 160
Cdd:PRK13409 177 KG-KVRELLKKV--------DER-GKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| |
