|
Name |
Accession |
Description |
Interval |
E-value |
| CcmA |
COG1131 |
ABC-type multidrug transport system, ATPase component [Defense mechanisms]; |
3-243 |
7.64e-97 |
|
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 282.72 E-value: 7.64e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPE 82
Cdd:COG1131 1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:COG1131 81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 163 GLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQtamphaTLDEIYIHVTKGA 242
Cdd:COG1131 161 GLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKAR------LLEDVFLELTGEE 234
|
.
gi 2095223075 243 Q 243
Cdd:COG1131 235 A 235
|
|
| NatA |
COG4555 |
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ... |
4-237 |
1.03e-73 |
|
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: 224.35 E-value: 1.03e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEA 83
Cdd:COG4555 3 EVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPDE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 84 PVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLG 163
Cdd:COG4555 83 RGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNG 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 164 LDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTAmpHATLDEIYIH 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 |
2.97e-72 |
|
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: 218.04 E-value: 2.97e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPE 82
Cdd:cd03230 1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEmtamaysidydtamaralpllktfrledqlhifpshFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd03230 81 EPSLYENLTVRENLK------------------------------------LSGGMKQRLALAQALLHDPELLILDEPTS 124
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095223075 163 GLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:cd03230 125 GLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
|
|
| YhaQ |
COG4152 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
2-223 |
2.00e-58 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 186.85 E-value: 2.00e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIhayRQHLSYIP 81
Cdd:COG4152 1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPED---RRRIGYLP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 EAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLED-------QLhifpshfSKGMKQKVMIICAFIVEPDF 154
Cdd:COG4152 78 EERGLYPKMKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDrankkveEL-------SKGNQQKVQLIAALLHDPEL 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 155 YIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQ 223
Cdd:COG4152 151 LILDEPFSGLDPVNVELLKDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEIRRQ 219
|
|
| ABC_BcrA_bacitracin_resist |
cd03268 |
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ... |
3-215 |
1.94e-55 |
|
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: 176.64 E-value: 1.94e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRqHLSYIPE 82
Cdd:cd03268 1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIGALIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYdtamARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd03268 80 APGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTN 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 163 GLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03268 156 GLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
|
|
| drrA |
TIGR01188 |
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ... |
12-222 |
6.53e-54 |
|
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: 175.66 E-value: 6.53e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 12 YGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEAPVIYDALT 91
Cdd:TIGR01188 3 YGDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 92 LKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQS 171
Cdd:TIGR01188 83 GRENLEMMGRLYGLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTRRA 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 172 MLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:TIGR01188 163 IWDYIRALKEEGVTILLTTHYMEEADKLCDRIAIIDHGRIIAEGTPEELKR 213
|
|
| ABC_subfamily_A |
cd03263 |
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ... |
3-215 |
9.57e-53 |
|
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: 169.99 E-value: 9.57e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGK--KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYI 80
Cdd:cd03263 1 LQIRNLTKTYKKgtKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:cd03263 81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKeEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
|
|
| EcfA2 |
COG1122 |
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ... |
3-220 |
4.03e-51 |
|
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: 165.97 E-value: 4.03e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSYI 80
Cdd:COG1122 1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDItKKNLRELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 ---PE----APVIYD--ALTLKehiemtamAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVE 151
Cdd:COG1122 81 fqnPDdqlfAPTVEEdvAFGPE--------NLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAME 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 152 PDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG1122 153 PEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREV 221
|
|
| ABC_putative_ATPase |
cd03269 |
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ... |
3-215 |
6.55e-51 |
|
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: 165.15 E-value: 6.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIhayRQHLSYIPE 82
Cdd:cd03269 1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA---RNRIGYLPE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd03269 78 ERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 163 GLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03269 158 GLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
|
|
| CcmA |
COG4133 |
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ... |
1-191 |
3.47e-50 |
|
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: 163.03 E-value: 3.47e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYI 80
Cdd:COG4133 1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARAlpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:COG4133 81 GHADGLKPELTVRENLRFWAALYGLRADREAIDE--ALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158
|
170 180 190
....*....|....*....|....*....|.
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEGRTVLMSTH 191
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLLTTH 189
|
|
| ABC_cobalt_CbiO_domain1 |
cd03225 |
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ... |
4-210 |
8.34e-48 |
|
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ABC component of a cobalt transport family found in bacteria, archaea, and eukaryota. The transition metal cobalt is an essential component of many enzymes and must be transported into cells in appropriate amounts when needed. This ABC transport system of the CbiMNQO family is involved in cobalt transport in association with the cobalamin (vitamin B12) biosynthetic pathways. Most of cobalt (Cbi) transport systems possess a separate CbiN component, the cobalt-binding periplasmic protein, and they are encoded by the conserved gene cluster cbiMNQO. Both the CbiM and CbiQ proteins are integral cytoplasmic membrane proteins, and the CbiO protein has the linker peptide and the Walker A and B motifs commonly found in the ATPase components of the ABC-type transport systems.
Pssm-ID: 213192 [Multi-domain] Cd Length: 211 Bit Score: 156.86 E-value: 8.34e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYI 80
Cdd:cd03225 1 ELKNLSFSYpdGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlSLKELRRKVGLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 ---PEAPVIydALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYII 157
Cdd:cd03225 81 fqnPDDQFF--GPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLL 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 158 DEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGE 210
Cdd:cd03225 159 DEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
3-220 |
1.12e-46 |
|
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: 161.99 E-value: 1.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY-----GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAY 73
Cdd:COG1123 261 LEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLtklsRRSLREL 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 74 RQHLSYIPEAPviYDAL----TLKEHIEMTAMAYSI-DYDTAMARALPLLKTFRL-EDQLHIFPSHFSKGMKQKVMIICA 147
Cdd:COG1123 341 RRRVQMVFQDP--YSSLnprmTVGDIIAEPLRLHGLlSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 148 FIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG1123 419 LALEPKLLILDEPTSALDVSVQAQILNLLRDlQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492
|
|
| ABC_DrrA |
cd03265 |
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ... |
3-221 |
2.94e-46 |
|
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: 153.29 E-value: 2.94e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPE 82
Cdd:cd03265 1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd03265 81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 163 GLDPIGIQSMLD-LMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALR 221
Cdd:cd03265 161 GLDPQTRAHVWEyIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEELK 220
|
|
| ABC_ATPase |
cd00267 |
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ... |
4-210 |
2.34e-45 |
|
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: 148.93 E-value: 2.34e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSYIPe 82
Cdd:cd00267 1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIaKLPLEELRRRIGYVP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 apviydaltlkehiemtamaysidydtamaralpllktfrledQLhifpshfSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd00267 80 -------------------------------------------QL-------SGGQRQRVALARALLLNPDLLLLDEPTS 109
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095223075 163 GLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGE 210
Cdd:cd00267 110 GLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
|
|
| ABC_drug_resistance_like |
cd03264 |
ABC-type multidrug transport system, ATPase component; The biological function of this family ... |
3-215 |
4.79e-45 |
|
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: 150.04 E-value: 4.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGeIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPE 82
Cdd:cd03264 1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd03264 80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 163 GLDP---IGIQSMLdlmaSKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03264 160 GLDPeerIRFRNLL----SELGEDRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
|
|
| ABC_NatA_sodium_exporter |
cd03266 |
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ... |
3-215 |
8.43e-45 |
|
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: 149.44 E-value: 8.43e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYG--KKPI--IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLS 78
Cdd:cd03266 2 ITADALTKRFRdvKKTVqaVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:cd03266 82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 159 EPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
|
|
| GsiA |
COG1123 |
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ... |
1-229 |
4.71e-44 |
|
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440740 [Multi-domain] Cd Length: 514 Bit Score: 155.06 E-value: 4.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MT--VQIKNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPT---EGDMSISGINIKEDIHAY 73
Cdd:COG1123 1 MTplLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 74 R-QHLSYIPEAP-VIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVE 151
Cdd:COG1123 81 RgRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 152 PDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTAMPHA 229
Cdd:COG1123 161 PDLLIADEPTTALDVTTQAEILDLLRElQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQALAA 239
|
|
| FepC |
COG1120 |
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ... |
3-215 |
1.47e-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: 1.47e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAYR-----QHL 77
Cdd:COG1120 2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDG----RDLASLSrrelaRRI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDALTLKEHIEMTAMAY--------SIDYDtAMARALPLLKTFRLEDQLHifpSHFSKGMKQKVMIICAFI 149
Cdd:COG1120 78 AYVPQEPPAPFGLTVRELVALGRYPHlglfgrpsAEDRE-AVEEALERTGLEHLADRPV---DELSGGERQRVLIARALA 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 150 VEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRlARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQG 220
|
|
| ABC_TM1139_LivF_branched |
cd03224 |
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ... |
4-222 |
2.52e-43 |
|
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of the LIV-I bacterial ABC-type two-component transport system that imports neutral, branched-chain amino acids. The E. coli branched-chain amino acid transporter comprises a heterodimer of ABC transporters (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules.
Pssm-ID: 213191 [Multi-domain] Cd Length: 222 Bit Score: 146.04 E-value: 2.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAYRQH------L 77
Cdd:cd03224 2 EVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDG----RDITGLPPHeraragI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDALTLKEHIEMTAMAYSID-YDTAMARALPLlktF-RLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFY 155
Cdd:cd03224 78 GYVPEGRRIFPELTVEENLLLGAYARRRAkRKARLERVYEL---FpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 156 IIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLA 221
|
|
| ZnuC |
COG1121 |
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-235 |
5.31e-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: 5.31e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAYRQHLSYIPE 82
Cdd:COG1121 7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFG----KPPRRARRRIGYVPQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIyDA---LTLKEHIEMTAMAYS--------IDYDTAMAralpLLKTFRLEDQLH--IfpSHFSKGMKQKVMIICAFI 149
Cdd:COG1121 83 RAEV-DWdfpITVRDVVLMGRYGRRglfrrpsrADREAVDE----ALERVGLEDLADrpI--GELSGGQQQRVLLARALA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 150 VEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGeIVAMGNLEalrhqTAMPHA 229
Cdd:COG1121 156 QDPDLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPE-----EVLTPE 229
|
....*.
gi 2095223075 230 TLDEIY 235
Cdd:COG1121 230 NLSRAY 235
|
|
| ABC_Metallic_Cations |
cd03235 |
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ... |
4-215 |
2.17e-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: 143.06 E-value: 2.17e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIH--AY-RQHLSYI 80
Cdd:cd03235 1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKriGYvPQRRSID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPV-IYD--ALTLKEHIEMTAMAYSIDYDTAMaRALPLLKTFRLEDQlHIfpSHFSKGMKQKVMIICAFIVEPDFYII 157
Cdd:cd03235 81 RDFPIsVRDvvLMGLYGHKGLFRRLSKADKAKVD-EALERVGLSELADR-QI--GELSGGQQQRVLLARALVQDPDLLLL 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 158 DEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDqGEIVAMG 215
Cdd:cd03235 157 DEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLLN-RTVVASG 213
|
|
| ABC_Org_Solvent_Resistant |
cd03261 |
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ... |
3-222 |
5.02e-42 |
|
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: 143.03 E-value: 5.02e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-----KEDIHAyRQHL 77
Cdd:cd03261 1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDIsglseAELYRL-RRRM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDALTLKEHI-----EMTAMaysidyDTAMARALPLLK--TFRLEDQLHIFPSHFSKGMKQKVMIICAFIV 150
Cdd:cd03261 80 GMLFQSGALFDSLTVFENVafplrEHTRL------SEEEIREIVLEKleAVGLRGAEDLYPAELSGGMKKRVALARALAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 151 EPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:cd03261 154 DPELLLYDEPTAGLDPIASGVIDDLIRSlKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
|
|
| ABC_NikE_OppD_transporters |
cd03257 |
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ... |
3-215 |
6.09e-42 |
|
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: 142.64 E-value: 6.09e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLT----GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYR 74
Cdd:cd03257 2 LEVKNLSvsfpTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLlklsRRLRKIRR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QHLSYIPEAPviYDAL----TLKEHIEMTAMAYSIDYDTAMARALPLLKTFRL---EDQLHIFPSHFSKGMKQKVMIICA 147
Cdd:cd03257 82 KEIQMVFQDP--MSSLnprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 148 FIVEPDFYIIDEPFLGLDPIgIQS-MLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03257 160 LALNPKLLIADEPTSALDVS-VQAqILDLLKKlQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
|
|
| MlaF |
COG1127 |
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ... |
3-222 |
2.39e-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: 141.27 E-value: 2.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHLS 78
Cdd:COG1127 6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDItglsEKELYELRRRIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDALT--------LKEHIEMTAmaysidyDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIV 150
Cdd:COG1127 86 MLFQGGALFDSLTvfenvafpLREHTDLSE-------AEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 151 EPD--FYiiDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:COG1127 159 DPEilLY--DEPTAGLDPITSAVIDELIRElRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231
|
|
| ABC_Iron-Siderophores_B12_Hemin |
cd03214 |
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ... |
4-215 |
3.13e-41 |
|
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: 139.11 E-value: 3.13e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYIPE 82
Cdd:cd03214 1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASlSPKELARKIAYVPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 ApviydaltlkehiemtamaysidydtamaralplLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd03214 81 A----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 163 GLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03214 127 HLDIAHQIELLELLRRlARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
|
|
| GldA_ABC_ATP |
TIGR03522 |
gliding motility-associated ABC transporter ATP-binding subunit GldA; Members of this protein ... |
1-225 |
8.47e-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: 139.14 E-value: 8.47e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYI 80
Cdd:TIGR03522 1 MSIRVSSLTKLYGTQNALDEVSFEAQKGRIVGFLGPNGAGKSTTMKIITGYLPPDSGSVQVCGEDVLQNPKEVQRNIGYL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:TIGR03522 81 PEHNPLYLDMYVREYLQFIAGIYGMKGQLLKQRVEEMIELVGLRPEQHKKIGQLSKGYRQRVGLAQALIHDPKVLILDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTA 225
Cdd:TIGR03522 161 TTGLDPNQLVEIRNVIKNIGKD-KTIILSTHIMQEVEAICDRVIIINKGKIVADKKLDELSAANK 224
|
|
| ABC_Class3 |
cd03229 |
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ... |
3-210 |
1.47e-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: 135.01 E-value: 1.47e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI---KEDIHAYRQHLSY 79
Cdd:cd03229 1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLtdlEDELPPLRRRIGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDALTLKEHIemtamaysidydtamarALPLlktfrledqlhifpshfSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:cd03229 81 VFQDFALFPHLTVLENI-----------------ALGL-----------------SGGQQQRVALARALAMDPDVLLLDE 126
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 160 PFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGE 210
Cdd:cd03229 127 PTSALDPITRREVRALLKSlQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
|
|
| ABC_PhnC_transporter |
cd03256 |
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ... |
4-235 |
1.48e-39 |
|
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: 136.93 E-value: 1.48e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYG-KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYR---- 74
Cdd:cd03256 2 EVENLSKTYPnGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDInklkGKALRQLRrqig 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 ---QHLSYIPEAPVIYDALT--LKEHIEMTAMA---YSIDYdtamARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIIC 146
Cdd:cd03256 82 mifQQFNLIERLSVLENVLSgrLGRRSTWRSLFglfPKEEK----QRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 147 AFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASK-KEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQta 225
Cdd:cd03256 158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDE-- 235
|
250
....*....|
gi 2095223075 226 mphaTLDEIY 235
Cdd:cd03256 236 ----VLDEIY 241
|
|
| galliderm_ABC |
TIGR03740 |
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ... |
4-220 |
2.16e-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: 135.99 E-value: 2.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGInikediHAYRQHLSYIP-- 81
Cdd:TIGR03740 2 ETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH------PWTRKDLHKIGsl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 -EAPVIYDALTLKEHIEMTAMAYSIDYdtamARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:TIGR03740 76 iESPPLYENLTARENLKVHTTLLGLPD----SRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDEP 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG------NLEAL 220
Cdd:TIGR03740 152 TNGLDPIGIQELRELIRSFPEQGITVILSSHILSEVQQLADHIGIISEGVLGYQGkinkseNLEKL 217
|
|
| ABC_tran |
pfam00005 |
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ... |
18-161 |
1.37e-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: 131.62 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSYIPEAPVIYDALTLKEHI 96
Cdd:pfam00005 1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLtDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 97 EMTAMAYSIDYDTAMARALPLLKTFRLEDQ----LHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPF 161
Cdd:pfam00005 81 RLGLLLKGLSKREKDARAEEALEKLGLGDLadrpVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
|
|
| ABC_MJ0796_LolCDE_FtsE |
cd03255 |
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ... |
3-211 |
2.38e-38 |
|
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: 133.00 E-value: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLT----GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-----KEDIHAY 73
Cdd:cd03255 1 IELKNLSktygGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDIsklseKELAAFR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 74 RQHLSYIPEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPD 153
Cdd:cd03255 81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILaTAERYCDRFIILDQGEI 211
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRElNKEAGTTIVVVTHDP-ELAEYADRIIELRDGKI 218
|
|
| PRK13536 |
PRK13536 |
nodulation factor ABC transporter ATP-binding protein NodI; |
1-233 |
1.85e-37 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 134.19 E-value: 1.85e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYI 80
Cdd:PRK13536 40 VAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:PRK13536 120 PQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEP 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNlealrhqtamPHATLDE 233
Cdd:PRK13536 200 TTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGR----------PHALIDE 262
|
|
| ABC_HisP_GlnQ |
cd03262 |
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ... |
3-211 |
2.05e-37 |
|
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.
Pssm-ID: 213229 [Multi-domain] Cd Length: 213 Bit Score: 130.34 E-value: 2.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI---KEDIHAYRQHLSY 79
Cdd:cd03262 1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDALTLKEHIEMTAM-AYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:cd03262 81 VFQQFNLFPHLTVLENITLAPIkVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 159 EPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
|
|
| LivF |
COG0410 |
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ... |
4-222 |
4.66e-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: 130.10 E-value: 4.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAYRQH------L 77
Cdd:COG0410 5 EVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDG----EDITGLPPHriarlgI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDALTLKEHIEMTAMAYSIDYDTAMaralpllktfRLEDQLHIFP----------SHFSKGMKQKVMIICA 147
Cdd:COG0410 81 GYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRA----------DLERVYELFPrlkerrrqraGTLSGGEQQMLAIGRA 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 148 FIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:COG0410 151 LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLA 225
|
|
| PRK13537 |
PRK13537 |
nodulation factor ABC transporter ATP-binding protein NodI; |
3-220 |
1.35e-36 |
|
nodulation factor ABC transporter ATP-binding protein NodI;
Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 131.08 E-value: 1.35e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPE 82
Cdd:PRK13537 8 IDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGVVPQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:PRK13537 88 FDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 163 GLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK13537 168 GLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225
|
|
| ABC_OpuCA_Osmoprotection |
cd03295 |
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ... |
3-223 |
2.57e-36 |
|
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: 128.57 E-value: 2.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGK-KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYI 80
Cdd:cd03295 1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREqDPVELRRKIGYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQ--LHIFPSHFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:cd03295 81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADPPLLLMD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 159 EPFLGLDPIGIQSMLDLMASKKEE-GRTVLMSTHILATAERYCDRFIILDQGEIVAMGN-LEALRHQ 223
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTpDEILRSP 227
|
|
| LPS_export_lptB |
TIGR04406 |
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ... |
2-216 |
3.10e-36 |
|
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]
Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 128.16 E-value: 3.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAY-RQHLSY 79
Cdd:TIGR04406 1 TLVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDItHLPMHERaRLGIGY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDALTLKEHIE-MTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:TIGR04406 81 LPQEASIFRKLTVEENIMaVLEIRKDLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLD 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 159 EPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:TIGR04406 161 EPFAGVDPIAVGDIKKIIKHLKERGIGVLITDHNVRETLDICDRAYIISDGKVLAEGT 218
|
|
| ABC_Carb_Solutes_like |
cd03259 |
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ... |
3-215 |
2.22e-35 |
|
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: 124.94 E-value: 2.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKeDIHAYRQHLSYIPE 82
Cdd:cd03259 1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVT-GVPPERRNIGMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIemtamAY-----SIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYII 157
Cdd:cd03259 80 DYALFPHLTVAENI-----AFglklrGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLL 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 158 DEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03259 155 DEPLSALDAKLREELREELKElQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
|
|
| PhnC |
COG3638 |
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ... |
3-235 |
3.45e-35 |
|
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 125.55 E-value: 3.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHL 77
Cdd:COG3638 3 LELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVtalrGRALRRLRRRI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAP-------VIYDAL--------TLKEhieMTAMAYSIDYDTAMAralpLLKTFRLEDQLHIFPSHFSKGMKQKV 142
Cdd:COG3638 83 GMIFQQFnlvprlsVLTNVLagrlgrtsTWRS---LLGLFPPEDRERALE----ALERVGLADKAYQRADQLSGGQQQRV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 143 MIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASK-KEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALr 221
Cdd:COG3638 156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIaREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL- 234
|
250
....*....|....
gi 2095223075 222 hqTAmphATLDEIY 235
Cdd:COG3638 235 --TD---AVLREIY 243
|
|
| ABC_NrtD_SsuB_transporters |
cd03293 |
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ... |
3-213 |
6.91e-35 |
|
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: 124.12 E-value: 6.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYG----KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAYRQHLS 78
Cdd:cd03293 1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDG----EPVTGPGPDRG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:cd03293 77 YVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLD 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 159 EPFLGLDPIGIQSM-LDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQ--GEIVA 213
Cdd:cd03293 157 EPFSALDALTREQLqEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVA 214
|
|
| CydD |
COG4988 |
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ... |
2-223 |
7.81e-35 |
|
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 444012 [Multi-domain] Cd Length: 563 Bit Score: 130.65 E-value: 7.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:COG4988 336 SIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWRRQIAW 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYdALTLKEHIEMTAMAYSidyDTAMARALPL--LKTF--RLEDQLHiFP-----SHFSKGMKQKVMIICAFIV 150
Cdd:COG4988 416 VPQNPYLF-AGTIRENLRLGRPDAS---DEELEAALEAagLDEFvaALPDGLD-TPlgeggRGLSGGQAQRLALARALLR 490
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 151 EPDFYIIDEPFLGLDPIG----IQSMLDLMAskkeeGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEALRHQ 223
Cdd:COG4988 491 DAPLLLLDEPTAHLDAETeaeiLQALRRLAK-----GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEELLAK 561
|
|
| ABC_phnC |
TIGR02315 |
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ... |
3-235 |
9.04e-35 |
|
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: 124.33 E-value: 9.04e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGK-KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHL 77
Cdd:TIGR02315 2 LEVENLSKVYPNgKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDItklrGKKLRKLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDALTLKEHIEMTAMAYSIDYDTAM--------ARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFI 149
Cdd:TIGR02315 82 GMIFQHYNLIERLTVLENVLHGRLGYKPTWRSLLgrfseedkERALSALERVGLADKAYQRADQLSGGQQQRVAIARALA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 150 VEPDFYIIDEPFLGLDPI-GIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQtamph 228
Cdd:TIGR02315 162 QQPDLILADEPIASLDPKtSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE----- 236
|
....*..
gi 2095223075 229 aTLDEIY 235
Cdd:TIGR02315 237 -VLRHIY 242
|
|
| ABC_NatA_like |
cd03267 |
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ... |
12-215 |
1.39e-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: 123.60 E-value: 1.39e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 12 YGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYI--PEAPVIYDa 89
Cdd:cd03267 31 YREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfgQKTQLWWD- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 90 LTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG- 168
Cdd:cd03267 110 LPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAq 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095223075 169 --IQSMLDlmASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03267 190 enIRNFLK--EYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
|
|
| ECF_ATPase_2 |
TIGR04521 |
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ... |
3-215 |
1.53e-34 |
|
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]
Pssm-ID: 275314 [Multi-domain] Cd Length: 277 Bit Score: 124.87 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGK-----KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAY 73
Cdd:TIGR04521 1 IKLKNVSYIYQPgtpfeKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDItakkKKKLKDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 74 RQHLSYI---PEAPVIydALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRL-EDQLHIFPSHFSKGMKQKVMIICAFI 149
Cdd:TIGR04521 81 RKKVGLVfqfPEHQLF--EETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 150 VEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRlHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDG 225
|
|
| ABCC_MRP_Like |
cd03228 |
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ... |
3-210 |
5.45e-34 |
|
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213195 [Multi-domain] Cd Length: 171 Bit Score: 120.18 E-value: 5.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYG--KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:cd03228 1 IEFKNVSFSYPgrPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAlTLKEHIemtamaysidydtamaralpllktfrledqlhifpshFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:cd03228 81 VPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDE 122
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 160 PFLGLDPIG----IQSMLDLMaskkeEGRTVLMSTHILATAERyCDRFIILDQGE 210
Cdd:cd03228 123 ATSALDPETealiLEALRALA-----KGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
|
|
| SunT |
COG2274 |
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ... |
3-220 |
7.63e-34 |
|
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: 128.41 E-value: 7.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYG--KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:COG2274 474 IELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQIGV 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAlTLKEHIemTAMAYSIDYDTAMA-----------RALPL-LKTFRLEDQlhifpSHFSKGMKQKVMIICA 147
Cdd:COG2274 554 VLQDVFLFSG-TIRENI--TLGDPDATDEEIIEaarlaglhdfiEALPMgYDTVVGEGG-----SNLSGGQRQRLAIARA 625
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 148 FIVEPDFYIIDEPFLGLDPIG---IQSMLDLMAskkeEGRTVLMSTHILATAeRYCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG2274 626 LLRNPRILILDEATSALDAETeaiILENLRRLL----KGRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEEL 696
|
|
| ABC_YhbG |
cd03218 |
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ... |
7-220 |
1.07e-33 |
|
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: 121.50 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 7 NLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHaYRQHL--SYIPEA 83
Cdd:cd03218 5 NLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDItKLPMH-KRARLgiGYLPQE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 84 PVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLG 163
Cdd:cd03218 84 ASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAG 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 164 LDPIGIQSMLDLMASKKEEGRTVLMSTH----ILATaeryCDRFIILDQGEIVAMGNLEAL 220
Cdd:cd03218 164 VDPIAVQDIQKIIKILKDRGIGVLITDHnvreTLSI----TDRAYIIYEGKVLAEGTPEEI 220
|
|
| ABC_MetN_methionine_transporter |
cd03258 |
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ... |
6-220 |
1.02e-32 |
|
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: 118.84 E-value: 1.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 6 KNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE----DIHAYRQHLSYI- 80
Cdd:cd03258 9 KVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkELRKARRRIGMIf 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 -----PEAPVIYD--ALTLKehIEMTAMAYSIdydtamARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPD 153
Cdd:cd03258 89 qhfnlLSSRTVFEnvALPLE--IAGVPKAEIE------ERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDiNRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEV 228
|
|
| COG4586 |
COG4586 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
18-225 |
1.26e-32 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 120.96 E-value: 1.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSY--------IPEAPVIyDA 89
Cdd:COG4586 38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKEFARRIGVvfgqrsqlWWDLPAI-DS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 90 LTLKEHIemtamaYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGI 169
Cdd:COG4586 117 FRLLKAI------YRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSK 190
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 170 QSMLD-LMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTA 225
Cdd:COG4586 191 EAIREfLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFG 247
|
|
| glnQ |
PRK09493 |
glutamine ABC transporter ATP-binding protein GlnQ; |
3-239 |
1.19e-31 |
|
glutamine ABC transporter ATP-binding protein GlnQ;
Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 116.35 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI---KEDIHAYRQhlsy 79
Cdd:PRK09493 2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQ---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 ipEAPVIYDALTLKEHieMTAM---------AYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIV 150
Cdd:PRK09493 78 --EAGMVFQQFYLFPH--LTALenvmfgplrVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 151 EPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALrhQTAMPHAT 230
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL--IKNPPSQR 231
|
....*....
gi 2095223075 231 LDEIYIHVT 239
Cdd:PRK09493 232 LQEFLQHVS 240
|
|
| FtsE |
COG2884 |
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning]; |
3-212 |
1.69e-31 |
|
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 115.15 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHL 77
Cdd:COG2884 2 IRFENVSKRYpGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLsrlkRREIPYLRRRI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIP-EAPVIYDaLTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYI 156
Cdd:COG2884 82 GVVFqDFRLLPD-RTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 157 IDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIV 212
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLV 216
|
|
| TauB |
COG1116 |
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ... |
3-213 |
5.17e-31 |
|
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 115.19 E-value: 5.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLT----GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAYRQHLS 78
Cdd:COG1116 8 LELRGVSkrfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDG----KPVTGPGPDRG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:COG1116 84 VVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEVLLMD 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 159 EPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQ--GEIVA 213
Cdd:COG1116 164 EPFGALDALTRERLQDELLRlWQETGKTVLFVTHDVDEAVFLADRVVVLSArpGRIVE 221
|
|
| ArtP |
COG4161 |
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism]; |
1-224 |
1.94e-30 |
|
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 113.18 E-value: 1.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKhILGLL-TPTEGDMSISG--------INIKEdIH 71
Cdd:COG4161 1 MSIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLR-VLNLLeTPDSGQLNIAGhqfdfsqkPSEKA-IR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 72 AYRQ-------------HLSYIP---EAPVIYDALTLKEhiemtamaysidydtAMARALPLLKTFRLEDQLHIFPSHFS 135
Cdd:COG4161 79 LLRQkvgmvfqqynlwpHLTVMEnliEAPCKVLGLSKEQ---------------AREKAMKLLARLRLTDKADRFPLHLS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 136 KGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:COG4161 144 GGQQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
|
250
....*....|
gi 2095223075 216 NLEALRH-QT 224
Cdd:COG4161 224 DASHFTQpQT 233
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
3-215 |
3.94e-30 |
|
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: 118.19 E-value: 3.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGK--KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYI 80
Cdd:TIGR01257 929 VCVKNLVKIFEPsgRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMC 1008
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:TIGR01257 1009 PQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEP 1088
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 161 FLGLDPIGIQSMLDLMAsKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:TIGR01257 1089 TSGVDPYSRRSIWDLLL-KYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
|
|
| LptB |
COG1137 |
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ... |
1-220 |
4.70e-30 |
|
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 112.04 E-value: 4.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAY------R 74
Cdd:COG1137 2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDG----EDITHLpmhkraR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QHLSYIPEAPVIYDALTLKEHI----EMTamaySIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIV 150
Cdd:COG1137 78 LGIGYLPQEASIFRKLTVEDNIlavlELR----KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 151 EPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTH----ILATaeryCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG1137 154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKERGIGVLITDHnvreTLGI----CDRAYIISEGKVLAEGTPEEI 223
|
|
| artP |
PRK11124 |
arginine transporter ATP-binding subunit; Provisional |
1-215 |
9.98e-30 |
|
arginine transporter ATP-binding subunit; Provisional
Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 111.26 E-value: 9.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKhILGLL-TPTEGDMSISG--------INIKEdIH 71
Cdd:PRK11124 1 MSIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLR-VLNLLeMPRSGTLNIAGnhfdfsktPSDKA-IR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 72 AYRQHLSYIPEAPVIYDALTLKEH-IEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIV 150
Cdd:PRK11124 79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 151 EPDFYIIDEPFLGLDP-IGIQsMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK11124 159 EPQVLLFDEPTAALDPeITAQ-IVSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
|
|
| DppD |
COG0444 |
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ... |
3-227 |
1.20e-29 |
|
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: 112.84 E-value: 1.20e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY----GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTP---TEGDMSISGINI----KEDIH 71
Cdd:COG0444 2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLlklsEKELR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 72 AYR-QHLSYIPEAPviYDAL----TLKEHIEMTAMAY-SIDYDTAMARALPLLKTFRL---EDQLHIFPSHFSKGMKQKV 142
Cdd:COG0444 82 KIRgREIQMIFQDP--MTSLnpvmTVGDQIAEPLRIHgGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 143 MIICAFIVEPDFYIIDEPFLGLDPIgIQ-SMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG0444 160 MIARALALEPKLLIADEPTTALDVT-IQaQILNLLKDlQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238
|
....*..
gi 2095223075 221 RHQTAMP 227
Cdd:COG0444 239 FENPRHP 245
|
|
| ABC_Pro_Gly_Betaine |
cd03294 |
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ... |
5-220 |
2.52e-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: 110.81 E-value: 2.52e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 5 IKNLTGGYGKKPIIK---------NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIH 71
Cdd:cd03294 18 FKLLAKGKSKEEILKktgqtvgvnDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIaamsRKELR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 72 AYR--------QHLSYIPEapviydaLTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVM 143
Cdd:cd03294 98 ELRrkkismvfQSFALLPH-------RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVG 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 144 IICAFIVEPDFYIIDEPFLGLDPIGIQSMLD-LMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:cd03294 171 LARALAVDPDILLMDEAFSALDPLIRREMQDeLLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEI 248
|
|
| ABC_Mj1267_LivG_branched |
cd03219 |
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ... |
4-222 |
2.95e-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: 109.83 E-value: 2.95e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAYRQHLsyIPEA 83
Cdd:cd03219 2 EVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDG----EDITGLPPHE--IARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 84 --------PVIYDALTLKEHIEMTAMA----------YSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMII 145
Cdd:cd03219 76 gigrtfqiPRLFPELTVLENVMVAAQArtgsglllarARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIA 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 146 CAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:cd03219 156 RALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRN 232
|
|
| ABC_KpsT_Wzt |
cd03220 |
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ... |
1-215 |
5.24e-29 |
|
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: 108.77 E-value: 5.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikedihayrqHLSYI 80
Cdd:cd03220 21 KKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG------------RVSSL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYD-ALTLKEHIEMTAMAYSIDyDTAMARALPLLKTF-RLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:cd03220 89 LGLGGGFNpELTGRENIYLNGRLLGLS-RKEIDEKIDEIIEFsELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLID 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 159 EPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
|
|
| ABC_cobalt_CbiO_domain2 |
cd03226 |
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ... |
4-212 |
9.62e-29 |
|
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: 107.73 E-value: 9.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKP-IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEdiHAYRQHLSYIPE 82
Cdd:cd03226 1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIKA--KERRKSIGYVMQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APviYDAL---TLKEHIEMTAMAYSIDYDTAMAralpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:cd03226 79 DV--DYQLftdSVREELLLGLKELDAGNEQAET----VLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 160 PFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIV 212
Cdd:cd03226 153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
|
|
| fecE |
PRK11231 |
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE; |
1-215 |
1.32e-28 |
|
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 108.56 E-value: 1.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG-----DMSISGINIKEdihaYRQ 75
Cdd:PRK11231 1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGtvflgDKPISMLSSRQ----LAR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLSYIPEAPVIYDALTLKEHIEMTAMAY-------SIDYDTAMARALPLLKTFRLEDQLhifPSHFSKGMKQKVMIICAF 148
Cdd:PRK11231 77 RLALLPQHHLTPEGITVRELVAYGRSPWlslwgrlSAEDNARVNQAMEQTRINHLADRR---LTDLSGGQRQRAFLAMVL 153
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 149 IVEPDFYIIDEPFLGLDpIGIQ-SMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK11231 154 AQDTPVVLLDEPTTYLD-INHQvELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQG 220
|
|
| MdlB |
COG1132 |
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms]; |
2-220 |
1.47e-28 |
|
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 112.95 E-value: 1.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:COG1132 339 EIEFENVSFSYpGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLESLRRQIGV 418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAlTLKEHIemtamAYS-IDYDTA-------MARALPLLKtfRLEDQLHiFP-----SHFSKGMKQKVMIIC 146
Cdd:COG1132 419 VPQDTFLFSG-TIRENI-----RYGrPDATDEeveeaakAAQAHEFIE--ALPDGYD-TVvgergVNLSGGQRQRIAIAR 489
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 147 AFIVEPDFYIIDEPFLGLDPIG---IQSMLD-LMAskkeeGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG1132 490 ALLKDPPILILDEATSALDTETealIQEALErLMK-----GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGTHEEL 561
|
|
| ABCC_Glucan_exporter_like |
cd03254 |
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ... |
3-223 |
1.48e-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: 107.70 E-value: 1.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYI 80
Cdd:cd03254 3 IEFENVNFSYdEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIGVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYdALTLKEHIEM---TAMAYSIDYDTAMARALPLLKtfRLEDQLHIFPSH----FSKGMKQKVMIICAFIVEPD 153
Cdd:cd03254 83 LQDTFLF-SGTIMENIRLgrpNATDEEVIEAAKEAGAHDFIM--KLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPK 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 154 FYIIDEPFLGLDPIG---IQS-MLDLMaskkeEGRTVLMSTHILATAeRYCDRFIILDQGEIVAMGNLEALRHQ 223
Cdd:cd03254 160 ILILDEATSNIDTETeklIQEaLEKLM-----KGRTSIIIAHRLSTI-KNADKILVLDDGKIIEEGTHDELLAK 227
|
|
| TagH |
COG1134 |
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ... |
11-218 |
1.93e-28 |
|
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 107.86 E-value: 1.93e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 11 GYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG----DMSIS-------GINikedihayrqhlsy 79
Cdd:COG1134 35 RREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGrvevNGRVSallelgaGFH-------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 iPEapviydaLTLKEHIEMTAMAYSIDYDtAMARALPLLKTF-RLEDQLHIfP-SHFSKGMKQKVMIICAFIVEPDFYII 157
Cdd:COG1134 101 -PE-------LTGRENIYLNGRLLGLSRK-EIDEKFDEIVEFaELGDFIDQ-PvKTYSSGMRARLAFAVATAVDPDILLV 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 158 DE-------PFLgldpigiQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLE 218
Cdd:COG1134 171 DEvlavgdaAFQ-------KKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPE 231
|
|
| ABC_Carb_Monos_I |
cd03216 |
First domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-213 |
3.33e-28 |
|
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: 104.82 E-value: 3.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYRqhlsyi 80
Cdd:cd03216 1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGkeVSFASPRDARR------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 peAPViydaltlkehiemtAMAYsidydtamaralpllktfrledQLhifpshfSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:cd03216 75 --AGI--------------AMVY----------------------QL-------SVGERQMVEIARALARNARLLILDEP 109
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVVG 162
|
|
| cbiO |
TIGR01166 |
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ... |
17-191 |
3.90e-28 |
|
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: 105.58 E-value: 3.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI---KEDIHAYRQHLSYIPEAP--VIYDAlT 91
Cdd:TIGR01166 7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLdysRKGLLERRQRVGLVFQDPddQLFAA-D 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 92 LKEHIEMTAMAYSIDYDTAMAR---ALPLLKTFRLEDQLhifPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG 168
Cdd:TIGR01166 86 VDQDVAFGPLNLGLSEAEVERRvreALTAVGASGLRERP---THCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
|
170 180
....*....|....*....|...
gi 2095223075 169 IQSMLDLMASKKEEGRTVLMSTH 191
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVISTH 185
|
|
| cbiO |
PRK13639 |
cobalt transporter ATP-binding subunit; Provisional |
18-215 |
8.34e-28 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 107.09 E-value: 8.34e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKED---IHAYRQHLSYIPEAPviyD----AL 90
Cdd:PRK13639 18 LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDkksLLEVRKTVGIVFQNP---DdqlfAP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 91 TLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQ 170
Cdd:PRK13639 95 TVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGAS 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095223075 171 SMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK13639 175 QIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEG 219
|
|
| cbiO |
PRK13652 |
cobalt transporter ATP-binding subunit; Provisional |
3-218 |
1.12e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 106.81 E-value: 1.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSYI 80
Cdd:PRK13652 4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPItKENIREVRKFVGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAP--VIYDAlTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:PRK13652 84 FQNPddQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 159 EPFLGLDPIGIQSMLDLM-ASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLE 218
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLnDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVE 223
|
|
| PRK13651 |
PRK13651 |
cobalt transporter ATP-binding subunit; Provisional |
1-216 |
1.96e-27 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 106.71 E-value: 1.96e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKK-PI----IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDiHAYRQ 75
Cdd:PRK13651 1 MQIKVKNIVKIFNKKlPTelkaLDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNK-KKTKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLSYIPEAPV----------------------------IYDAlTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRL-EDQ 126
Cdd:PRK13651 80 KEKVLEKLVIqktrfkkikkikeirrrvgvvfqfaeyqLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 127 LHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIIL 206
Cdd:PRK13651 159 LQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFF 238
|
250
....*....|
gi 2095223075 207 DQGEIVAMGN 216
Cdd:PRK13651 239 KDGKIIKDGD 248
|
|
| CydC |
COG4987 |
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ... |
2-223 |
2.26e-27 |
|
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: 109.47 E-value: 2.26e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLS 78
Cdd:COG4987 333 SLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDlDEDDLRRRIA 412
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDAlTLKEHIEMTAMAYSidyDTAMARALpllKTFRLEDQLHIFP-----------SHFSKGMKQKVMIICA 147
Cdd:COG4987 413 VVPQRPHLFDT-TLRENLRLARPDAT---DEELWAAL---ERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARA 485
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 148 FIVEPDFYIIDEPFLGLDPIGIQSML-DLMASKKeeGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEALRHQ 223
Cdd:COG4987 486 LLRDAPILLLDEPTEGLDAATEQALLaDLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQ 559
|
|
| PRK11264 |
PRK11264 |
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional |
2-220 |
4.06e-27 |
|
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 104.45 E-value: 4.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI---------KEDIHA 72
Cdd:PRK11264 3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtarslsqqKGLIRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 73 YRQHLSYIPEAPVIYDALTLKEH-IEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVE 151
Cdd:PRK11264 83 LRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMR 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 152 PDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK11264 163 PEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKAL 231
|
|
| LivG |
COG0411 |
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ... |
4-222 |
1.69e-26 |
|
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: 103.19 E-value: 1.69e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIH---AYR------ 74
Cdd:COG0411 6 EVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDG----RDITglpPHRiarlgi 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 ----QHLSYIPEapviydaLTLKEHIEMTAMA---------------YSIDYDTAMARALPLLKTFRLEDQLHIFPSHFS 135
Cdd:COG0411 82 artfQNPRLFPE-------LTVLENVLVAAHArlgrgllaallrlprARREEREARERAEELLERVGLADRADEPAGNLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 136 KGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAM 214
Cdd:COG0411 155 YGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRlRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAE 234
|
....*...
gi 2095223075 215 GNLEALRH 222
Cdd:COG0411 235 GTPAEVRA 242
|
|
| CydD |
TIGR02857 |
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ... |
2-206 |
5.04e-26 |
|
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex. Unfortunately, the gene symbol nomenclature adopted based on this operon in B. subtilis assigns cydC to the third gene in the operon where this gene is actually homologous to the E. coli cydD gene. We have chosen to name all homologs in this family in accordance with the precedence of publication of the E. coli name, CydD
Pssm-ID: 274323 [Multi-domain] Cd Length: 529 Bit Score: 105.45 E-value: 5.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:TIGR02857 321 SLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADaDADSWRDQIAW 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAlTLKEHIEMTAMAYSidyDTAMARAL------PLLKTFR--LEDQLHIFPSHFSKGMKQKVMIICAFIVE 151
Cdd:TIGR02857 401 VPQHPFLFAG-TIAENIRLARPDAS---DAEIREALeragldEFVAALPqgLDTPIGEGGAGLSGGQAQRLALARAFLRD 476
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 152 PDFYIIDEPFLGLDPIGIQSMLDLMAsKKEEGRTVLMSTHILATAERyCDRFIIL 206
Cdd:TIGR02857 477 APLLLLDEPTAHLDAETEAEVLEALR-ALAQGRTVLLVTHRLALAAL-ADRIVVL 529
|
|
| cbiO |
PRK13637 |
energy-coupling factor transporter ATPase; |
1-216 |
7.97e-26 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 102.05 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGK-----KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDihayRQ 75
Cdd:PRK13637 1 MSIKIENLTHIYMEgtpfeKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDK----KV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLSYI----------PEAPVIYDalTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRL--EDQLHIFPSHFSKGMKQKVM 143
Cdd:PRK13637 77 KLSDIrkkvglvfqyPEYQLFEE--TIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVA 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 144 IICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:PRK13637 155 IAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKElHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228
|
|
| PRK10895 |
PRK10895 |
lipopolysaccharide ABC transporter ATP-binding protein; Provisional |
2-220 |
1.18e-25 |
|
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 100.74 E-value: 1.18e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISginiKEDI-----HAY-RQ 75
Cdd:PRK10895 3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIID----DEDIsllplHARaRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLSYIPEAPVIYDALTLKEHIeMTAMAYSIDYDTAMA--RALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPD 153
Cdd:PRK10895 79 GIGYLPQEASIFRRLSVYDNL-MAVLQIRDDLSAEQRedRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPK 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK10895 158 FILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224
|
|
| cbiO |
PRK13641 |
energy-coupling factor transporter ATPase; |
1-212 |
1.61e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 101.06 E-value: 1.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYG-----KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-----KEDI 70
Cdd:PRK13641 1 MSIKFENVDYIYSpgtpmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetgNKNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 71 HAYRQHLSYI---PEAPVIYDalTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQL-HIFPSHFSKGMKQKVMIIC 146
Cdd:PRK13641 81 KKLRKKVSLVfqfPEAQLFEN--TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDLiSKSPFELSGGQMRRVAIAG 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 147 AFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIV 212
Cdd:PRK13641 159 VMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLI 224
|
|
| cbiO |
PRK13631 |
cobalt transporter ATP-binding subunit; Provisional |
3-231 |
1.72e-25 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 101.85 E-value: 1.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKP-----IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHL 77
Cdd:PRK13631 22 LRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELIT 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYI--------------------PEAPVIYDalTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRL-EDQLHIFPSHFSK 136
Cdd:PRK13631 102 NPYskkiknfkelrrrvsmvfqfPEYQLFKD--TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLSG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 137 GMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:PRK13631 180 GQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKTGT 259
|
250
....*....|....*.
gi 2095223075 217 -LEALRHQTAMPHATL 231
Cdd:PRK13631 260 pYEIFTDQHIINSTSI 275
|
|
| cbiO |
PRK13646 |
energy-coupling factor transporter ATPase; |
1-224 |
2.08e-25 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 101.01 E-value: 2.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGK-----KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-----KEDI 70
Cdd:PRK13646 1 MTIRFDNVSYTYQKgtpyeHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIthktkDKYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 71 HAYRQHLSYI---PEAPVIYDalTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLE-DQLHIFPSHFSKGMKQKVMIIC 146
Cdd:PRK13646 81 RPVRKRIGMVfqfPESQLFED--TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVS 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 147 AFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQT 224
Cdd:PRK13646 159 ILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSlQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDK 237
|
|
| rim_protein |
TIGR01257 |
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ... |
16-223 |
5.30e-25 |
|
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: 103.55 E-value: 5.30e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 16 PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEAPVIYDALTLKEH 95
Cdd:TIGR01257 1953 PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREH 2032
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 96 IEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDL 175
Cdd:TIGR01257 2033 LYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNT 2112
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095223075 176 MASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQ 223
Cdd:TIGR01257 2113 IVSIIREGRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHLKSK 2160
|
|
| 3a01208 |
TIGR00958 |
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other] |
14-226 |
9.66e-25 |
|
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 102.49 E-value: 9.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 14 KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYIPEAPVIYdALTL 92
Cdd:TIGR00958 493 DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQyDHHYLHRQVALVGQEPVLF-SGSV 571
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 KEHIemtamAYSIDYdTAMARALPLLKTFRLEDQLHIFP-----------SHFSKGMKQKVMIICAFIVEPDFYIIDEPF 161
Cdd:TIGR00958 572 RENI-----AYGLTD-TPDEEIMAAAKAANAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 162 LGLDpigIQSMLDLMASKKEEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEALRHQTAM 226
Cdd:TIGR00958 646 SALD---AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQGC 706
|
|
| cbiO |
PRK13635 |
energy-coupling factor ABC transporter ATP-binding protein; |
3-232 |
1.35e-24 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 98.55 E-value: 1.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE----DIhayRQH 76
Cdd:PRK13635 6 IRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEetvwDV---RRQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 LSYIPEAP--------VIYD-ALTLKEHiemtamaySIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICA 147
Cdd:PRK13635 83 VGMVFQNPdnqfvgatVQDDvAFGLENI--------GVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 148 FIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGR-TVLMSTHILATAERyCDRFIILDQGEIVAMGN-LEALRHQTA 225
Cdd:PRK13635 155 LALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTpEEIFKSGHM 233
|
....*..
gi 2095223075 226 MPHATLD 232
Cdd:PRK13635 234 LQEIGLD 240
|
|
| PRK13540 |
PRK13540 |
cytochrome c biogenesis protein CcmA; Provisional |
7-191 |
1.53e-24 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 96.56 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 7 NLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEAPVI 86
Cdd:PRK13540 6 ELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGHRSGI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 87 YDALTLKEHIemtamAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDP 166
Cdd:PRK13540 86 NPYLTLRENC-----LYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
|
170 180
....*....|....*....|....*
gi 2095223075 167 IGIQSMLDLMASKKEEGRTVLMSTH 191
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGGAVLLTSH 185
|
|
| livF |
PRK11614 |
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF; |
3-231 |
1.84e-24 |
|
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 97.26 E-value: 1.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE--DIHAYRQHLSYI 80
Cdd:PRK11614 6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwqTAKIMREAVAIV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAM-AYSIDYDTAMARALPLLKtfRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:PRK11614 86 PEGRRVFSRMTVEENLAMGGFfAERDQFQERIKWVYELFP--RLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 160 PFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTAMPHATL 231
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLANEAVRSAYL 235
|
|
| ABCC_MRP_domain2 |
cd03244 |
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ... |
3-216 |
3.14e-24 |
|
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: 96.41 E-value: 3.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:cd03244 3 IEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiGLHDLRSRISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAlTLKEHIEmtamAYSIDYDTAMARALPL--LKTF------RLEDQLHIFPSHFSKGMKQkvmIIC---AF 148
Cdd:cd03244 83 IPQDPVLFSG-TIRSNLD----PFGEYSDEELWQALERvgLKEFveslpgGLDTVVEEGGENLSVGQRQ---LLClarAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIG---IQSMLdlmaskKEE--GRTVLMSTHILAT-AEryCDRFIILDQGEIVAMGN 216
Cdd:cd03244 155 LRKSKILVLDEATASVDPETdalIQKTI------REAfkDCTVLTIAHRLDTiID--SDRILVLDKGRVVEFDS 220
|
|
| ABCC_bacteriocin_exporters |
cd03245 |
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ... |
14-215 |
4.86e-24 |
|
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.
Pssm-ID: 213212 [Multi-domain] Cd Length: 220 Bit Score: 95.73 E-value: 4.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 14 KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYIPEAPVIYDAlTL 92
Cdd:cd03245 16 EIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNIGYVPQDVTLFYG-TL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 KEHIemtAMAYSIDYDTAMARALPL--LKTFR------LEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPflgl 164
Cdd:cd03245 95 RDNI---TLGAPLADDERILRAAELagVTDFVnkhpngLDLQIGERGRGLSGGQRQAVALARALLNDPPILLLDEP---- 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 165 dpigiQSMLDLMASKK--------EEGRTVLMSTHILAtAERYCDRFIILDQGEIVAMG 215
Cdd:cd03245 168 -----TSAMDMNSEERlkerlrqlLGDKTLIIITHRPS-LLDLVDRIIVMDSGRIVADG 220
|
|
| ABC_MalK_N |
cd03301 |
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ... |
3-215 |
4.96e-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: 95.40 E-value: 4.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKeDIHAYRQHLSYIPE 82
Cdd:cd03301 1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVT-DLPPKDRDIAMVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd03301 80 NYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 163 GLDP-IGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03301 160 NLDAkLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
|
|
| metN |
PRK11153 |
DL-methionine transporter ATP-binding subunit; Provisional |
3-215 |
7.67e-24 |
|
DL-methionine transporter ATP-binding subunit; Provisional
Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 97.56 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY--GKKPII--KNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-----KEDIHAY 73
Cdd:PRK11153 2 IELKNISKVFpqGGRTIHalNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLtalseKELRKAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 74 R------QH---LSyipeAPVIYD--ALTL------KEHIEmtamaysidydtamARALPLLKTFRLEDQLHIFPSHFSK 136
Cdd:PRK11153 82 RqigmifQHfnlLS----SRTVFDnvALPLelagtpKAEIK--------------ARVTELLELVGLSDKADRYPAQLSG 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 137 GMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK11153 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDiNRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQG 223
|
|
| ABC_PstB_phosphate_transporter |
cd03260 |
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ... |
3-220 |
9.30e-24 |
|
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: 95.33 E-value: 9.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLL-----TPTEGDMSISGINIKE---DIHAYR 74
Cdd:cd03260 1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDldvDVLELR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 -------QHLSYIPEApvIYD--ALTLKEHIEmtamaysIDYDTAMARALPLLKTFRL----EDQLHifPSHFSKGMKQK 141
Cdd:cd03260 81 rrvgmvfQKPNPFPGS--IYDnvAYGLRLHGI-------KLKEELDERVEEALRKAALwdevKDRLH--ALGLSGGQQQR 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 142 VMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:cd03260 150 LCLARALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
|
|
| btuD |
PRK09536 |
corrinoid ABC transporter ATPase; Reviewed |
1-215 |
1.27e-23 |
|
corrinoid ABC transporter ATPase; Reviewed
Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 97.99 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:PRK09536 2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEAlSARAASRRVAS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDALTLKEHIEMT--------AMAYSIDyDTAMARALPLLKTFRLEDQlhifP-SHFSKGMKQKVMIICAFIV 150
Cdd:PRK09536 82 VPQDTSLSFEFDVRQVVEMGrtphrsrfDTWTETD-RAAVERAMERTGVAQFADR----PvTSLSGGERQRVLLARALAQ 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 151 EPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK09536 157 ATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAG 221
|
|
| ModF |
COG1119 |
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ... |
3-220 |
1.32e-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: 95.15 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG-DMSISGINI-KEDIHAYRQHLSYI 80
Cdd:COG1119 4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRgGEDVWELRKRIGLV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 -PEAPVIYDALTLKEHIEMTAmAY-SI----DYDTAM-ARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPD 153
Cdd:COG1119 84 sPALQLRFPRDETVLDVVLSG-FFdSIglyrEPTDEQrERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPE 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTH----ILAtaeryC-DRFIILDQGEIVAMGNLEAL 220
Cdd:COG1119 163 LLILDEPTAGLDLGARELLLALLDKlAAEGAPTLVLVTHhveeIPP-----GiTHVLLLKDGRVVAAGPKEEV 230
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
20-236 |
1.46e-23 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 99.04 E-value: 1.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEAPVIYDALTLKEHIEMT 99
Cdd:NF033858 284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELH 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 100 AMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG----IQSMLDL 175
Cdd:NF033858 364 ARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVArdmfWRLLIEL 443
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 176 masKKEEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEALRHQTAmpHATLDEIYI 236
Cdd:NF033858 444 ---SREDGVTIFISTHFMNEAER-CDRISLMHAGRVLASDTPAALVAARG--AATLEEAFI 498
|
|
| cbiO |
PRK13634 |
cobalt transporter ATP-binding subunit; Provisional |
18-215 |
1.53e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 95.86 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSI------SGINIKeDIHAYRQHLSYI---PEAPVIYD 88
Cdd:PRK13634 23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNK-KLKPLRKKVGIVfqfPEHQLFEE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 89 alTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRL-EDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPI 167
Cdd:PRK13634 102 --TVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095223075 168 GIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK13634 180 GRKEMMEMFYKlHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQG 228
|
|
| PRK10619 |
PRK10619 |
histidine ABC transporter ATP-binding protein HisP; |
12-220 |
1.81e-23 |
|
histidine ABC transporter ATP-binding protein HisP;
Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 95.04 E-value: 1.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 12 YGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI--------------KEDIHAYRQHL 77
Cdd:PRK10619 15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdkdgqlkvadKNQLRLLRTRL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDALTLKEHI-EMTAMAYSIDYDTAMARALPLLKTFRLEDQLHI-FPSHFSKGMKQKVMIICAFIVEPDFY 155
Cdd:PRK10619 95 TMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGkYPVHLSGGQQQRVSIARALAMEPEVL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 156 IIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK10619 175 LFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQL 239
|
|
| cbiO |
PRK13647 |
cobalt transporter ATP-binding subunit; Provisional |
3-220 |
1.96e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 95.57 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY--GKKPIiKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSY 79
Cdd:PRK13647 5 IEVEDLHFRYkdGTKAL-KGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVnAENEKWVRSKVGL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 I---PEAPVIydALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYI 156
Cdd:PRK13647 84 VfqdPDDQVF--SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIV 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 157 IDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK13647 162 LDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLL 225
|
|
| hmuV |
PRK13548 |
hemin importer ATP-binding subunit; Provisional |
1-224 |
2.15e-23 |
|
hemin importer ATP-binding subunit; Provisional
Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 94.84 E-value: 2.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAYR-----Q 75
Cdd:PRK13548 1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNG----RPLADWSpaelaR 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLSYIPEAPVIYDALTLKEHIEMTAMAYSIDY-------DTAMARA-LPLLKTfRLEDQLhifpshfSKGMKQKVMI--I 145
Cdd:PRK13548 77 RRAVLPQHSSLSFPFTVEEVVAMGRAPHGLSRaeddalvAAALAQVdLAHLAG-RDYPQL-------SGGEQQRVQLarV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 146 CAFIVEPD----FYIIDEPFLGLDPIGIQSMLDLMASK-KEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN-LEA 219
Cdd:PRK13548 149 LAQLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLaHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTpAEV 228
|
....*
gi 2095223075 220 LRHQT 224
Cdd:PRK13548 229 LTPET 233
|
|
| ABC_FtsE |
cd03292 |
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ... |
3-211 |
4.68e-23 |
|
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: 92.86 E-value: 4.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKK-PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHL 77
Cdd:cd03292 1 IEFINVTKTYPNGtAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVsdlrGRAIPYLRRKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYI-PEAPVIYDaLTLKEHIemtAMAYSIDYDT---AMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPD 153
Cdd:cd03292 81 GVVfQDFRLLPD-RNVYENV---AFALEVTGVPpreIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:cd03292 157 ILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHAKELVDTTRHRVIALERGKL 214
|
|
| ThiQ |
COG3840 |
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism]; |
4-220 |
4.74e-23 |
|
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 93.28 E-value: 4.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPiiKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINikedihayrqHLSYIPEA 83
Cdd:COG3840 3 RLDDLTYRYGDFP--LRFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD----------LTALPPAE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 84 -PV--------IYDALTLKEHIEM---TAMAYSIDYDTAMARALpllKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVE 151
Cdd:COG3840 71 rPVsmlfqennLFPHLTVAQNIGLglrPGLKLTAEQRAQVEQAL---ERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 152 PDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG3840 148 RPILLLDEPFSALDPALRQEMLDLVDElCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAAL 217
|
|
| cbiO |
PRK13636 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
7.44e-23 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 94.14 E-value: 7.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI---KEDIHAYRQHLSYIPEAP--VIYDAlTL 92
Cdd:PRK13636 22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdysRKGLMKLRESVGMVFQDPdnQLFSA-SV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 KEHIEMTAMAYSIDYDTAMARALPLLKTFRLEdQLHIFPSH-FSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQS 171
Cdd:PRK13636 101 YQDVSFGAVNLKLPEDEVRKRVDNALKRTGIE-HLKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGVSE 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095223075 172 MLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:PRK13636 180 IMKLLVEmQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGN 225
|
|
| PhnL |
COG4778 |
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ... |
16-209 |
8.96e-23 |
|
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: 92.50 E-value: 8.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 16 PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSI----SGINIKE----DIHAYR--------QHLSY 79
Cdd:COG4778 25 PVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQasprEILALRrrtigyvsQFLRV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAP---VIYDALtlkehIEMtamaySIDYDTAMARALPLLKTFRLEDQL-HIFPSHFSKGMKQKVMIICAFIVEPDFY 155
Cdd:COG4778 105 IPRVSaldVVAEPL-----LER-----GVDREEARARARELLARLNLPERLwDLPPATFSGGEQQRVNIARGFIADPPLL 174
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 156 IIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQG 209
Cdd:COG4778 175 LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPF 228
|
|
| ABCC_ATM1_transporter |
cd03253 |
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ... |
3-220 |
1.31e-22 |
|
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: 92.29 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYG-KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYI 80
Cdd:cd03253 1 IEFENVTFAYDpGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvTLDSLRRAIGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDaltlkehiemTAMAYSIDY------DTAMARAlplLKTFRLEDQLHIFPSHF-----------SKGMKQKVM 143
Cdd:cd03253 81 PQDTVLFN----------DTIGYNIRYgrpdatDEEVIEA---AKAAQIHDKIMRFPDGYdtivgerglklSGGEKQRVA 147
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 144 IICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAsKKEEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEAL 220
Cdd:cd03253 148 IARAILKNPPILLLDEATSALDTHTEREIQAALR-DVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEEL 222
|
|
| ABC_PotA_N |
cd03300 |
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ... |
3-216 |
1.47e-22 |
|
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: 91.91 E-value: 1.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIkEDIHAYRQHLSYIPE 82
Cdd:cd03300 1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDI-TNLPPHKRPVNTVFQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:cd03300 80 NYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 163 GLDPIGIQSM-LDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:cd03300 160 ALDLKLRKDMqLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGT 214
|
|
| ABCC_Protease_Secretion |
cd03246 |
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ... |
4-211 |
1.63e-22 |
|
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.
Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 90.35 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYG--KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYI 80
Cdd:cd03246 2 EVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQwDPNELGDHVGYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDAlTLKEHIemtamaysidydtamaralpllktfrledqlhifpshFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:cd03246 82 PQDDELFSG-SIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEP 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERyCDRFIILDQGEI 211
Cdd:cd03246 124 NSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLAS-ADRILVLEDGRV 173
|
|
| PRK10070 |
PRK10070 |
proline/glycine betaine ABC transporter ATP-binding protein ProV; |
18-225 |
3.51e-22 |
|
proline/glycine betaine ABC transporter ATP-binding protein ProV;
Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 93.94 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHA-----YRQHLSYIPEAPVIYDALTL 92
Cdd:PRK10070 44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevRRKKIAMVFQSFALMPHMTV 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 KEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSM 172
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEM 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 173 LD-LMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTA 225
Cdd:PRK10070 204 QDeLVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPA 257
|
|
| cbiO |
PRK13643 |
energy-coupling factor transporter ATPase; |
20-230 |
3.61e-22 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 92.49 E-value: 3.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG-----DMSISGINIKEDIHAYRQHLSYIPEAP--VIYDALTL 92
Cdd:PRK13643 24 DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGkvtvgDIVVSSTSKQKEIKPVRKKVGVVFQFPesQLFEETVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 KEhIEMTAMAYSIDYDTAMARALPLLKTFRLEDQL-HIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQS 171
Cdd:PRK13643 104 KD-VAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 172 MLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN-------LEALR-HQTAMPHAT 230
Cdd:PRK13643 183 MMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTpsdvfqeVDFLKaHELGVPKAT 249
|
|
| ABCC_cytochrome_bd |
cd03247 |
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ... |
3-215 |
7.09e-22 |
|
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome bd biogenesis. The CydC and CydD proteins are important for the formation of cytochrome bd terminal oxidase of E. coli and it has been proposed that they were necessary for biosynthesis of the cytochrome bd quinol oxidase and for periplasmic c-type cytochromes. CydCD were proposed to determine a heterooligomeric complex important for heme export into the periplasm or to be involved in the maintenance of the proper redox state of the periplasmic space. In Bacillus subtilis, the absence of CydCD does not affect the presence of halo-cytochrome c in the membrane and this observation suggests that CydCD proteins are not involved in the export of heme in this organism.
Pssm-ID: 213214 [Multi-domain] Cd Length: 178 Bit Score: 88.91 E-value: 7.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYG--KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYI 80
Cdd:cd03247 1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDAlTLKEHIEmtamaysidydtamaralpllktfrledqlhifpSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:cd03247 81 NQRPYLFDT-TLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEP 125
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYcDRFIILDQGEIVAMG 215
Cdd:cd03247 126 TVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
|
|
| ABC_ThiQ_thiamine_transporter |
cd03298 |
ATP-binding cassette domain of the thiamine transport system; Part of the ... |
20-215 |
2.02e-21 |
|
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: 88.70 E-value: 2.02e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELT--DGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQhLSYIPEAPVIYDALTLKEHIE 97
Cdd:cd03298 14 PMHFDLTfaQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQENNLFAHLTVEQNVG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 98 M---TAMAYSIDYDTAMARALPLLKTFRLEDQLhifPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLD 174
Cdd:cd03298 93 LglsPGLKLTAEDRQAIEVALARVGLAGLEKRL---PGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLD 169
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095223075 175 LMA-SKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03298 170 LVLdLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
|
|
| ABCC_MsbA |
cd03251 |
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ... |
3-220 |
2.57e-21 |
|
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; MsbA is an essential ABC transporter, closely related to eukaryotic MDR proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213218 [Multi-domain] Cd Length: 234 Bit Score: 88.83 E-value: 2.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKK--PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:cd03251 1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAlTLKEHIemtamAYSiDYDTAMARALPLLKT-----F--RLEDQLHIF----PSHFSKGMKQKVMIICAF 148
Cdd:cd03251 81 VSQDVFLFND-TVAENI-----AYG-RPGATREEVEEAARAanaheFimELPEGYDTVigerGVKLSGGQRQRIAIARAL 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIG---IQSMLD-LMaskkeEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEAL 220
Cdd:cd03251 154 LKDPPILILDEATSALDTESerlVQAALErLM-----KNRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEEL 223
|
|
| AbcC |
COG1135 |
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism]; |
3-225 |
3.40e-21 |
|
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 90.52 E-value: 3.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLT----GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYR 74
Cdd:COG1135 2 IELENLSktfpTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLtalsERELRAAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QHLSYIP------EAPVIYD--ALTL------KEHIEmtamaysidydtamARALPLLKTFRLEDQLHIFPSHFSKGMKQ 140
Cdd:COG1135 82 RKIGMIFqhfnllSSRTVAEnvALPLeiagvpKAEIR--------------KRVAELLELVGLSDKADAYPSQLSGGQKQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 141 KVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEA 219
Cdd:COG1135 148 RVGIARALANNPKVLLCDEATSALDPETTRSILDLLKDiNRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLD 227
|
250
....*....|
gi 2095223075 220 L----RHQTA 225
Cdd:COG1135 228 VfanpQSELT 237
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
5-211 |
4.72e-21 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 91.28 E-value: 4.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 5 IKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSIS-GINIkedihAY-RQHLSYIPE 82
Cdd:COG0488 1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRI-----GYlPQEPPLDDD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVI----------YDALTLKEHIEMTAMAYSIDYD---------------TAMARALPLLKTFRLEDQLHIFP-SHFSK 136
Cdd:COG0488 76 LTVLdtvldgdaelRALEAELEELEAKLAEPDEDLErlaelqeefealggwEAEARAEEILSGLGFPEEDLDRPvSELSG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 137 GMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQ---SMLdlmasKKEEGrTVLMSTHilataERY-----CDRFIILDQ 208
Cdd:COG0488 156 GWRRRVALARALLSEPDLLLLDEPTNHLDLESIEwleEFL-----KNYPG-TVLVVSH-----DRYfldrvATRILELDR 224
|
...
gi 2095223075 209 GEI 211
Cdd:COG0488 225 GKL 227
|
|
| nikE |
PRK10419 |
nickel ABC transporter ATP-binding protein NikE; |
7-222 |
4.78e-21 |
|
nickel ABC transporter ATP-binding protein NikE;
Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 88.98 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 7 NLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHLSYipe 82
Cdd:PRK10419 17 GLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLaklnRAQRKAFRRDIQM--- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 apVIYDAL-------TLKEHIEmTAMAYSIDYDTA--MARALPLLKTFRLEDQ-LHIFPSHFSKGMKQKVMIICAFIVEP 152
Cdd:PRK10419 94 --VFQDSIsavnprkTVREIIR-EPLRHLLSLDKAerLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCLARALAVEP 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 153 DFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTV-LMSTHILATAERYCDRFIILDQGEIV---AMGNLEALRH 222
Cdd:PRK10419 171 KLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIVetqPVGDKLTFSS 244
|
|
| cbiO |
PRK13632 |
cobalt transporter ATP-binding subunit; Provisional |
3-215 |
6.65e-21 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 88.51 E-value: 6.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYG--KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSY 79
Cdd:PRK13632 8 IKVENVSFSYPnsENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIsKENLKEIRKKIGI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 I---PEAPVIydALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYI 156
Cdd:PRK13632 88 IfqnPDNQFI--GATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 157 IDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMS-TH-----ILAtaerycDRFIILDQGEIVAMG 215
Cdd:PRK13632 166 FDESTSMLDPKGKREIKKIMVDLRKTRKKTLISiTHdmdeaILA------DKVIVFSEGKLIAQG 224
|
|
| ABC_MTABC3_MDL1_MDL2 |
cd03249 |
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ... |
3-215 |
8.15e-21 |
|
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: 87.60 E-value: 8.15e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKP---IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLS 78
Cdd:cd03249 1 IEFKNVSFRYPSRPdvpILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDAlTLKEHIemtamAYSIDYDTA--------MARALPLLKTF--RLEDQLHIFPSHFSKGMKQKVMIICAF 148
Cdd:cd03249 81 LVSQEPVLFDG-TIAENI-----RYGKPDATDeeveeaakKANIHDFIMSLpdGYDTLVGERGSQLSGGQKQRIAIARAL 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIG---IQSMLDlmasKKEEGRTVLMSTHILATAeRYCDRFIILDQGEIVAMG 215
Cdd:cd03249 155 LRNPKILLLDEATSALDAESeklVQEALD----RAMKGRTTIVIAHRLSTI-RNADLIAVLQNGQVVEQG 219
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
4-220 |
8.59e-21 |
|
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: 8.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLT----GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTP----TEGDMSISGINI----KEDIH 71
Cdd:COG4172 8 SVEDLSvafgQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpaahPSGSILFDGQDLlglsERELR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 72 AYR-QHLSYI---------PEAPV---IYDALTLkeHIEMTAMAysidydtAMARALPLLKTFRL---EDQLHIFPSHFS 135
Cdd:COG4172 88 RIRgNRIAMIfqepmtslnPLHTIgkqIAEVLRL--HRGLSGAA-------ARARALELLERVGIpdpERRLDAYPHQLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 136 KGMKQKVMIICAFIVEPDFYIIDEPFLGLDpIGIQS-MLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:COG4172 159 GGQRQRVMIAMALANEPDLLIADEPTTALD-VTVQAqILDLLKDlQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVE 237
|
....*..
gi 2095223075 214 MGNLEAL 220
Cdd:COG4172 238 QGPTAEL 244
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
19-213 |
9.05e-21 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 90.47 E-value: 9.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 19 KNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYR-------QHLSYIPeapviydA 89
Cdd:COG3845 22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSPRDAIAlgigmvhQHFMLVP-------N 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 90 LTLKEHI----EMTAMAYsIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLD 165
Cdd:COG3845 95 LTVAENIvlglEPTKGGR-LDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095223075 166 PIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:COG3845 174 PQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVG 221
|
|
| ABCG_EPDR |
cd03213 |
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ... |
1-215 |
1.00e-20 |
|
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette superfamily; ABCG transporters are involved in eye pigment (EP) precursor transport, regulation of lipid-trafficking mechanisms, and pleiotropic drug resistance (DR). DR is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. Compared to other members of the ABC transporter subfamilies, the ABCG transporter family is composed of proteins that have an ATP-binding cassette domain at the N-terminus and a TM (transmembrane) domain at the C-terminus.
Pssm-ID: 213180 [Multi-domain] Cd Length: 194 Bit Score: 86.45 E-value: 1.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGyGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTP--TEGDMSISGINIKEDihAYRQHLS 78
Cdd:cd03213 9 LTVTVKSSPSK-SGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR--SFRKIIG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDALTLKEHIEMTAMAYSIdydtamaralpllktfrledqlhifpshfSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:cd03213 86 YVPQDDILHPTLTVRETLMFAAKLRGL-----------------------------SGGERKRVSIALELVSNPSLLFLD 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 159 EPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHiLATAERY--CDRFIILDQGEIVAMG 215
Cdd:cd03213 137 EPTSGLDSSSALQVMSLLRRLADTGRTIICSIH-QPSSEIFelFDKLLLLSQGRVIYFG 194
|
|
| PRK13633 |
PRK13633 |
energy-coupling factor transporter ATPase; |
15-216 |
1.20e-20 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 87.84 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 15 KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAY--RQHLSYI---PEAPVIydA 89
Cdd:PRK13633 23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENLWdiRNKAGMVfqnPDNQIV--A 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 90 LTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGI 169
Cdd:PRK13633 101 TIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095223075 170 QSMLD-LMASKKEEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGN 216
Cdd:PRK13633 181 REVVNtIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGT 227
|
|
| ABC_CysA_sulfate_importer |
cd03296 |
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ... |
1-237 |
1.40e-20 |
|
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: 87.01 E-value: 1.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKeDIHAYRQHLSYI 80
Cdd:cd03296 1 MSIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDAT-DVPVQERNVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHI----EMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYI 156
Cdd:cd03296 80 FQHYALFRHMTVFDNVafglRVKPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 157 IDEPFLGLDpigiqsmldlmASKKEEGR------------TVLMSTHILATAERYCDRFIILDQGEIVAMGnlealrhqt 224
Cdd:cd03296 160 LDEPFGALD-----------AKVRKELRrwlrrlhdelhvTTVFVTHDQEEALEVADRVVVMNKGRIEQVG--------- 219
|
250
....*....|...
gi 2095223075 225 amphaTLDEIYIH 237
Cdd:cd03296 220 -----TPDEVYDH 227
|
|
| PRK13539 |
PRK13539 |
cytochrome c biogenesis protein CcmA; Provisional |
1-192 |
1.89e-20 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 85.70 E-value: 1.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHlsYI 80
Cdd:PRK13539 1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACH--YL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAmAYsidYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:PRK13539 79 GHRNAMKPALTVAENLEFWA-AF---LGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154
|
170 180 190
....*....|....*....|....*....|..
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEGRTVLMSTHI 192
Cdd:PRK13539 155 TAALDAAAVALFAELIRAHLAQGGIVIAATHI 186
|
|
| ssuB |
PRK11247 |
aliphatic sulfonates transport ATP-binding subunit; Provisional |
5-211 |
1.99e-20 |
|
aliphatic sulfonates transport ATP-binding subunit; Provisional
Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 87.04 E-value: 1.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 5 IKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMsISG----INIKEDIHAYRQHLSYI 80
Cdd:PRK11247 15 LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGtaplAEAREDTRLMFQDARLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYD-ALTLKEHIEmtamaysidydtamARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:PRK11247 94 PWKKVIDNvGLGLKGQWR--------------DAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 160 PFLGLDPIGIQSMLDLMASK-KEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
|
|
| cbiO |
PRK13638 |
energy-coupling factor ABC transporter ATP-binding protein; |
12-215 |
2.87e-20 |
|
energy-coupling factor ABC transporter ATP-binding protein;
Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 86.98 E-value: 2.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 12 YGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI---KEDIHAYRQHLSYI---PEAPV 85
Cdd:PRK13638 11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdysKRGLLALRQQVATVfqdPEQQI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 86 IYDaltlkehiemtamaySIDYDTAMA-RALPLLK---TFRLEDQLHIFPS-HF--------SKGMKQKVMIICAFIVEP 152
Cdd:PRK13638 91 FYT---------------DIDSDIAFSlRNLGVPEaeiTRRVDEALTLVDAqHFrhqpiqclSHGQKKRVAIAGALVLQA 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 153 DFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK13638 156 RYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHG 218
|
|
| ABC_Carb_Monos_II |
cd03215 |
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ... |
3-211 |
3.71e-20 |
|
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: 84.41 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGkkpiIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYRQHLSYI 80
Cdd:cd03215 5 LEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGkpVTRRSPRDAIRAGIAYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPviydaltlkeHIEMTAMAYSIDYDTAMaralpllktfrledqlhifPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:cd03215 81 PEDR----------KREGLVLDLSVAENIAL-------------------SSLLSGGNQQKVVLARWLARDPRVLILDEP 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 161 FLGLDpIG-IQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:cd03215 132 TRGVD-VGaKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
|
|
| ccmA |
TIGR01189 |
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ... |
6-192 |
3.87e-20 |
|
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]
Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 84.72 E-value: 3.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 6 KNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEAPV 85
Cdd:TIGR01189 4 RNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGHLPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 86 IYDALTLKEHIEMtamaYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLD 165
Cdd:TIGR01189 84 LKPELSALENLHF----WAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
|
170 180
....*....|....*....|....*..
gi 2095223075 166 PIGIQSMLDLMASKKEEGRTVLMSTHI 192
Cdd:TIGR01189 160 KAGVALLAGLLRAHLARGGIVLLTTHQ 186
|
|
| ABC_CcmA_heme_exporter |
cd03231 |
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ... |
6-192 |
4.72e-20 |
|
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.
Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 84.85 E-value: 4.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 6 KNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEAPV 85
Cdd:cd03231 4 DELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGHAPG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 86 IYDALTLKEHIEMtamaYSIDYDTamARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLD 165
Cdd:cd03231 84 IKTTLSVLENLRF----WHADHSD--EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
|
170 180
....*....|....*....|....*..
gi 2095223075 166 PIGIQSMLDLMASKKEEGRTVLMSTHI 192
Cdd:cd03231 158 KAGVARFAEAMAGHCARGGMVVLTTHQ 184
|
|
| MalK |
COG3839 |
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ... |
2-215 |
4.94e-20 |
|
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism];
Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 87.44 E-value: 4.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKeDIHAYRQHLSYIP 81
Cdd:COG3839 3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVT-DLPPKDRNIAMVF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 EAPVIYDALTLKEHiemtaMAYS-----IDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYI 156
Cdd:COG3839 82 QSYALYPHMTVYEN-----IAFPlklrkVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFL 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 157 IDEPFLGLDPIGIQSM-LDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:COG3839 157 LDEPLSNLDAKLRVEMrAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVG 216
|
|
| COG4559 |
COG4559 |
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism]; |
4-215 |
5.22e-20 |
|
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 85.94 E-value: 5.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIkEDIHAY---------R 74
Cdd:COG4559 3 EAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPL-AAWSPWelarrravlP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QH--LSYipeapviydALTLKEHIEMTAMAYSIDY---DTAMARALPLLKTFRLEDQLhiFPShFSKGMKQKVMI--ICA 147
Cdd:COG4559 82 QHssLAF---------PFTVEEVVALGRAPHGSSAaqdRQIVREALALVGLAHLAGRS--YQT-LSGGEQQRVQLarVLA 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 148 FIVEPD-----FYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:COG4559 150 QLWEPVdggprWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQG 222
|
|
| ntrCD |
TIGR01184 |
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ... |
18-209 |
5.90e-20 |
|
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: 85.21 E-value: 5.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE---DIHAYRQHLSYIPeapviydALTLKE 94
Cdd:TIGR01184 1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEpgpDRMVVFQNYSLLP-------WLTVRE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 95 HIEMTAMAYSIDYDTAMARAL--PLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSM 172
Cdd:TIGR01184 74 NIALAVDRVLPDLSKSERRAIveEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153
|
170 180 190
....*....|....*....|....*....|....*...
gi 2095223075 173 LD-LMASKKEEGRTVLMSTHILATAERYCDRFIILDQG 209
Cdd:TIGR01184 154 QEeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
|
|
| HisP |
COG4598 |
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism]; |
2-211 |
6.20e-20 |
|
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 85.62 E-value: 6.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYR----- 74
Cdd:COG4598 8 ALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGeeIRLKPDRDGELvpadr 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 --------------QH---------LSYIPEAPViydaltlkeHIemtamaYSIDYDTAMARALPLLKTFRLEDQLHIFP 131
Cdd:COG4598 88 rqlqrirtrlgmvfQSfnlwshmtvLENVIEAPV---------HV------LGRPKAEAIERAEALLAKVGLADKRDAYP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 132 SHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:COG4598 153 AHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRI 232
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
19-220 |
7.27e-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: 7.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 19 KNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYR-------QHLSYIPEapviyda 89
Cdd:COG1129 21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAagiaiihQELNLVPN------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 90 LTLKEHI----EMTAmAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLD 165
Cdd:COG1129 94 LSVAENIflgrEPRR-GGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 166 PIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG1129 173 EREVERLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
|
|
| PRK15056 |
PRK15056 |
manganese/iron ABC transporter ATP-binding protein; |
18-222 |
9.98e-20 |
|
manganese/iron ABC transporter ATP-binding protein;
Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 85.32 E-value: 9.98e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEdihAYRQHL-SYIPEA-------PV-IYD 88
Cdd:PRK15056 23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQ---ALQKNLvAYVPQSeevdwsfPVlVED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 89 ALTLKEHIEMTAMAYSIDYDTAMARALplLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG 168
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAA--LARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKT 177
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 169 IQSMLDLMASKKEEGRTVLMSTHILATAERYCDrFIILDQGEIVAMG---------NLE-----ALRH 222
Cdd:PRK15056 178 EARIISLLRELRDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGptettftaeNLElafsgVLRH 244
|
|
| cbiO |
PRK13649 |
energy-coupling factor transporter ATPase; |
20-215 |
1.07e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 85.57 E-value: 1.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIK-----EDIHAYRQHLSYI---PEAPViYDALT 91
Cdd:PRK13649 25 DVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITstsknKDIKQIRKKVGLVfqfPESQL-FEETV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 92 LKEhIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLhiF---PSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG 168
Cdd:PRK13649 104 LKD-VAFGPQNFGVSQEEAEALAREKLALVGISESL--FeknPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095223075 169 IQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK13649 181 RKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSG 227
|
|
| BtuD |
COG4138 |
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ... |
21-216 |
4.11e-19 |
|
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];
Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 83.35 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 21 INFELTDGEIVGLIGLNGAGKSTTIKHILGLLtPTEGDMSISGINIKE-DIHAYRQHLSYIPEA-------PViYDALTL 92
Cdd:COG4138 15 ISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDwSAAELARHRAYLSQQqsppfamPV-FQYLAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 keHIEMTAMAYSIdyDTAMARalpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFI-----VEPD--FYIIDEPFLGLD 165
Cdd:COG4138 93 --HQPAGASSEAV--EQLLAQ---LAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDEPMNSLD 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 166 pIGIQSMLD-LMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:COG4138 166 -VAQQAALDrLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGE 216
|
|
| PRK09984 |
PRK09984 |
phosphonate ABC transporter ATP-binding protein; |
3-211 |
5.27e-19 |
|
phosphonate ABC transporter ATP-binding protein;
Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 83.14 E-value: 5.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLT---PTEGDMSISGINIK------EDIHAY 73
Cdd:PRK09984 5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQregrlaRDIRKS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 74 RQHLSYIPEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHF--------SKGMKQKVMII 145
Cdd:PRK09984 85 RANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFahqrvstlSGGQQQRVAIA 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 146 CAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDiNQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
|
|
| ABCF_EF-3 |
cd03221 |
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ... |
3-210 |
6.72e-19 |
|
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: 80.19 E-value: 6.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDM-SISGINIkedihayrqhlSYIP 81
Cdd:cd03221 1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVtWGSTVKI-----------GYFE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 eapviydaltlkehiemtamaysidydtamaralpllktfrledqlhifpsHFSKGMKQKVMIICAFIVEPDFYIIDEPF 161
Cdd:cd03221 70 ---------------------------------------------------QLSGGEKMRLALAKLLLENPNLLLLDEPT 98
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095223075 162 LGLDPIGIQSMLDLMaskKEEGRTVLMSTHILATAERYCDRFIILDQGE 210
Cdd:cd03221 99 NHLDLESIEALEEAL---KEYPGTVILVSHDRYFLDQVATKIIELEDGK 144
|
|
| cbiO |
PRK13644 |
energy-coupling factor transporter ATPase; |
16-220 |
8.27e-19 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 83.11 E-value: 8.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 16 PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE--DIHAYRQHLSYI---PEAPVIydAL 90
Cdd:PRK13644 16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDfsKLQGIRKLVGIVfqnPETQFV--GR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 91 TLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQ 170
Cdd:PRK13644 94 TVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 2095223075 171 SMLDLMASKKEEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK13644 174 AVLERIKKLHEKGKTIVYITHNLEELHD-ADRIIVMDRGKIVLEGEPENV 222
|
|
| ABCC_Hemolysin |
cd03252 |
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ... |
17-220 |
9.30e-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: 82.15 E-value: 9.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYIPEAPVIYDAlTLKEH 95
Cdd:cd03252 17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLFNR-SIRDN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 96 IEMTAMAYS---IDYDTAMARALPLLKTFRL--EDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLD----P 166
Cdd:cd03252 96 IALADPGMSmerVIEAAKLAGAHDFISELPEgyDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALDyeseH 175
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 167 IGIQSMLDLMAskkeeGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEAL 220
Cdd:cd03252 176 AIMRNMHDICA-----GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDEL 223
|
|
| PRK13538 |
PRK13538 |
cytochrome c biogenesis heme-transporting ATPase CcmA; |
4-191 |
1.09e-18 |
|
cytochrome c biogenesis heme-transporting ATPase CcmA;
Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 81.00 E-value: 1.09e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEA 83
Cdd:PRK13538 3 EARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEYHQDLLYLGHQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 84 PVIYDALTLKEHIEMtAMAYSIDYDTAMARAlpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLG 163
Cdd:PRK13538 83 PGIKTELTALENLRF-YQRLHGPGDDEALWE--ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTA 159
|
170 180
....*....|....*....|....*...
gi 2095223075 164 LDPIGIQSMLDLMASKKEEGRTVLMSTH 191
Cdd:PRK13538 160 IDKQGVARLEALLAQHAEQGGMVILTTH 187
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
18-218 |
1.24e-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: 84.47 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG-----------DMSISGINIKEDIHAY----RQHLSYIPE 82
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGevnvrvgdewvDMTKPGPDGRGRAKRYigilHQEYDLYPH 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIyDALTlkehiemTAMAYSIDYDTAMARALPLLKTFRLEDQ-----LHIFPSHFSKGMKQKVMIICAFIVEPDFYII 157
Cdd:TIGR03269 380 RTVL-DNLT-------EAIGLELPDELARMKAVITLKMVGFDEEkaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVIL 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 158 DEPFLGLDPIGIQSMLD-LMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLE 218
Cdd:TIGR03269 452 DEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPE 513
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
3-215 |
1.34e-18 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 84.07 E-value: 1.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIH--AYRQHLSYI 80
Cdd:PRK09700 6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHklAAQLGIGII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAMAYS-------IDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPD 153
Cdd:PRK09700 86 YQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK09700 166 VIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSG 227
|
|
| nikD |
PRK10418 |
nickel transporter ATP-binding protein NikD; Provisional |
2-222 |
1.51e-18 |
|
nickel transporter ATP-binding protein NikD; Provisional
Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 81.67 E-value: 1.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGgYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTP----TEGDMSISGINIKEDihAYR-QH 76
Cdd:PRK10418 4 QIELRNIAL-QAAQPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVAPC--ALRgRK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 LSYIPEAP--VIYDALTLKEHIEMTAMAYSIDYDTAMARALplLKTFRLEDQ---LHIFPSHFSKGMKQKVMIICAFIVE 151
Cdd:PRK10418 81 IATIMQNPrsAFNPLHTMHTHARETCLALGKPADDATLTAA--LEAVGLENAarvLKLYPFEMSGGMLQRMMIALALLCE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 152 PDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:PRK10418 159 APFIIADEPTTDLDVVAQARILDLLESiVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
|
|
| cbiO |
PRK13640 |
energy-coupling factor transporter ATPase; |
3-226 |
2.20e-18 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 81.77 E-value: 2.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMS---ISGINIKED-IHAYRQH 76
Cdd:PRK13640 6 VEFKHVSFTYpdSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSkitVDGITLTAKtVWDIREK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 LSYIPEAPviydaltlkehiEMTAMAYSIDYDTAMA---RALP----------LLKTFRLEDQLHIFPSHFSKGMKQKVM 143
Cdd:PRK13640 86 VGIVFQNP------------DNQFVGATVGDDVAFGlenRAVPrpemikivrdVLADVGMLDYIDSEPANLSGGQKQRVA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 144 IICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAErYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:PRK13640 154 IAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKlKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFS 232
|
....
gi 2095223075 223 QTAM 226
Cdd:PRK13640 233 KVEM 236
|
|
| ABC_ModC_molybdenum_transporter |
cd03297 |
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ... |
20-215 |
2.77e-18 |
|
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: 80.42 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFElTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGI-----NIKEDIHAYRQHLSYIPEAPVIYDALTLKE 94
Cdd:cd03297 16 KIDFD-LNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTvlfdsRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 95 HIEMTAMAYSIDYDTAMARAlpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLD-PIGIQSML 173
Cdd:cd03297 95 NLAFGLKRKRNREDRISVDE--LLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDrALRLQLLP 172
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2095223075 174 DLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:cd03297 173 ELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
|
|
| bacteriocin_ABC |
TIGR01193 |
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ... |
3-215 |
5.93e-18 |
|
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]
Pssm-ID: 130261 [Multi-domain] Cd Length: 708 Bit Score: 82.48 E-value: 5.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYG-KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYI 80
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDiDRHTLRQFINYL 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTL---------KEHIEMTAMAYSIDYDTAMARALPLlktfRLEDQLHIFPSHFSKGMKQKVMIICAFIVE 151
Cdd:TIGR01193 554 PQEPYIFSGSILenlllgakeNVSQDEIWAACEIAEIKDDIENMPL----GYQTELSEEGSSISGGQKQRIALARALLTD 629
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 152 PDFYIIDEPFLGLDPIGIQSMLDLMASKKEegRTVLMSTHILATAERyCDRFIILDQGEIVAMG 215
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQG 690
|
|
| Uup |
COG0488 |
ATPase components of ABC transporters with duplicated ATPase domains [General function ... |
3-218 |
6.78e-18 |
|
ATPase components of ABC transporters with duplicated ATPase domains [General function prediction only];
Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 82.03 E-value: 6.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSIsGINIKedIHAYRQHLSYIPE 82
Cdd:COG0488 316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--IGYFDQHQEELDP 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 apviydALTLKEHI--------EMTAMAYsidydtaMARALpllktFRLEDQL-HIfpSHFSKGMKQKVMIICAFIVEPD 153
Cdd:COG0488 393 ------DKTVLDELrdgapggtEQEVRGY-------LGRFL-----FSGDDAFkPV--GVLSGGEKARLALAKLLLSPPN 452
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMASKkeEGrTVLMSTHilataERY-----CDRFIILDQGEIVA-MGNLE 218
Cdd:COG0488 453 VLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSH-----DRYfldrvATRILEFEDGGVREyPGGYD 515
|
|
| ABCG_White |
cd03234 |
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ... |
17-215 |
8.77e-18 |
|
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.
Pssm-ID: 213201 [Multi-domain] Cd Length: 226 Bit Score: 79.24 E-value: 8.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLtptEGDMSISG---INIKE-DIHAYRQHLSYIPEAPVIYDALTL 92
Cdd:cd03234 22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRV---EGGGTTSGqilFNGQPrKPDQFQKCVAYVRQDDILLPGLTV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 KEHIEMTAM----AYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG 168
Cdd:cd03234 99 RETLTYTAIlrlpRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2095223075 169 IQSMLDLMASKKEEGRTVLMSTHiLATAE--RYCDRFIILDQGEIVAMG 215
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIH-QPRSDlfRLFDRILLLSSGEIVYSG 226
|
|
| CeuD |
COG4604 |
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ... |
3-235 |
1.17e-17 |
|
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 79.36 E-value: 1.17e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYIP 81
Cdd:COG4604 2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATtPSRELAKRLAILR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 EAPVIYDALTLKEHIEMTAMAYS------IDYDtAMARALPLLKtfrLEDQLHIFPSHFSKGMKQKV---MIICAfivEP 152
Cdd:COG4604 82 QENHINSRLTVRELVAFGRFPYSkgrltaEDRE-IIDEAIAYLD---LEDLADRYLDELSGGQRQRAfiaMVLAQ---DT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 153 DFYIIDEPFLGLDP---IGIQSMLDLMAskKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALrhqtaMPHA 229
Cdd:COG4604 155 DYVLLDEPLNNLDMkhsVQMMKLLRRLA--DELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI-----ITPE 227
|
....*.
gi 2095223075 230 TLDEIY 235
Cdd:COG4604 228 VLSDIY 233
|
|
| CydC |
TIGR02868 |
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ... |
2-191 |
1.54e-17 |
|
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: 81.25 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSlDQDEVRRRVSV 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAlTLKEHIEMTAMAYSidyDTAMARAlplLKTFRLEDQLHIFP-----------SHFSKGMKQKVMIICAF 148
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLARPDAT---DEELWAA---LERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARAL 486
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIGIQSMLDLMASkKEEGRTVLMSTH 191
Cdd:TIGR02868 487 LADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITH 528
|
|
| ABCC_TAP |
cd03248 |
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ... |
3-211 |
1.96e-17 |
|
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: 78.28 E-value: 1.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKP---IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAY-RQHLS 78
Cdd:cd03248 12 VKFQNVTFAYPTRPdtlVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYlHSKVS 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYdALTLKEHIEMTAMAYSIDYDTAMARALPlLKTFRLEDQLHIFP------SHFSKGMKQKVMIICAFIVEP 152
Cdd:cd03248 92 LVGQEPVLF-ARSLQDNIAYGLQSCSFECVKEAAQKAH-AHSFISELASGYDTevgekgSQLSGGQKQRVAIARALIRNP 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 153 DFYIIDEPFLGLDpIGIQSMLDLMASKKEEGRTVLMSTHILATAERyCDRFIILDQGEI 211
Cdd:cd03248 170 QVLILDEATSALD-AESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
|
|
| PRK11831 |
PRK11831 |
phospholipid ABC transporter ATP-binding protein MlaF; |
3-224 |
2.72e-17 |
|
phospholipid ABC transporter ATP-binding protein MlaF;
Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 78.65 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHLS 78
Cdd:PRK11831 8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDALTLKEHI-----EMTAMAYSIDYDTAMARalplLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPD 153
Cdd:PRK11831 88 MLFQSGALFTDMNVFDNVayplrEHTQLPAPLLHSTVMMK----LEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTH----ILATAERycdRFIILDQgEIVAMGNLEALRHQT 224
Cdd:PRK11831 164 LIMFDEPFVGQDPITMGVLVKLISElNSALGVTCVVVSHdvpeVLSIADH---AYIVADK-KIVAHGSAQALQANP 235
|
|
| thiQ |
PRK10771 |
thiamine ABC transporter ATP-binding protein ThiQ; |
22-231 |
3.02e-17 |
|
thiamine ABC transporter ATP-binding protein ThiQ;
Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 77.70 E-value: 3.02e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 22 NFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINikedihayrqHLSYIP-EAPV--------IYDALTL 92
Cdd:PRK10771 19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD----------HTTTPPsRRPVsmlfqennLFSHLTV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 KEHIEMtAMAYSIDYDTAMARAL-PLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQS 171
Cdd:PRK10771 89 AQNIGL-GLNPGLKLNAAQREKLhAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 172 MLDLMASK-KEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTAmPHATL 231
Cdd:PRK10771 168 MLTLVSQVcQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDELLSGKA-SASAL 227
|
|
| ABCC_NFT1 |
cd03369 |
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ... |
3-215 |
4.07e-17 |
|
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: 77.07 E-value: 4.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKK--PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:cd03369 7 IEVENLSVRYAPDlpPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTiPLEDLRSSLTI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAlTLKEHIEMTAMaYSidyDTAMARALPLLKTfrledqlhifPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:cd03369 87 IPQDPTLFSG-TIRSNLDPFDE-YS---DEEIYGALRVSEG----------GLNLSQGQRQLLCLARALLKRPRVLVLDE 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 160 PFLGLDpigIQSMLDLMASKKEE--GRTVLMSTHILATAERyCDRFIILDQGEIVAMG 215
Cdd:cd03369 152 ATASID---YATDALIQKTIREEftNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
|
|
| PRK11174 |
PRK11174 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
15-223 |
4.59e-17 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 79.89 E-value: 4.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 15 KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLtPTEGDMSISGINIKE-DIHAYRQHLSYIPEAPVIYDAlTLK 93
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLSWVGQNPQLPHG-TLR 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 94 EHIEMTAMAYSID-YDTAMARA--------LPLLKTFRLEDQlhifPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGL 164
Cdd:PRK11174 441 DNVLLGNPDASDEqLQQALENAwvseflplLPQGLDTPIGDQ----AAGLSVGQAQRLALARALLQPCQLLLLDEPTASL 516
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 165 DpigIQSMLDLMASKKE--EGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEALRHQ 223
Cdd:PRK11174 517 D---AHSEQLVMQALNAasRRQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAELSQA 573
|
|
| MglA |
COG1129 |
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism]; |
4-213 |
4.80e-17 |
|
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 79.68 E-value: 4.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGygkkPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYRQHLSYIP 81
Cdd:COG1129 258 EVEGLSVG----GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGkpVRIRSPRDAIRAGIAYVP 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 EapviyD--------ALTLKEHIEMTAMA-YS----IDYDTAMARALPLLKTFRL----EDQLhifPSHFSKGMKQKVMI 144
Cdd:COG1129 334 E-----DrkgeglvlDLSIRENITLASLDrLSrgglLDRRRERALAEEYIKRLRIktpsPEQP---VGNLSGGNQQKVVL 405
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 145 ICAFIVEPDFYIIDEPFLGLDpIG----IQSMLDLMAskkEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:COG1129 406 AKWLATDPKVLILDEPTRGID-VGakaeIYRLIRELA---AEGKAVIVISSELPELLGLSDRILVMREGRIVG 474
|
|
| oppD |
PRK09473 |
oligopeptide transporter ATP-binding component; Provisional |
18-229 |
4.85e-17 |
|
oligopeptide transporter ATP-binding component; Provisional
Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 78.61 E-value: 4.85e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTP---TEGDMSISGINI----KEDIHAYR-QHLSYIPEAPV---- 85
Cdd:PRK09473 32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREIlnlpEKELNKLRaEQISMIFQDPMtsln 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 86 ----IYDALT--LKEHIEM---TAMAYSIdydtamaRALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYI 156
Cdd:PRK09473 112 pymrVGEQLMevLMLHKGMskaEAFEESV-------RMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLLI 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 157 IDEPFLGLD-PIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTAMPHA 229
Cdd:PRK09473 185 ADEPTTALDvTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYS 258
|
|
| PRK03695 |
PRK03695 |
vitamin B12-transporter ATPase; Provisional |
21-215 |
8.37e-17 |
|
vitamin B12-transporter ATPase; Provisional
Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 76.90 E-value: 8.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 21 INFELTDGEIVGLIGLNGAGKSTTIKHILGLLtPTEGDMSISGINIKEDIHA----YR----QHLSYIPEAPVI-YDALT 91
Cdd:PRK03695 15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSAAelarHRaylsQQQTPPFAMPVFqYLTLH 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 92 LKEHIEMTAMAYSIDYdtaMARALpllktfRLEDQLHIFPSHFSKGMKQKVMIICAFI-VEPD------FYIIDEPFLGL 164
Cdd:PRK03695 94 QPDKTRTEAVASALNE---VAEAL------GLDDKLGRSVNQLSGGEWQRVRLAAVVLqVWPDinpagqLLLLDEPMNSL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 165 DpIGIQSMLDLMASK-KEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK03695 165 D-VAQQAALDRLLSElCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASG 215
|
|
| lolD |
PRK11629 |
lipoprotein-releasing ABC transporter ATP-binding protein LolD; |
17-198 |
1.14e-16 |
|
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 76.39 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKSTTIkHIL-GLLTPTEGDMSISGINIKEDIHAYR-----QHLSYIPEAPVIYDAL 90
Cdd:PRK11629 24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLL-HLLgGLDTPTSGDVIFNGQPMSKLSSAAKaelrnQKLGFIYQFHHLLPDF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 91 TLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQ 170
Cdd:PRK11629 103 TALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNAD 182
|
170 180
....*....|....*....|....*....
gi 2095223075 171 SMLDLMAS-KKEEGRTVLMSTHILATAER 198
Cdd:PRK11629 183 SIFQLLGElNRLQGTAFLVVTHDLQLAKR 211
|
|
| ABC2_perm_RbbA |
NF033858 |
ribosome-associated ATPase/putative transporter RbbA; |
3-237 |
1.16e-16 |
|
ribosome-associated ATPase/putative transporter RbbA;
Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.63 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTtikhILGLLTPTE-----------GDMSISginikedih 71
Cdd:NF033858 2 ARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSS----LLSLIAGARkiqqgrvevlgGDMADA--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 72 AYRQHLsyipeAPVI-----------YDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDqlhiFPS----HFSK 136
Cdd:NF033858 69 RHRRAV-----CPRIaympqglgknlYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAP----FADrpagKLSG 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 137 GMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEE--GRTVLMSTHILATAERYcDRFIILDQGEIVAM 214
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPTTGVDPLSRRQFWELIDRIRAErpGMSVLVATAYMEEAERF-DWLVAMDAGRVLAT 218
|
250 260
....*....|....*....|...
gi 2095223075 215 GNLEALRHQTAmpHATLDEIYIH 237
Cdd:NF033858 219 GTPAELLARTG--ADTLEAAFIA 239
|
|
| cbiO |
PRK13650 |
energy-coupling factor transporter ATPase; |
3-211 |
1.78e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 76.69 E-value: 1.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGK---KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKED-IHAYRQHLS 78
Cdd:PRK13650 5 IEVKNLTFKYKEdqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAP-VIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYII 157
Cdd:PRK13650 85 MVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 158 DEPFLGLDPIGIQSMLDLMASKKEE-GRTVLMSTHILATAErYCDRFIILDQGEI 211
Cdd:PRK13650 165 DEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
16-228 |
1.85e-16 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 77.97 E-value: 1.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 16 PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG----------INIKEDIHAYRQH-----LSYI 80
Cdd:PRK10261 30 AAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKmllrrrsrqvIELSEQSAAQMRHvrgadMAMI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPV--IYDALTLKEHI-EMTAMAYSIDYDTAMARALPLLKTFRLEDQLHI---FPSHFSKGMKQKVMIICAFIVEPDF 154
Cdd:PRK10261 110 FQEPMtsLNPVFTVGEQIaESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIlsrYPHQLSGGMRQRVMIAMALSCRPAV 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 155 YIIDEPFLGLDpIGIQS-MLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTAMPH 228
Cdd:PRK10261 190 LIADEPTTALD-VTIQAqILQLIKVlQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQHPY 264
|
|
| PRK14267 |
PRK14267 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-215 |
2.08e-16 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 76.03 E-value: 2.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLL-----TPTEGDMSISGINI-KEDIHA--YR 74
Cdd:PRK14267 5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIySPDVDPieVR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QHLSYIPEAPVIYDALTLKEHI----EMTAMAYSID-YDTAMARALPLLKTF-RLEDQLHIFPSHFSKGMKQKVMIICAF 148
Cdd:PRK14267 85 REVGMVFQYPNPFPHLTIYDNVaigvKLNGLVKSKKeLDERVEWALKKAALWdEVKDRLNDYPSNLSGGQRQRLVIARAL 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK14267 165 AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
|
|
| PRK10253 |
PRK10253 |
iron-enterobactin ABC transporter ATP-binding protein; |
6-215 |
2.36e-16 |
|
iron-enterobactin ABC transporter ATP-binding protein;
Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 76.18 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 6 KNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEdiHAYRQ---HLSYIPE 82
Cdd:PRK10253 11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQH--YASKEvarRIGLLAQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKE--------HIEMTAMAYSIDYDtAMARALPLLKTFRLEDQlhiFPSHFSKGMKQKVMIICAFIVEPDF 154
Cdd:PRK10253 89 NATTPGDITVQElvargrypHQPLFTRWRKEDEE-AVTKAMQATGITHLADQ---SVDTLSGGQRQRAWIAMVLAQETAI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 155 YIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK10253 165 MLLDEPTTWLDISHQIDLLELLSElNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
|
|
| PRK10851 |
PRK10851 |
sulfate/thiosulfate ABC transporter ATP-binding protein CysA; |
1-215 |
3.58e-16 |
|
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 76.66 E-value: 3.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEdIHAYRQHLSYI 80
Cdd:PRK10851 1 MSIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSR-LHARDRKVGFV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIE--MTAM-------AYSIDYdtamaRALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVE 151
Cdd:PRK10851 80 FQHYALFRHMTVFDNIAfgLTVLprrerpnAAAIKA-----KVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 152 PDFYIIDEPFLGLDpigiqsmldlmASKKEEGR------------TVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK10851 155 PQILLLDEPFGALD-----------AQVRKELRrwlrqlheelkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAG 219
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
15-220 |
3.95e-16 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 77.32 E-value: 3.95e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 15 KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEgdmsISGINIkedihayRQHLSYIPEAPVIYDAlTLKE 94
Cdd:PLN03232 630 KPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAE----TSSVVI-------RGSVAYVPQVSWIFNA-TVRE 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 95 HIemtamAYSIDYDTamARALPLLKTFRLEDQLHIFPSH-----------FSKGMKQKVMIICAFIVEPDFYIIDEPFLG 163
Cdd:PLN03232 698 NI-----LFGSDFES--ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 164 LDPIGIQSMLDLMASKKEEGRTVLMST---HILATAerycDRFIILDQGEIVAMGNLEAL 220
Cdd:PLN03232 771 LDAHVAHQVFDSCMKDELKGKTRVLVTnqlHFLPLM----DRIILVSEGMIKEEGTFAEL 826
|
|
| PRK10535 |
PRK10535 |
macrolide ABC transporter ATP-binding protein/permease MacB; |
17-213 |
4.41e-16 |
|
macrolide ABC transporter ATP-binding protein/permease MacB;
Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 77.07 E-value: 4.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKStTIKHILGLL-TPTEGDMSISGINIKE---DIHAY--RQHLSYIPEAPVIYDAL 90
Cdd:PRK10535 23 VLKGISLDIYAGEMVAIVGASGSGKS-TLMNILGCLdKPTSGTYRVAGQDVATldaDALAQlrREHFGFIFQRYHLLSHL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 91 TLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQ 170
Cdd:PRK10535 102 TAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGE 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095223075 171 SMLDLMASKKEEGRTVLMSTH---ILATAErycdRFIILDQGEIVA 213
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTHdpqVAAQAE----RVIEIRDGEIVR 223
|
|
| PRK14239 |
PRK14239 |
phosphate transporter ATP-binding protein; Provisional |
3-216 |
5.11e-16 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 74.81 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHI--LGLLTP---TEGDMSISGINI---KEDIHAYR 74
Cdd:PRK14239 6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIyspRTDTVDLR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QHLSYIPEAP----------VIY--------DALTLKEHIEMTAMAYSIdYDtamaralpllktfRLEDQLHIFPSHFSK 136
Cdd:PRK14239 86 KEIGMVFQQPnpfpmsiyenVVYglrlkgikDKQVLDEAVEKSLKGASI-WD-------------EVKDRLHDSALGLSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 137 GMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:PRK14239 152 GQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQQASRISDRTGFFLDGDLIEYND 230
|
|
| cbiO |
PRK13642 |
energy-coupling factor transporter ATPase; |
3-212 |
6.51e-16 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 75.13 E-value: 6.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNIN---FELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIK-EDIHAYRQHLS 78
Cdd:PRK13642 5 LEVENLVFKYEKESDVNQLNgvsFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTaENVWNLRRKIG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAP-VIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYII 157
Cdd:PRK13642 85 MVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIIL 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 158 DEPFLGLDPIGIQSMLDLMASKKEEGR-TVLMSTHILATAERyCDRFIILDQGEIV 212
Cdd:PRK13642 165 DESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEII 219
|
|
| 40850658_otr |
NF000106 |
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit; |
3-221 |
1.05e-15 |
|
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 75.16 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAG--KSTTIKHILGlltPTEGDMSISGINIKEDIHAYRQHLS-Y 79
Cdd:NF000106 14 VEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*G---PDAGRRPWRF*TWCANRRALRRTIG*H 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:NF000106 91 RPVR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDE 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 160 PFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALR 221
Cdd:NF000106 171 PTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELK 232
|
|
| PRK11000 |
PRK11000 |
maltose/maltodextrin ABC transporter ATP-binding protein MalK; |
3-222 |
1.76e-15 |
|
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 74.68 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKeDIHAYRQHLSYIPE 82
Cdd:PRK11000 4 VTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMN-DVPPAERGVGMVFQ 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEM---TAMAYSIDYDTAMARALPLLKTFRLEDQLhifPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:PRK11000 83 SYALYPHLSVAENMSFglkLAGAKKEEINQRVNQVAEVLQLAHLLDRK---PKALSGGQRQRVAIGRTLVAEPSVFLLDE 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 160 PFLGLDP-IGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:PRK11000 160 PLSNLDAaLRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYH 223
|
|
| cbiO |
PRK13645 |
energy-coupling factor transporter ATPase; |
5-216 |
2.35e-15 |
|
energy-coupling factor transporter ATPase;
Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 73.50 E-value: 2.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 5 IKNLTGGYGKKP-----IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTpTE------GDMSI-SGINIKEDIHA 72
Cdd:PRK13645 9 LDNVSYTYAKKTpfefkALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLII-SEtgqtivGDYAIpANLKKIKEVKR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 73 YRQHLSYI---PEAPVIYDalTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRL-EDQLHIFPSHFSKGMKQKVMIICAF 148
Cdd:PRK13645 88 LRKEIGLVfqfPEYQLFQE--TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGII 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:PRK13645 166 AMDGNTLVLDEPTGGLDPKGEEDFINLFERlNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGS 234
|
|
| cbiO |
PRK13648 |
cobalt transporter ATP-binding subunit; Provisional |
18-216 |
2.66e-15 |
|
cobalt transporter ATP-binding subunit; Provisional
Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 73.25 E-value: 2.66e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG-----DMSISGINIKEdihaYRQHLSYIPEAP-------- 84
Cdd:PRK13648 25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGeifynNQAITDDNFEK----LRKHIGIVFQNPdnqfvgsi 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 85 VIYD-ALTLKEHiemtamaySIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLG 163
Cdd:PRK13648 101 VKYDvAFGLENH--------AVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSM 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 164 LDPIGIQSMLDLMASKKEEGRTVLMS-THILATAERyCDRFIILDQGEIVAMGN 216
Cdd:PRK13648 173 LDPDARQNLLDLVRKVKSEHNITIISiTHDLSEAME-ADHVIVMNKGTVYKEGT 225
|
|
| PhnK |
COG1101 |
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ... |
3-212 |
3.49e-15 |
|
ABC-type uncharacterized transport system, ATPase component [General function prediction only];
Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 72.81 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLT-----GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI---KEDIHAyr 74
Cdd:COG1101 2 LELKNLSktfnpGTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtklPEYKRA-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 qhlSYIpeAPVIYD-------ALTLKEHIemtAMAYS-----------IDYDTAMARAlpLLKTFR--LEDQLHIFPSHF 134
Cdd:COG1101 80 ---KYI--GRVFQDpmmgtapSMTIEENL---ALAYRrgkrrglrrglTKKRRELFRE--LLATLGlgLENRLDTKVGLL 149
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 135 SKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASK-KEEGRTVLMSTHILATAERYCDRFIILDQGEIV 212
Cdd:COG1101 150 SGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIvEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
|
|
| potA |
PRK09452 |
spermidine/putrescine ABC transporter ATP-binding protein PotA; |
3-211 |
4.28e-15 |
|
spermidine/putrescine ABC transporter ATP-binding protein PotA;
Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 73.44 E-value: 4.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI------KEDIHAYRQH 76
Cdd:PRK09452 15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIthvpaeNRHVNTVFQS 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 LSYIPEAPViYD--ALTLK------EHIEmtamaysidydtamARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAF 148
Cdd:PRK09452 95 YALFPHMTV-FEnvAFGLRmqktpaAEIT--------------PRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAV 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 149 IVEPDFYIIDEPFLGLD-PIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:PRK09452 160 VNKPKVLLLDESLSALDyKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
|
|
| PRK15079 |
PRK15079 |
oligopeptide ABC transporter ATP-binding protein OppF; Provisional |
18-228 |
4.29e-15 |
|
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 73.20 E-value: 4.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHLSYIPEAPV-------- 85
Cdd:PRK15079 37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgmkDDEWRAVRSDIQMIFQDPLaslnprmt 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 86 IYD--ALTLKE-HIEMTAMAYSiDYDTAMaralpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:PRK15079 117 IGEiiAEPLRTyHPKLSRQEVK-DRVKAM-----MLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 163 GLDpIGIQS-MLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTAMPH 228
Cdd:PRK15079 191 ALD-VSIQAqVVNLLQQlQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPY 257
|
|
| tagH |
PRK13545 |
teichoic acids export protein ATP-binding subunit; Provisional |
18-217 |
4.35e-15 |
|
teichoic acids export protein ATP-binding subunit; Provisional
Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 74.16 E-value: 4.35e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikedihayrqHLSYIPEAPVIYDALTLKEHIE 97
Cdd:PRK13545 40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------------SAALIAISSGLNGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 98 MTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMA 177
Cdd:PRK13545 108 LKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMN 187
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2095223075 178 SKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNL 217
Cdd:PRK13545 188 EFKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDI 227
|
|
| met_CoM_red_A2 |
TIGR03269 |
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ... |
3-216 |
4.55e-15 |
|
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: 74.07 E-value: 4.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGL--LTPTEGDM----------------SISGI 64
Cdd:TIGR03269 1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgyverpSKVGE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 65 NI--------KEDI------HAYRQHLS-----YIPEAPVIYDALTLKEHIeMTAMaYSIDY--DTAMARALPLLKTFRL 123
Cdd:TIGR03269 81 PCpvcggtlePEEVdfwnlsDKLRRRIRkriaiMLQRTFALYGDDTVLDNV-LEAL-EEIGYegKEAVGRAVDLIEMVQL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 124 EDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLD-LMASKKEEGRTVLMSTHILATAERYCDR 202
Cdd:TIGR03269 159 SHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNaLEEAVKASGISMVLTSHWPEVIEDLSDK 238
|
250
....*....|....
gi 2095223075 203 FIILDQGEIVAMGN 216
Cdd:TIGR03269 239 AIWLENGEIKEEGT 252
|
|
| tauB |
PRK11248 |
taurine ABC transporter ATP-binding subunit; |
4-191 |
5.31e-15 |
|
taurine ABC transporter ATP-binding subunit;
Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 72.04 E-value: 5.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIkEDIHAYR----QHLSY 79
Cdd:PRK11248 3 QISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAERgvvfQNEGL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIydaltlkEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:PRK11248 82 LPWRNVQ-------DNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154
|
170 180 190
....*....|....*....|....*....|...
gi 2095223075 160 PFLGLDPIGIQSMLDLMASK-KEEGRTVLMSTH 191
Cdd:PRK11248 155 PFGALDAFTREQMQTLLLKLwQETGKQVLLITH 187
|
|
| PRK10575 |
PRK10575 |
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC; |
28-235 |
5.83e-15 |
|
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 72.13 E-value: 5.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 28 GEIVGLIGLNGAGKSTTIKhILGL-LTPTEGDMSISGINIKE-DIHAYRQHLSYIPEAPVIYDALTLKEHIEMT------ 99
Cdd:PRK10575 37 GKVTGLIGHNGSGKSTLLK-MLGRhQPPSEGEILLDAQPLESwSSKAFARKVAYLPQQLPAAEGMTVRELVAIGrypwhg 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 100 AMA-YSIDYDTAMARALPL--LKTF--RLEDQLhifpshfSKGMKQKVMIicAFIVEPDF--YIIDEPFLGLDpigIQSM 172
Cdd:PRK10575 116 ALGrFGAADREKVEEAISLvgLKPLahRLVDSL-------SGGERQRAWI--AMLVAQDSrcLLLDEPTSALD---IAHQ 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 173 LDLMA----SKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALrhqtaMPHATLDEIY 235
Cdd:PRK10575 184 VDVLAlvhrLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL-----MRGETLEQIY 245
|
|
| ABCC_MRP_domain1 |
cd03250 |
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ... |
3-210 |
8.59e-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: 70.58 E-value: 8.59e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLT-----GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikedihayrqHL 77
Cdd:cd03250 1 ISVEDASftwdsGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDAlTLKEHIemtAMAYSID---YDTAmaralplLKTFRLEDQLHIFPSH-----------FSKGMKQKVM 143
Cdd:cd03250 69 AYVSQEPWIQNG-TIRENI---LFGKPFDeerYEKV-------IKACALEPDLEILPDGdlteigekginLSGGQKQRIS 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 144 IICAFIVEPDFYIIDEPFLGLDP-----I---GIQSMLdlmaskkEEGRTVLMSTHILATAeRYCDRFIILDQGE 210
Cdd:cd03250 138 LARAVYSDADIYLLDDPLSAVDAhvgrhIfenCILGLL-------LNNKTRILVTHQLQLL-PHADQIVVLDNGR 204
|
|
| PRK10908 |
PRK10908 |
cell division ATP-binding protein FtsE; |
13-212 |
8.79e-15 |
|
cell division ATP-binding protein FtsE;
Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 71.06 E-value: 8.79e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 13 GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYRQHLSYIPEAPVIYD 88
Cdd:PRK10908 13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQDHHLLM 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 89 ALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG 168
Cdd:PRK10908 93 DRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDAL 172
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095223075 169 IQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIV 212
Cdd:PRK10908 173 SEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
|
|
| potG |
PRK11607 |
putrescine ABC transporter ATP-binding subunit PotG; |
3-239 |
8.80e-15 |
|
putrescine ABC transporter ATP-binding subunit PotG;
Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 72.56 E-value: 8.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIkEDIHAYRQHLSYIPE 82
Cdd:PRK11607 20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-SHVPPYQRPINMMFQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APVIYDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:PRK11607 99 SYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMG 178
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 163 GLDPIGIQSM-LDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEalrhqtamphatldEIYIHVT 239
Cdd:PRK11607 179 ALDKKLRDRMqLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPE--------------EIYEHPT 242
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
3-235 |
1.03e-14 |
|
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]
Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 72.94 E-value: 1.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKhILGLLTPT---EGDMSISGINIK---------EDI 70
Cdd:TIGR02633 2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMK-ILSGVYPHgtwDGEIYWSGSPLKasnirdterAGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 71 HAYRQHLSYIPEapviydaLTLKEHI----EMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFP-SHFSKGMKQKVMII 145
Cdd:TIGR02633 81 VIIHQELTLVPE-------LSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 146 CAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL----- 220
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMSTMseddi 233
|
250 260
....*....|....*....|....*
gi 2095223075 221 ------RHQTAM----PHATLDEIY 235
Cdd:TIGR02633 234 itmmvgREITSLyphePHEIGDVIL 258
|
|
| PRK09700 |
PRK09700 |
D-allose ABC transporter ATP-binding protein AlsA; |
4-233 |
1.26e-14 |
|
D-allose ABC transporter ATP-binding protein AlsA;
Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 72.51 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKpiIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYRQHLSYIP 81
Cdd:PRK09700 267 EVRNVTSRDRKK--VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGkdISPRSPLDAVKKGMAYIT 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 EAPV---IYDALTLKEHIEMTAMAYSIDYDTAM--------------ARALPLLKTFRLEDQLhifpSHFSKGMKQKVMI 144
Cdd:PRK09700 345 ESRRdngFFPNFSIAQNMAISRSLKDGGYKGAMglfhevdeqrtaenQRELLALKCHSVNQNI----TELSGGNQQKVLI 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 145 ICAFIVEPDFYIIDEPFLGLDpIGIQS-MLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA-MGNLEALRH 222
Cdd:PRK09700 421 SKWLCCCPEVIIFDEPTRGID-VGAKAeIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQiLTNRDDMSE 499
|
250
....*....|.
gi 2095223075 223 QTAMPHATLDE 233
Cdd:PRK09700 500 EEIMAWALPQE 510
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
17-215 |
1.51e-14 |
|
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: 72.67 E-value: 1.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSYIPEAPVIYDAlTLKEH 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIaKIGLHDLRFKITIIPQDPVLFSG-SLRMN 1379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 96 IEMTAmAYSiDYDTAMARALPLLKTF------RLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDpIGI 169
Cdd:TIGR00957 1380 LDPFS-QYS-DEEVWWALELAHLKTFvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEATAAVD-LET 1456
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2095223075 170 QSMLDLMASKKEEGRTVLMSTHILATAERYCdRFIILDQGEIVAMG 215
Cdd:TIGR00957 1457 DNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFG 1501
|
|
| znuC |
PRK09544 |
high-affinity zinc transporter ATPase; Reviewed |
3-193 |
1.72e-14 |
|
high-affinity zinc transporter ATPase; Reviewed
Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 70.53 E-value: 1.72e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGiniKEDIHAYRQHLSYIPE 82
Cdd:PRK09544 5 VSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG---KLRIGYVPQKLYLDTT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 APviydaLTLKEHIEMTAMAYSIDYdtamaraLPLLKTFRLEdQLHIFP-SHFSKGMKQKVMIICAFIVEPDFYIIDEPF 161
Cdd:PRK09544 82 LP-----LTVNRFLRLRPGTKKEDI-------LPALKRVQAG-HLIDAPmQKLSGGETQRVLLARALLNRPQLLVLDEPT 148
|
170 180 190
....*....|....*....|....*....|...
gi 2095223075 162 LGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHIL 193
Cdd:PRK09544 149 QGVDVNGQVALYDLIDQlRRELDCAVLMVSHDL 181
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
13-220 |
2.17e-14 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 72.05 E-value: 2.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 13 GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLtPTEGDMSISGinikEDIHAY--RQHLSYIPEAPVI---- 86
Cdd:PRK15134 297 DHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLI-NSQGEIWFDG----QPLHNLnrRQLLPVRHRIQVVfqdp 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 87 YDALTLKEHIE-MTAMAYSIDYDTAMA-----RALPLLKTFRLE-DQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:PRK15134 372 NSSLNPRLNVLqIIEEGLRVHQPTLSAaqreqQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDE 451
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 160 PFLGLDPIGIQSMLDLMASKKEEGR-TVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK15134 452 PTSSLDKTVQAQILALLKSLQQKHQlAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERV 513
|
|
| ABCC_CFTR2 |
cd03289 |
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ... |
1-225 |
2.70e-14 |
|
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: 70.27 E-value: 2.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVqiKNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTpTEGDMSISGINI-KEDIHAYRQHL 77
Cdd:cd03289 3 MTV--KDLTAKYteGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWnSVPLQKWRKAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDAlTLKEHI---------EMTAMAYSIDYDTAMARaLPLLKTFRLEDQLHIfpshFSKGMKQKVMIICAF 148
Cdd:cd03289 80 GVIPQKVFIFSG-TFRKNLdpygkwsdeEIWKVAEEVGLKSVIEQ-FPGQLDFVLVDGGCV----LSHGHKQLMCLARSV 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIGIQsMLDLMASKKEEGRTVLMSTHILaTAERYCDRFIILDQGEIVAMGNLEALRHQTA 225
Cdd:cd03289 154 LSKAKILLLDEPSAHLDPITYQ-VIRKTLKQAFADCTVILSEHRI-EAMLECQRFLVIEENKVRQYDSIQKLLNEKS 228
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
16-221 |
2.77e-14 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 71.87 E-value: 2.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 16 PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikedihayrqHLSYIPEAPVIYDAlTLKEH 95
Cdd:TIGR01271 440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQTSWIMPG-TIKDN 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 96 IemtamAYSIDYDTamARALPLLKTFRLEDQLHIFPSH-----------FSKGMKQKVMIICAFIVEPDFYIIDEPFLGL 164
Cdd:TIGR01271 507 I-----IFGLSYDE--YRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHL 579
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 165 DPIGIQSMLD-----LMASKkeegrtvlmsTHILATAE----RYCDRFIILDQGEIVAMGNLEALR 221
Cdd:TIGR01271 580 DVVTEKEIFEsclckLMSNK----------TRILVTSKlehlKKADKILLLHEGVCYFYGTFSELQ 635
|
|
| ABCC_CFTR1 |
cd03291 |
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ... |
16-223 |
3.43e-14 |
|
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: 70.27 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 16 PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikedihayrqHLSYIPEAPVIYDAlTLKEH 95
Cdd:cd03291 51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQFSWIMPG-TIKEN 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 96 IemtamAYSIDYDTamARALPLLKTFRLEDQLHIFPSH-----------FSKGMKQKVMIICAFIVEPDFYIIDEPFLGL 164
Cdd:cd03291 118 I-----IFGVSYDE--YRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFGYL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 165 DPIGIQSMLD-----LMASKkeegrtvlmsTHILATAE----RYCDRFIILDQGEIVAMGNLEALRHQ 223
Cdd:cd03291 191 DVFTEKEIFEscvckLMANK----------TRILVTSKmehlKKADKILILHEGSSYFYGTFSELQSL 248
|
|
| PRK15112 |
PRK15112 |
peptide ABC transporter ATP-binding protein SapF; |
18-216 |
4.84e-14 |
|
peptide ABC transporter ATP-binding protein SapF;
Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 69.43 E-value: 4.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYR-QHLSYIPEAPViyDALTLKEHI 96
Cdd:PRK15112 29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYSYRsQRIRMIFQDPS--TSLNPRQRI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 97 -EMTAMAYSIDYD-TAMARALPLLKTFR----LEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQ 170
Cdd:PRK15112 107 sQILDFPLRLNTDlEPEQREKQIIETLRqvglLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRS 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095223075 171 SMLDLMASKKEE-GRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:PRK15112 187 QLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGS 233
|
|
| ABC_FeS_Assembly |
cd03217 |
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ... |
4-222 |
4.88e-14 |
|
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.
Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 68.32 E-value: 4.88e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGL--LTPTEGDMSISGINIKE---DIHAyRQHLS 78
Cdd:cd03217 2 EIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHpkYEVTEGEILFKGEDITDlppEERA-RLGIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPEAPVIYDALTLKEHIEmtamaySIDYDtamaralpllktfrledqlhifpshFSKGMKQKVMIICAFIVEPDFYIID 158
Cdd:cd03217 81 LAFQYPPEIPGVKNADFLR------YVNEG-------------------------FSGGEKKRNEILQLLLLEPDLAILD 129
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 159 EPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTH---ILATAERycDRFIILDQGEIVAMGNLEALRH 222
Cdd:cd03217 130 EPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqrLLDYIKP--DRVHVLYDGRIVKSGDKELALE 194
|
|
| SufC |
COG0396 |
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ... |
4-218 |
7.95e-14 |
|
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 68.56 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGL--LTPTEGDMSISGINIKE-DIH--AYR---- 74
Cdd:COG0396 2 EIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILElSPDerARAgifl 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 --QHLSYIPEAPVIY---DALTLKEHIEMTAMAYSIDYDTAMARalpllktfrledqLHIFPSH--------FSKGMKQK 141
Cdd:COG0396 82 afQYPVEIPGVSVSNflrTALNARRGEELSAREFLKLLKEKMKE-------------LGLDEDFldryvnegFSGGEKKR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 142 VMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTH---ILataeRY--CDRFIILDQGEIVAMGN 216
Cdd:COG0396 149 NEILQMLLLEPKLAILDETDSGLDIDALRIVAEGVNKLRSPDRGILIITHyqrIL----DYikPDFVHVLVDGRIVKSGG 224
|
..
gi 2095223075 217 LE 218
Cdd:COG0396 225 KE 226
|
|
| PRK11160 |
PRK11160 |
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed |
3-220 |
1.05e-13 |
|
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 69.85 E-value: 1.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTtikhILGLLT----PTEGDMSISGINIKE-DIHAYRQ 75
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKST----LLQLLTrawdPQQGEILLNGQPIADySEAALRQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLSYIPEAPVIYDAlTLKEHIEMTAMAYSidyDTAMARAL------PLLKTFRLED--------QLhifpshfSKGMKQK 141
Cdd:PRK11160 415 AISVVSQRVHLFSA-TLRDNLLLAAPNAS---DEALIEVLqqvgleKLLEDDKGLNawlgeggrQL-------SGGEQRR 483
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 142 VMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAsKKEEGRTVLMSTHILATAERYcDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLA-EHAQNKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQEL 560
|
|
| fbpC |
PRK11432 |
ferric ABC transporter ATP-binding protein; |
3-225 |
1.33e-13 |
|
ferric ABC transporter ATP-binding protein;
Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 68.98 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE------DIHAYRQh 76
Cdd:PRK11432 7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHrsiqqrDICMVFQ- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 lSYipeapVIYDALTLKEHIEMTAMAYSIDYDTAMAR---ALPLLKTFRLEDQlhiFPSHFSKGMKQKVMIICAFIVEPD 153
Cdd:PRK11432 86 -SY-----ALFPHMSLGENVGYGLKMLGVPKEERKQRvkeALELVDLAGFEDR---YVDQISGGQQQRVALARALILKPK 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 154 FYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTA 225
Cdd:PRK11432 157 VLLFDEPLSNLDANLRRSMREKIRElQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229
|
|
| PRK10261 |
PRK10261 |
glutathione transporter ATP-binding protein; Provisional |
18-220 |
1.48e-13 |
|
glutathione transporter ATP-binding protein; Provisional
Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 69.50 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIK----EDIHAYRQHLSYIPEAPviYDALTLK 93
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDtlspGKLQALRRDIQFIFQDP--YASLDPR 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 94 EHIemtamAYSI----------DYDTAMARALPLLKTFRLEDQlHI--FPSHFSKGMKQKVMIICAFIVEPDFYIIDEPF 161
Cdd:PRK10261 418 QTV-----GDSImeplrvhgllPGKAAAARVAWLLERVGLLPE-HAwrYPHEFSGGQRQRICIARALALNPKVIIADEAV 491
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 162 LGLDpIGIQS-----MLDLmasKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK10261 492 SALD-VSIRGqiinlLLDL---QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAV 551
|
|
| PRK10584 |
PRK10584 |
putative ABC transporter ATP-binding protein YbbA; Provisional |
28-211 |
1.74e-13 |
|
putative ABC transporter ATP-binding protein YbbA; Provisional
Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 67.50 E-value: 1.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 28 GEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI----KEDIHAYR-QHLSYIPEAPVIYDALTLKEHIEMTAMA 102
Cdd:PRK10584 36 GETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLhqmdEEARAKLRaKHVGFVFQSFMLIPTLNALENVELPALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 103 YSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKE 181
Cdd:PRK10584 116 RGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSlNRE 195
|
170 180 190
....*....|....*....|....*....|
gi 2095223075 182 EGRTVLMSTHILATAERyCDRFIILDQGEI 211
Cdd:PRK10584 196 HGTTLILVTHDLQLAAR-CDRRLRLVNGQL 224
|
|
| ABCG_PDR_domain1 |
cd03233 |
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ... |
11-215 |
2.24e-13 |
|
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: 66.52 E-value: 2.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 11 GYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPT---EGDMSISGINIKEDIHAYRQHLSYIPEAPVIY 87
Cdd:cd03233 16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEKYPGEIIYVSEEDVHF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 88 DALTLKEHIEmtamaysidydtamaralpllktFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDP- 166
Cdd:cd03233 96 PTLTVRETLD-----------------------FALRCKGNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSs 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 167 --IGIQSMLDLMAskKEEGRTVLMSthILATAERYCDRF---IILDQGEIVAMG 215
Cdd:cd03233 153 taLEILKCIRTMA--DVLKTTTFVS--LYQASDEIYDLFdkvLVLYEGRQIYYG 202
|
|
| PRK14247 |
PRK14247 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-236 |
2.28e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 67.63 E-value: 2.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGL--LTP---TEGDMSISGINI-KEDIHAYRQH 76
Cdd:PRK14247 4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIfKMDVIELRRR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 LSYIPEAPVIYDALTLKEHIEMTAMAYSIDYDTA--MARALPLLKTFRL----EDQLHIFPSHFSKGMKQKVMIICAFIV 150
Cdd:PRK14247 84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKelQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 151 EPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYCDRFIILDQGEIVAMGnleALRHQTAMPHAT 230
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWG---PTREVFTNPRHE 239
|
....*.
gi 2095223075 231 LDEIYI 236
Cdd:PRK14247 240 LTEKYV 245
|
|
| PRK13657 |
PRK13657 |
glucan ABC transporter ATP-binding protein/ permease; |
2-220 |
2.43e-13 |
|
glucan ABC transporter ATP-binding protein/ permease;
Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 68.83 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIkhilGLL----TPTEGDMSISGINIKE-DIHAYRQ 75
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLI----NLLqrvfDPQSGRILIDGTDIRTvTRASLRR 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLsyipeAPVIYDAL----TLKEHI----------EMTAMAysidyDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQK 141
Cdd:PRK13657 410 NI-----AVVFQDAGlfnrSIEDNIrvgrpdatdeEMRAAA-----ERAQAHDFIERKPDGYDTVVGERGRQLSGGERQR 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 142 VMIICAFIVEPDFYIIDEPFLGLD---PIGIQSMLD-LMaskkeEGRTVLMSTHILATAeRYCDRFIILDQGEIVAMGNL 217
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDvetEAKVKAALDeLM-----KGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSF 553
|
...
gi 2095223075 218 EAL 220
Cdd:PRK13657 554 DEL 556
|
|
| ABC_RNaseL_inhibitor_domain2 |
cd03237 |
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
24-207 |
2.60e-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: 67.43 E-value: 2.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 24 ELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIkedihAYR-QHLSyiPEAPVIYDALTLKEHIEMTAMA 102
Cdd:cd03237 21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-----SYKpQYIK--ADYEGTVRDLLSSITKDFYTHP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 103 YsidYDTAMARALPLLKTfrLEDQLhifpSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDpigiqSMLDLMASK--- 179
Cdd:cd03237 94 Y---FKTEIAKPLQIEQI--LDREV----PELSGGELQRVAIAACLSKDADIYLLDEPSAYLD-----VEQRLMASKvir 159
|
170 180 190
....*....|....*....|....*....|.
gi 2095223075 180 ---KEEGRTVLMSTHILATAERYCDRFIILD 207
Cdd:cd03237 160 rfaENNEKTAFVVEHDIIMIDYLADRLIVFE 190
|
|
| PRK13546 |
PRK13546 |
teichoic acids export ABC transporter ATP-binding subunit TagH; |
18-228 |
3.24e-13 |
|
teichoic acids export ABC transporter ATP-binding subunit TagH;
Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 67.15 E-value: 3.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikedihayrqHLSYIPEAPVIYDALTLKEHIE 97
Cdd:PRK13546 40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG------------EVSVIAISAGLSGQLTGIENIE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 98 --MTAMAYSidyDTAMARALPLLKTF-RLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLD 174
Cdd:PRK13546 108 fkMLCMGFK---RKEIKAMTPKIIEFsELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLD 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 175 LMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEalrhqTAMPH 228
Cdd:PRK13546 185 KIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELD-----DVLPK 233
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
3-226 |
5.99e-13 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 67.77 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE--DIHAYRQHLSYI 80
Cdd:PRK15439 12 LCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARltPAKAHQLGIYLV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIeMTAMAYSIDydtAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:PRK15439 92 PQEPLLFPNLSVKENI-LFGLPKRQA---SMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRILILDEP 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQ---TAM 226
Cdd:PRK15439 168 TASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDdiiQAI 236
|
|
| PRK14258 |
PRK14258 |
phosphate ABC transporter ATP-binding protein; Provisional |
3-201 |
6.93e-13 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 66.21 E-value: 6.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHiLGLLTPTEGDMSISG------INIKE---DIHAY 73
Cdd:PRK14258 8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKC-LNRMNELESEVRVEGrveffnQNIYErrvNLNRL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 74 RQHLSYIPEAP-----VIYDALTLKehIEMTAMAYSIDYDTAMARALPLLKTF-RLEDQLHIFPSHFSKGMKQKVMIICA 147
Cdd:PRK14258 87 RRQVSMVHPKPnlfpmSVYDNVAYG--VKIVGWRPKLEIDDIVESALKDADLWdEIKHKIHKSALDLSGGQQQRLCIARA 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 148 FIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGR-TVLMSTHILATAERYCD 201
Cdd:PRK14258 165 LAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNLHQVSRLSD 219
|
|
| PRK11176 |
PRK11176 |
lipid A ABC transporter ATP-binding protein/permease MsbA; |
3-220 |
6.98e-13 |
|
lipid A ABC transporter ATP-binding protein/permease MsbA;
Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 67.35 E-value: 6.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGY-GK-KPIIKNINFELTDGEIVGLIGLNGAGKSTtikhILGLLTP----TEGDMSISGINIKE-DIHAYRQ 75
Cdd:PRK11176 342 IEFRNVTFTYpGKeVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRDyTLASLRN 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLSYIPE---------APVIYDALTLK---EHIEMTA-MAYSIDYDTAMARAlplLKTFRLEDQLHIfpshfSKGMKQKV 142
Cdd:PRK11176 418 QVALVSQnvhlfndtiANNIAYARTEQysrEQIEEAArMAYAMDFINKMDNG---LDTVIGENGVLL-----SGGQRQRI 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 143 MIICAFIVEPDFYIIDEPFLGLD---PIGIQSMLDLMasKKEegRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEA 219
Cdd:PRK11176 490 AIARALLRDSPILILDEATSALDtesERAIQAALDEL--QKN--RTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAE 564
|
.
gi 2095223075 220 L 220
Cdd:PRK11176 565 L 565
|
|
| PvdE |
COG4615 |
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ... |
21-221 |
8.71e-13 |
|
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: 67.13 E-value: 8.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 21 INFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSyipeapVIY------DALtlk 93
Cdd:COG4615 351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVtADNREAYRQLFS------AVFsdfhlfDRL--- 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 94 ehiemtamaYSIDYDTAMARALPLLKTFRLEDQLHIFPSHF-----SKGMKQKVMIICAFIVEPDFYIIDE--------- 159
Cdd:COG4615 422 ---------LGLDGEADPARARELLERLELDHKVSVEDGRFsttdlSQGQRKRLALLVALLEDRPILVFDEwaadqdpef 492
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 160 ---------PFLgldpigiqsmldlmaskKEEGRTVLMSTHilatAERY---CDRFIILDQGEIVAMGNLEALR 221
Cdd:COG4615 493 rrvfytellPEL-----------------KARGKTVIAISH----DDRYfdlADRVLKMDYGKLVELTGPAALA 545
|
|
| PstB |
COG1117 |
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ... |
3-216 |
1.82e-12 |
|
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism];
Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 65.06 E-value: 1.82e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGL--LTP---TEGDMSISGINI---KEDIHAYR 74
Cdd:COG1117 12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIydpDVDVVELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QHLSYIPEAPV-----IYD--ALTLKEHiEMTAMAysiDYDTAMARALpllktfR-------LEDQLHIFPSHFSKGMKQ 140
Cdd:COG1117 92 RRVGMVFQKPNpfpksIYDnvAYGLRLH-GIKSKS---ELDEIVEESL------RkaalwdeVKDRLKKSALGLSGGQQQ 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 141 KVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:COG1117 162 RLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGP 236
|
|
| PRK10522 |
PRK10522 |
multidrug transporter membrane component/ATP-binding component; Provisional |
2-211 |
2.71e-12 |
|
multidrug transporter membrane component/ATP-binding component; Provisional
Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 65.76 E-value: 2.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGYGKKPI-IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSY 79
Cdd:PRK10522 322 TLELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVtAEQPEDYRKLFSA 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDALTLKEHIEmtamAYSIDYDTAMARaLPLLKTFRLEDQlHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDE 159
Cdd:PRK10522 402 VFTDFHLFDQLLGPEGKP----ANPALVEKWLER-LKMAHKLELEDG-RISNLKLSKGQKKRLALLLALAEERDILLLDE 475
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 160 PFLGLDP----IGIQSMLDLMaskKEEGRTVLMSTH-----ILAtaerycDRFIILDQGEI 211
Cdd:PRK10522 476 WAADQDPhfrrEFYQVLLPLL---QEMGKTIFAISHddhyfIHA------DRLLEMRNGQL 527
|
|
| YejF |
COG4172 |
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ... |
19-220 |
3.27e-12 |
|
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: 65.48 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 19 KNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLtPTEGDMSISGINI----KEDIHAYRQHLSYIPEAPviYDAL---- 90
Cdd:COG4172 303 DGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLdglsRRALRPLRRRMQVVFQDP--FGSLsprm 379
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 91 TLKEHIE--MTAMAYSIDYDTAMARALPLLKTFRL-EDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDpI 167
Cdd:COG4172 380 TVGQIIAegLRVHGPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALD-V 458
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 168 GIQS-MLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:COG4172 459 SVQAqILDLLRDlQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQV 513
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
3-61 |
3.90e-12 |
|
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: 65.34 E-value: 3.90e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSI 61
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI 381
|
|
| dppD |
PRK11022 |
dipeptide transporter ATP-binding subunit; Provisional |
18-215 |
4.11e-12 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 64.76 E-value: 4.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLT-P---TEGDMSISGINIKEDIHAYRQHLSYIPEAPVIYDAltlk 93
Cdd:PRK11022 23 VDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIDyPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQDP---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 94 ehieMTAM--AYSIDYD--------------TAMARALPLLKTFRLED---QLHIFPSHFSKGMKQKVMIICAFIVEPDF 154
Cdd:PRK11022 99 ----MTSLnpCYTVGFQimeaikvhqggnkkTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKL 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 155 YIIDEPFLGLD-PIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK11022 175 LIADEPTTALDvTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETG 236
|
|
| phnK |
PRK11701 |
phosphonate C-P lyase system protein PhnK; Provisional |
4-215 |
4.25e-12 |
|
phosphonate C-P lyase system protein PhnK; Provisional
Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 63.79 E-value: 4.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGD------------------------- 58
Cdd:PRK11701 8 SVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEvhyrmrdgqlrdlyalseaerrrll 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 59 ----------------MSIS-GINIKEDIHAYRQ-HLSYIPEApviydALTLKEHIEmtamaysIDYDtamaralpllkt 120
Cdd:PRK11701 88 rtewgfvhqhprdglrMQVSaGGNIGERLMAVGArHYGDIRAT-----AGDWLERVE-------IDAA------------ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 121 fRLEDQlhifPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDpIGIQS-MLDLMAS-KKEEGRTVLMSTHILATAER 198
Cdd:PRK11701 144 -RIDDL----PTTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLD-VSVQArLLDLLRGlVRELGLAVVIVTHDLAVARL 217
|
250
....*....|....*..
gi 2095223075 199 YCDRFIILDQGEIVAMG 215
Cdd:PRK11701 218 LAHRLLVMKQGRVVESG 234
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
4-211 |
5.75e-12 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 64.64 E-value: 5.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGgygkkPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYRQHLSYIP 81
Cdd:PRK10762 259 KVDNLSG-----PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGheVVTRSPQDGLANGIVYIS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 EAPViYDALTL----KEHIEMTAMAY------SIDYDTAMARALPLLKTFRLEDqlhifPSH------FSKGMKQKVMII 145
Cdd:PRK10762 334 EDRK-RDGLVLgmsvKENMSLTALRYfsraggSLKHADEQQAVSDFIRLFNIKT-----PSMeqaiglLSGGNQQKVAIA 407
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 146 CAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGrtvlMSThILATAER-----YCDRFIILDQGEI 211
Cdd:PRK10762 408 RGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEG----LSI-ILVSSEMpevlgMSDRILVMHEGRI 473
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
20-213 |
6.36e-12 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 64.55 E-value: 6.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG-----INIKEDIHA-----YrQHLSYIPEapviyda 89
Cdd:PRK11288 22 DISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGqemrfASTTAALAAgvaiiY-QELHLVPE------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 90 LTLKEHI---EMTAMAYSIDYDTAMARALPLLKtfRLedQLHIFPS----HFSKGMKQKVMIICAfiVEPDFYII--DEP 160
Cdd:PRK11288 94 MTVAENLylgQLPHKGGIVNRRLLNYEAREQLE--HL--GVDIDPDtplkYLSIGQRQMVEIAKA--LARNARVIafDEP 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 161 FLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
|
|
| PRK15134 |
PRK15134 |
microcin C ABC transporter ATP-binding protein YejF; Provisional |
4-228 |
7.76e-12 |
|
microcin C ABC transporter ATP-binding protein YejF; Provisional
Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 64.34 E-value: 7.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGK----KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLL-TP----TEGDMSISGINIkedIHAYR 74
Cdd:PRK15134 7 AIENLSVAFRQqqtvRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPpvvyPSGDIRFHGESL---LHASE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QHLSYI---------PEAPVIYDAL-TL-KEHIEMTAMAYSIDYDTAMARALPLLKTF-------RLEDqlhiFPSHFSK 136
Cdd:PRK15134 84 QTLRGVrgnkiamifQEPMVSLNPLhTLeKQLYEVLSLHRGMRREAARGEILNCLDRVgirqaakRLTD----YPHQLSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 137 GMKQKVMIICAFIVEPDFYIIDEPFLGLDpIGIQS-MLDLMASKKEE-GRTVLMSTHILATAERYCDRFIILDQGEIVAM 214
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALD-VSVQAqILQLLRELQQElNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQ 238
|
250
....*....|....
gi 2095223075 215 GNLEALRHQTAMPH 228
Cdd:PRK15134 239 NRAATLFSAPTHPY 252
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
3-222 |
9.06e-12 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 64.37 E-value: 9.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNltgGY------GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPtegdMSISGINIkedihayRQH 76
Cdd:PLN03130 615 ISIKN---GYfswdskAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPP----RSDASVVI-------RGT 680
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 LSYIPEAPVIYDAlTLKEHI----EMTAMAY--SIDYdTAMARALPLLKTfrlEDQLHIFPS--HFSKGMKQKVMIICAF 148
Cdd:PLN03130 681 VAYVPQVSWIFNA-TVRDNIlfgsPFDPERYerAIDV-TALQHDLDLLPG---GDLTEIGERgvNISGGQKQRVSMARAV 755
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMST---HILAtaerYCDRFIILDQGEIVAMGNLEALRH 222
Cdd:PLN03130 756 YSNSDVYIFDDPLSALDAHVGRQVFDKCIKDELRGKTRVLVTnqlHFLS----QVDRIILVHEGMIKEEGTYEELSN 828
|
|
| PRK15439 |
PRK15439 |
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional |
4-211 |
2.85e-11 |
|
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 62.76 E-value: 2.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTG-GYgkkpiiKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYR--QHLSYI 80
Cdd:PRK15439 270 TVEDLTGeGF------RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlaRGLVYL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PE----------APVIYDALTLKEHiemtAMAYSIdyDTAMARAlpLLKTFRleDQLHIFPSH-------FSKGMKQKVM 143
Cdd:PRK15439 344 PEdrqssglyldAPLAWNVCALTHN----RRGFWI--KPARENA--VLERYR--RALNIKFNHaeqaartLSGGNQQKVL 413
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 144 IICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:PRK15439 414 IAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
3-61 |
3.05e-11 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 62.44 E-value: 3.05e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSI 61
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
|
|
| CFTR_protein |
TIGR01271 |
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ... |
1-226 |
3.25e-11 |
|
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]
Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 63.01 E-value: 3.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQikNLTGGY--GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTpTEGDMSISGINIKE-DIHAYRQHL 77
Cdd:TIGR01271 1218 MDVQ--GLTAKYteAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAF 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVIYDAlTLKEHI---------EMTAMAYSIDYDTaMARALPLLKTFRLEDQLHIfpshFSKGMKQKVMIICAF 148
Cdd:TIGR01271 1295 GVIPQKVFIFSG-TFRKNLdpyeqwsdeEIWKVAEEVGLKS-VIEQFPDKLDFVLVDGGYV----LSNGHKQLMCLARSI 1368
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIGIQsMLDLMASKKEEGRTVLMSTH-ILATAEryCDRFIILDQGEIVAMGNLEALRHQTAM 226
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQ-IIRKTLKQSFSNCTVILSEHrVEALLE--CQQFLVIEGSSVKQYDSIQKLLNETSL 1444
|
|
| PRK14243 |
PRK14243 |
phosphate transporter ATP-binding protein; Provisional |
3-201 |
4.46e-11 |
|
phosphate transporter ATP-binding protein; Provisional
Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 61.34 E-value: 4.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIK--HILGLLTPT---EGDMSISGINIKE---DIHAYR 74
Cdd:PRK14243 11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfNRLNDLIPGfrvEGKVTFHGKNLYApdvDPVEVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 QHLSYIPEAP-----VIYDALTLKEHIEmtamAYSIDYDTAMARALPLLKTF-RLEDQLHIFPSHFSKGMKQKVMIICAF 148
Cdd:PRK14243 91 RRIGMVFQKPnpfpkSIYDNIAYGARIN----GYKGDMDELVERSLRQAALWdEVKDKLKQSGLSLSGGQQQRLCIARAI 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 149 IVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYCD 201
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAARVSD 218
|
|
| 3a01204 |
TIGR00955 |
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ... |
13-215 |
5.18e-11 |
|
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 61.99 E-value: 5.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 13 GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTP---TEGDMSISGINIKED----IHAY-RQHLSYIPeap 84
Cdd:TIGR00955 36 PRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPIDAKemraISAYvQQDDLFIP--- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 85 viydALTLKEHIEMTA---MAYSIDYDTAMARALPLLKTFRLEDQLHI------FPSHFSKGMKQKVMIICAFIVEPDFY 155
Cdd:TIGR00955 113 ----TLTVREHLMFQAhlrMPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLL 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 156 IIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHiLATAERYC--DRFIILDQGEIVAMG 215
Cdd:TIGR00955 189 FCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIH-QPSSELFElfDKIILMAEGRVAYLG 249
|
|
| YnjD |
COG4136 |
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ... |
4-219 |
5.65e-11 |
|
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function prediction only];
Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 60.19 E-value: 5.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTP---TEGDMSISGINIkEDIHAYRQHLSYI 80
Cdd:COG4136 3 SLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-TALPAEQRRIGIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMtAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:COG4136 82 FQDDLLFPHLSVGENLAF-ALPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEP 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 161 FLGLDPIGIQSMLDLMASK-KEEGRTVLMSTHilataerycDRFIILDQGEIVAMGNLEA 219
Cdd:COG4136 161 FSKLDAALRAQFREFVFEQiRQRGIPALLVTH---------DEEDAPAAGRVLDLGNWQH 211
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
4-213 |
6.44e-11 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 61.48 E-value: 6.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKhILGLLTPT---EGDMSISG-----INIKED------ 69
Cdd:PRK13549 7 EMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMK-VLSGVYPHgtyEGEIIFEGeelqaSNIRDTeragia 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 70 -IHayrQHLSYIPEapviydaLTLKEHI----EMTAMAYsIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMI 144
Cdd:PRK13549 86 iIH---QELALVKE-------LSVLENIflgnEITPGGI-MDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEI 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 145 ICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:PRK13549 155 AKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGRHIG 223
|
|
| PRK10789 |
PRK10789 |
SmdA family multidrug ABC transporter permease/ATP-binding protein; |
1-224 |
7.95e-11 |
|
SmdA family multidrug ABC transporter permease/ATP-binding protein;
Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 61.27 E-value: 7.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:PRK10789 314 LDVNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAV 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYD-------AL----TLKEHIEMTAMAYSID---------YDTAMA-RALPLlktfrledqlhifpshfSKGM 138
Cdd:PRK10789 394 VSQTPFLFSdtvanniALgrpdATQQEIEHVARLASVHddilrlpqgYDTEVGeRGVML-----------------SGGQ 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 139 KQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMaSKKEEGRTVLMSTHILaTAERYCDRFIILDQGEIVAMGNLE 218
Cdd:PRK10789 457 KQRISIARALLLNAEILILDDALSAVDGRTEHQILHNL-RQWGEGRTVIISAHRL-SALTEASEILVMQHGHIAQRGNHD 534
|
....*.
gi 2095223075 219 ALRHQT 224
Cdd:PRK10789 535 QLAQQS 540
|
|
| SapD |
COG4170 |
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms]; |
5-227 |
8.00e-11 |
|
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 61.07 E-value: 8.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 5 IKNLT----GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTP----TEGDMSISGIN-----IKEDIH 71
Cdd:COG4170 6 IRNLTieidTPQGRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKDnwhvTADRFRWNGIDllklsPRERRK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 72 AYRQHLSYIPEAPVIY-D-ALTLKEHIEMtamaySIDYDT-----------AMARALPLLKTFRLEDQLHI---FPSHFS 135
Cdd:COG4170 86 IIGREIAMIFQEPSSClDpSAKIGDQLIE-----AIPSWTfkgkwwqrfkwRKKRAIELLHRVGIKDHKDImnsYPHELT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 136 KGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAM 214
Cdd:COG4170 161 EGECQKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARlNQLQGTSILLISHDLESISQWADTITVLYCGQTVES 240
|
250
....*....|...
gi 2095223075 215 GNLEALRHQTAMP 227
Cdd:COG4170 241 GPTEQILKSPHHP 253
|
|
| livG |
PRK11300 |
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional |
4-233 |
8.01e-11 |
|
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 60.39 E-value: 8.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIkEDIHAYR--------- 74
Cdd:PRK11300 7 SVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHI-EGLPGHQiarmgvvrt 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 -QHLSYIPEAPVIyDALTLKEHIEMTA---------MAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMI 144
Cdd:PRK11300 86 fQHVRLFREMTVI-ENLLVAQHQQLKTglfsgllktPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 145 ICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQ 223
Cdd:PRK11300 165 ARCMVTQPEILMLDEPAAGLNPKETKELDELIAElRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNN 244
|
250
....*....|
gi 2095223075 224 TAMPHATLDE 233
Cdd:PRK11300 245 PDVIKAYLGE 254
|
|
| NupO |
COG3845 |
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ... |
4-213 |
1.25e-10 |
|
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and metabolism];
Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 60.81 E-value: 1.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLT-GGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQH-LSYI 80
Cdd:COG3845 259 EVENLSvRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDItGLSPRERRRLgVAYI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PE-------APviydALTLKEHIEMTA---MAYS----IDYDTAMARALPLLKTF--RLEDqLHIFPSHFSKGMKQKVMI 144
Cdd:COG3845 339 PEdrlgrglVP----DMSVAENLILGRyrrPPFSrggfLDRKAIRAFAEELIEEFdvRTPG-PDTPARSLSGGNQQKVIL 413
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 145 ICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLmsthiLATAE-----RYCDRFIILDQGEIVA 213
Cdd:COG3845 414 ARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVL-----LISEDldeilALSDRIAVMYEGRIVG 482
|
|
| PRK10247 |
PRK10247 |
putative ABC transporter ATP-binding protein YbbL; Provisional |
13-225 |
2.63e-10 |
|
putative ABC transporter ATP-binding protein YbbL; Provisional
Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 58.57 E-value: 2.63e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 13 GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSYIPEAPV-----I 86
Cdd:PRK10247 18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlKPEIYRQQVSYCAQTPTlfgdtV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 87 YDALTL-----KEHIEMTAMAYSIDYdtamaRALPllktfrlEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPF 161
Cdd:PRK10247 98 YDNLIFpwqirNQQPDPAIFLDDLER-----FALP-------DTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 162 LGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHilATAE-RYCDRFIILDQgeivAMGNLEALRHQTA 225
Cdd:PRK10247 166 SALDESNKHNVNEIIHRyVREQNIAVLWVTH--DKDEiNHADKVITLQP----HAGEMQEARYELA 225
|
|
| MRP_assoc_pro |
TIGR00957 |
multi drug resistance-associated protein (MRP); This model describes multi drug ... |
1-220 |
2.92e-10 |
|
multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]
Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 59.96 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikedihayrqHLSYI 80
Cdd:TIGR00957 637 ITVHNATFTWARDLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYV 704
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDAlTLKEHIeMTAMAYSIDYDTAMARALPLLKtfrledQLHIFPS-----------HFSKGMKQKVMIICAFI 149
Cdd:TIGR00957 705 PQQAWIQND-SLRENI-LFGKALNEKYYQQVLEACALLP------DLEILPSgdrteigekgvNLSGGQKQRVSLARAVY 776
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 150 VEPDFYIIDEPFLGLDP----------IGIQSMLdlmaskkeEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEA 219
Cdd:TIGR00957 777 SNADIYLFDDPLSAVDAhvgkhifehvIGPEGVL--------KNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQE 847
|
.
gi 2095223075 220 L 220
Cdd:TIGR00957 848 L 848
|
|
| modC |
PRK11144 |
molybdenum ABC transporter ATP-binding protein ModC; |
20-226 |
5.00e-10 |
|
molybdenum ABC transporter ATP-binding protein ModC;
Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 58.73 E-value: 5.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG---INIKEDIH--AYRQHLSYipeapVIYDAlTLKE 94
Cdd:PRK11144 16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGIClpPEKRRIGY-----VFQDA-RLFP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 95 HiemtamaYSID----YdtAMARALP-----LLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLD 165
Cdd:PRK11144 90 H-------YKVRgnlrY--GMAKSMVaqfdkIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2095223075 166 pigiqsmldlMASKKE----------EGRT-VLMSTHILATAERYCDRFIILDQGEIVAMGNLEALRHQTAM 226
Cdd:PRK11144 161 ----------LPRKREllpylerlarEINIpILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAM 222
|
|
| PRK14246 |
PRK14246 |
phosphate ABC transporter ATP-binding protein; Provisional |
15-216 |
1.21e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 56.98 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 15 KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIH-----AYRQHLSYIPEAPVIY 87
Cdd:PRK14246 23 KAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvLYFGKDIFqidaiKLRKEVGMVFQQPNPF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 88 DALTLKEHIEMTAMAYSI----DYDTAMARALPLLKTFR-LEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:PRK14246 103 PHLSIYDNIAYPLKSHGIkekrEIKKIVEECLRKVGLWKeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTS 182
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 163 GLDPIGIQSMLDLMASKKEEGRTVLMStHILATAERYCDRFIILDQGEIVAMGN 216
Cdd:PRK14246 183 MIDIVNSQAIEKLITELKNEIAIVIVS-HNPQQVARVADYVAFLYNGELVEWGS 235
|
|
| PRK14271 |
PRK14271 |
phosphate ABC transporter ATP-binding protein; Provisional |
7-220 |
1.30e-09 |
|
phosphate ABC transporter ATP-binding protein; Provisional
Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 57.03 E-value: 1.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 7 NLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG-----DMSISGINI--KEDIHAYRQHLSY 79
Cdd:PRK14271 26 NLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIfnYRDVLEFRRRVGM 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYdALTLKEHIEMTAMAYSID-----YDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDF 154
Cdd:PRK14271 106 LFQRPNPF-PMSIMDNVLAGVRAHKLVprkefRGVAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEV 184
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 155 YIIDEPFLGLDPIGIQSMLDLMASKKEEgRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK14271 185 LLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQL 249
|
|
| PLN03232 |
PLN03232 |
ABC transporter C family member; Provisional |
13-230 |
1.42e-09 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 58.06 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 13 GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSYIPEAPVIYDAlT 91
Cdd:PLN03232 1247 GLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVaKFGLTDLRRVLSIIPQSPVLFSG-T 1325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 92 LKEHIEMTAMAYSIDYDTAMARAlpLLK------TFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLD 165
Cdd:PLN03232 1326 VRFNIDPFSEHNDADLWEALERA--HIKdvidrnPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVD 1403
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 166 pIGIQSMLDLMASKKEEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEAL--RHQTA---MPHAT 230
Cdd:PLN03232 1404 -VRTDSLIQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELlsRDTSAffrMVHST 1471
|
|
| PRK10790 |
PRK10790 |
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein; |
2-220 |
1.84e-09 |
|
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 57.42 E-value: 1.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGYGK-KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIH-AYRQHLSY 79
Cdd:PRK10790 340 RIDIDNVSFAYRDdNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHsVLRQGVAM 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVI-----YDALTLKEHI---------EMTAMAysidydtAMARALPLLKTFRLEDQlhifPSHFSKGMKQKVMII 145
Cdd:PRK10790 420 VQQDPVVladtfLANVTLGRDIseeqvwqalETVQLA-------ELARSLPDGLYTPLGEQ----GNNLSVGQKQLLALA 488
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 146 CAFIVEPDFYIIDEPFLGLDP---IGIQSMLDLMaskkEEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSgteQAIQQALAAV----REHTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGTHQQL 561
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
24-210 |
2.36e-09 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 57.13 E-value: 2.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 24 ELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISginIKedihayrqhLSYIPEapviYdaltLKEHIEMTAMAY 103
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE---LK---------ISYKPQ----Y----IKPDYDGTVEDL 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 104 --SI--DYDTAMARALpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPflgldpigiQSMLD----L 175
Cdd:PRK13409 421 lrSItdDLGSSYYKSE-IIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP---------SAHLDveqrL 490
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2095223075 176 MASK------KEEGRTVLMSTHILATAERYCDRFIILDqGE 210
Cdd:PRK13409 491 AVAKairriaEEREATALVVDHDIYMIDYISDRLMVFE-GE 530
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
3-57 |
2.46e-09 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 56.82 E-value: 2.46e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG 57
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSG 374
|
|
| araG |
PRK11288 |
L-arabinose ABC transporter ATP-binding protein AraG; |
4-231 |
3.21e-09 |
|
L-arabinose ABC transporter ATP-binding protein AraG;
Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.46 E-value: 3.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIikniNFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYRQHLSYIP 81
Cdd:PRK11288 259 RLDGLKGPGLREPI----SFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRDAIRAGIMLCP 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 E---APVIYDALTLKEHIEMTAMAYSI----------DYDTAMARALPL-LKTfRLEDQLHIFpshFSKGMKQKVmIICA 147
Cdd:PRK11288 335 EdrkAEGIIPVHSVADNINISARRHHLragclinnrwEAENADRFIRSLnIKT-PSREQLIMN---LSGGNQQKA-ILGR 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 148 FIVEP-DFYIIDEPFLGLDpIGIQS-MLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAmgnleALRHQTA 225
Cdd:PRK11288 410 WLSEDmKVILLDEPTRGID-VGAKHeIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIAG-----ELAREQA 483
|
....*.
gi 2095223075 226 MPHATL 231
Cdd:PRK11288 484 TERQAL 489
|
|
| PRK10636 |
PRK10636 |
putative ABC transporter ATP-binding protein; Provisional |
3-165 |
4.44e-09 |
|
putative ABC transporter ATP-binding protein; Provisional
Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 56.33 E-value: 4.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSIS-GINIKedihAYRQH-LSYI 80
Cdd:PRK10636 313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGLAkGIKLG----YFAQHqLEFL 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 --PEAPViydaltlkEHiemtamaysidydtaMARALPLLKTFRLEDQLHIF----------PSHFSKGmkQKVMIICAF 148
Cdd:PRK10636 389 raDESPL--------QH---------------LARLAPQELEQKLRDYLGGFgfqgdkvteeTRRFSGG--EKARLVLAL 443
|
170
....*....|....*....
gi 2095223075 149 IV--EPDFYIIDEPFLGLD 165
Cdd:PRK10636 444 IVwqRPNLLLLDEPTNHLD 462
|
|
| PRK15093 |
PRK15093 |
peptide ABC transporter ATP-binding protein SapD; |
5-228 |
4.46e-09 |
|
peptide ABC transporter ATP-binding protein SapD;
Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 55.96 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 5 IKNLTGGY----GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLltpTEGDMSISGINIK-EDIHAYR----- 74
Cdd:PRK15093 6 IRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV---TKDNWRVTADRMRfDDIDLLRlspre 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 75 ------QHLSYIPEAPviYDALTLKEHIEmTAMAYSIDYDTAMA-----------RALPLLKTFRLEDQ---LHIFPSHF 134
Cdd:PRK15093 83 rrklvgHNVSMIFQEP--QSCLDPSERVG-RQLMQNIPGWTYKGrwwqrfgwrkrRAIELLHRVGIKDHkdaMRSFPYEL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 135 SKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMAS-KKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:PRK15093 160 TEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRlNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVE 239
|
250
....*....|....*
gi 2095223075 214 MGNLEALrhqTAMPH 228
Cdd:PRK15093 240 TAPSKEL---VTTPH 251
|
|
| ATM1 |
COG5265 |
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ... |
2-220 |
4.89e-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: 55.98 E-value: 4.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKE-DIHAYRQHLSY 79
Cdd:COG5265 357 EVRFENVSFGYdPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvTQASLRAAIGI 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPV-----IY--------DAltLKEHIEMTAMAYSID---------YDTAMA-RALPLlktfrledqlhifpshfSK 136
Cdd:COG5265 437 VPQDTVlfndtIAyniaygrpDA--SEEEVEAAARAAQIHdfieslpdgYDTRVGeRGLKL-----------------SG 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 137 GMKQKVMIICAFIVEPDFYIIDEPFLGLDPI---GIQSMLDLMAskkeEGRTVLMSTHILATAeRYCDRFIILDQGEIVA 213
Cdd:COG5265 498 GEKQRVAIARTLLKNPPILIFDEATSALDSRterAIQAALREVA----RGRTTLVIAHRLSTI-VDADEILVLEAGRIVE 572
|
....*..
gi 2095223075 214 MGNLEAL 220
Cdd:COG5265 573 RGTHAEL 579
|
|
| dppF |
PRK11308 |
dipeptide transporter ATP-binding subunit; Provisional |
21-222 |
6.89e-09 |
|
dipeptide transporter ATP-binding subunit; Provisional
Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 55.36 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 21 INFELTDGEIVGLIGLNGAGKSTtikhiLG-LLT----PTEGDMSISGINI----KEDIHAYRQHLSYIPEAPviYDALT 91
Cdd:PRK11308 34 VSFTLERGKTLAVVGESGCGKST-----LArLLTmietPTGGELYYQGQDLlkadPEAQKLLRQKIQIVFQNP--YGSLN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 92 LKEHIEMTaMAYSIDYDTAM------ARALPLLKTFRLE-DQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGL 164
Cdd:PRK11308 107 PRKKVGQI-LEEPLLINTSLsaaerrEKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSAL 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 165 DpIGIQS-MLDLMASKKEE-GRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL----RH 222
Cdd:PRK11308 186 D-VSVQAqVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIfnnpRH 248
|
|
| ABC_ABC_ChvD |
TIGR03719 |
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ... |
13-165 |
7.69e-09 |
|
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: 55.33 E-value: 7.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 13 GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSIS-GINIkedihayrqhlSYIPEAPVIYDALT 91
Cdd:TIGR03719 16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQpGIKV-----------GYLPQEPQLDPTKT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 92 LKEHIEM--------------TAMAYS---IDYDTAMARALPL------LKTFRLEDQLHI------FP------SHFSK 136
Cdd:TIGR03719 85 VRENVEEgvaeikdaldrfneISAKYAepdADFDKLAAEQAELqeiidaADAWDLDSQLEIamdalrCPpwdadvTKLSG 164
|
170 180 190
....*....|....*....|....*....|
gi 2095223075 137 GMKQKVMiICAFIVE-PDFYIIDEPFLGLD 165
Cdd:TIGR03719 165 GERRRVA-LCRLLLSkPDMLLLDEPTNHLD 193
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
20-212 |
1.08e-08 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 54.80 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELTDGEIVGLIGLNGAGKSTTIKhILGLLTPT---EGD-------MSISGINIKED-----IHayrQHLSYIPEap 84
Cdd:NF040905 19 DVNLSVREGEIHALCGENGAGKSTLMK-VLSGVYPHgsyEGEilfdgevCRFKDIRDSEAlgiviIH---QELALIPY-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 85 viydaLTLKEHIEM---TAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPF 161
Cdd:NF040905 93 -----LSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2095223075 162 LGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIV 212
Cdd:NF040905 168 AALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
|
|
| xylG |
TIGR02633 |
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ... |
4-213 |
1.43e-08 |
|
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: 54.45 E-value: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIK---NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPT-EGDMSISG--INIKEDIHAYRQHL 77
Cdd:TIGR02633 259 EARNLTCWDVINPHRKrvdDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKfEGNVFINGkpVDIRNPAQAIRAGI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPE---APVIYDALTLKEHIEMTAMAySIDYDTAMARALPLLKTFRLEDQLHIFPSH-------FSKGMKQKVMIICA 147
Cdd:TIGR02633 339 AMVPEdrkRHGIVPILGVGKNITLSVLK-SFCFKMRIDAAAELQIIGSAIQRLKVKTASpflpigrLSGGNQQKAVLAKM 417
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 148 FIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:TIGR02633 418 LLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKG 483
|
|
| ABCC_SUR2 |
cd03288 |
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ... |
3-231 |
1.47e-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: 53.76 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGK--KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSY 79
Cdd:cd03288 20 IKIHDLCVRYENnlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsKLPLHTLRSRLSI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 80 IPEAPVIYDAL--------------TLKEHIEMTAMaysidydTAMARALPllktFRLEDQLHIFPSHFSKGMKQKVMII 145
Cdd:cd03288 100 ILQDPILFSGSirfnldpeckctddRLWEALEIAQL-------KNMVKSLP----GGLDAVVTEGGENFSVGQRQLFCLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 146 CAFIVEPDFYIIDEPFLGLDpIGIQSMLDLMASKKEEGRTVLMSTHILATAERyCDRFIILDQGEIVAMGNLEALRHQTA 225
Cdd:cd03288 169 RAFVRKSSILIMDEATASID-MATENILQKVVMTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQED 246
|
....*.
gi 2095223075 226 MPHATL 231
Cdd:cd03288 247 GVFASL 252
|
|
| PRK15064 |
PRK15064 |
ABC transporter ATP-binding protein; Provisional |
7-165 |
2.24e-08 |
|
ABC transporter ATP-binding protein; Provisional
Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 54.13 E-value: 2.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 7 NLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSIS-GINI---KEDIHAYRQHlSYIPE 82
Cdd:PRK15064 6 NITMQFGAKPLFENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNVSLDpNERLgklRQDQFAFEEF-TVLDT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 83 apVI------YDALTLKEHI----EMT----------AMAYSiDYD--TAMARALPLLKTFRLEDQLHIFP-SHFSKGMK 139
Cdd:PRK15064 85 --VImghtelWEVKQERDRIyalpEMSeedgmkvadlEVKFA-EMDgyTAEARAGELLLGVGIPEEQHYGLmSEVAPGWK 161
|
170 180
....*....|....*....|....*.
gi 2095223075 140 QKVMIICAFIVEPDFYIIDEPFLGLD 165
Cdd:PRK15064 162 LRVLLAQALFSNPDILLLDEPTNNLD 187
|
|
| ugpC |
PRK11650 |
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC; |
2-63 |
3.14e-08 |
|
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 53.31 E-value: 3.14e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2095223075 2 TVQIKNLTGGY-GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG 63
Cdd:PRK11650 3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGG 65
|
|
| PRK13543 |
PRK13543 |
heme ABC exporter ATP-binding protein CcmA; |
8-191 |
3.26e-08 |
|
heme ABC exporter ATP-binding protein CcmA;
Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 52.54 E-value: 3.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 8 LTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGiniKEDIHAYR-QHLSYIPEAPVI 86
Cdd:PRK13543 17 LAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDG---KTATRGDRsRFMAYLGHLPGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 87 YDALTLKEHIEMTAMAYSIDYDTAMARALPLLKTFRLEDQLhifPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDP 166
Cdd:PRK13543 94 KADLSTLENLHFLCGLHGRRAKQMPGSALAIVGLAGYEDTL---VRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
|
170 180
....*....|....*....|....*
gi 2095223075 167 IGIQSMLDLMASKKEEGRTVLMSTH 191
Cdd:PRK13543 171 EGITLVNRMISAHLRGGGAALVTTH 195
|
|
| PLN03130 |
PLN03130 |
ABC transporter C family member; Provisional |
16-220 |
5.19e-08 |
|
ABC transporter C family member; Provisional
Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 53.20 E-value: 5.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 16 PIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI-KEDIHAYRQHLSYIPEAPVIYDAlTLKE 94
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDIsKFGLMDLRKVLGIIPQAPVLFSG-TVRF 1331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 95 HIEMTAMAYSIDYDTAMARAlpLLK------TFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDpIG 168
Cdd:PLN03130 1332 NLDPFNEHNDADLWESLERA--HLKdvirrnSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVD-VR 1408
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 169 ----IQSMLdlmaskKEEGR--TVLMSTHILATAERyCDRFIILDQGEIVAMGNLEAL 220
Cdd:PLN03130 1409 tdalIQKTI------REEFKscTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENL 1459
|
|
| MK0520 |
COG2401 |
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ... |
7-191 |
6.07e-08 |
|
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];
Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 51.50 E-value: 6.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 7 NLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLL--TPTEGDMSISGINIKEdihayrqhlsyipEAP 84
Cdd:COG2401 35 GVELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALkgTPVAGCVDVPDNQFGR-------------EAS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 85 VIyDALTLKEhiemtamaysiDYDTAMAralpLLKTFRLEDQLHIF--PSHFSKGMKQKVMIICAFIVEPDFYIIDEPFL 162
Cdd:COG2401 102 LI-DAIGRKG-----------DFKDAVE----LLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCS 165
|
170 180 190
....*....|....*....|....*....|...
gi 2095223075 163 GLDP----IGIQSMLDLMaskKEEGRTVLMSTH 191
Cdd:COG2401 166 HLDRqtakRVARNLQKLA---RRAGITLVVATH 195
|
|
| PTZ00265 |
PTZ00265 |
multidrug resistance protein (mdr1); Provisional |
3-210 |
6.28e-08 |
|
multidrug resistance protein (mdr1); Provisional
Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 53.11 E-value: 6.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKP---IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHA--YRQHL 77
Cdd:PTZ00265 383 IQFKNVRFHYDTRKdveIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLKDINLkwWRSKI 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 78 SYIPEAPVI----------YDALTLK--EHIE---------------------------MTAMAYSIDYDTAM------- 111
Cdd:PTZ00265 463 GVVSQDPLLfsnsiknnikYSLYSLKdlEALSnyynedgndsqenknkrnscrakcagdLNDMSNTTDSNELIemrknyq 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 112 ----ARALPLLKTFRLEDQLHIFP-----------SHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG---IQSML 173
Cdd:PTZ00265 543 tikdSEVVDVSKKVLIHDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSeylVQKTI 622
|
250 260 270
....*....|....*....|....*....|....*..
gi 2095223075 174 DLMasKKEEGRTVLMSTHILATAeRYCDRFIILDQGE 210
Cdd:PTZ00265 623 NNL--KGNENRITIIIAHRLSTI-RYANTIFVLSNRE 656
|
|
| PRK10762 |
PRK10762 |
D-ribose transporter ATP binding protein; Provisional |
28-213 |
1.05e-07 |
|
D-ribose transporter ATP binding protein; Provisional
Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 51.93 E-value: 1.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 28 GEIVGLIGLNGAGKSTTIKHILGLLTPTEG---------------DMSISGINIkedIHayrQHLSYIPEapviydaLTL 92
Cdd:PRK10762 30 GRVMALVGENGAGKSTMMKVLTGIYTRDAGsilylgkevtfngpkSSQEAGIGI---IH---QELNLIPQ-------LTI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 93 KEHI----EMTAMAYSIDYDTAMARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG 168
Cdd:PRK10762 97 AENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2095223075 169 IQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVA 213
Cdd:PRK10762 177 TESLFRVIRELKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIA 221
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-160 |
1.10e-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: 52.09 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 28 GEIVGLIGLNGAGKSTTIKHILGLLTPTEGDmsisgINIKEDIhayrqhlSYIPEapviYdaltLKEHIEMTAMAY---- 103
Cdd:COG1245 366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGE-----VDEDLKI-------SYKPQ----Y----ISPDYDGTVEEFlrsa 425
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 104 -SIDYDTAMARALpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:COG1245 426 nTDDFGSSYYKTE-IIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEP 482
|
|
| ABCG_PDR_domain2 |
cd03232 |
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ... |
2-209 |
2.58e-07 |
|
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.
Pssm-ID: 213199 [Multi-domain] Cd Length: 192 Bit Score: 49.55 E-value: 2.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNltggyGKKPIIKNINFELTDGEIVGLIGLNGAGKSTtikhILGLLTP------TEGDMSISGINIKEDihaYRQ 75
Cdd:cd03232 12 TVPVKG-----GKRQLLNNISGYVKPGTLTALMGESGAGKTT----LLDVLAGrktagvITGEILINGRPLDKN---FQR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 76 HLSYIPEAPVIYDALTLKEHIEMTAmaysidydtamaralpLLKTFRLEDqlhifpshfskgmKQKVMIICAFIVEPDFY 155
Cdd:cd03232 80 STGYVEQQDVHSPNLTVREALRFSA----------------LLRGLSVEQ-------------RKRLTIGVELAAKPSIL 130
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2095223075 156 IIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTH-----ILAtaerYCDRFIILDQG 209
Cdd:cd03232 131 FLDEPTSGLDSQAAYNIVRFLKKLADSGQAILCTIHqpsasIFE----KFDRLLLLKRG 185
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
3-188 |
2.69e-07 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.78 E-value: 2.69e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 3 VQIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTtikhILGLLTpteGDMSISGINikeDIHAY-RQHLSyip 81
Cdd:PRK10938 261 IVLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKST----LLSLIT---GDHPQGYSN---DLTLFgRRRGS--- 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 82 eAPVIYDaltLKEHIEMTAMAYSIDY-------------------------DTAMARALPLLKTFRLEDQLHIFPSH-FS 135
Cdd:PRK10938 328 -GETIWD---IKKHIGYVSSSLHLDYrvstsvrnvilsgffdsigiyqavsDRQQKLAQQWLDILGIDKRTADAPFHsLS 403
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 136 KGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIG---IQSMLDLMASkkeEGRTVLM 188
Cdd:PRK10938 404 WGQQRLALIVRALVKHPTLLILDEPLQGLDPLNrqlVRRFVDVLIS---EGETQLL 456
|
|
| ycf16 |
CHL00131 |
sulfate ABC transporter protein; Validated |
4-77 |
3.09e-07 |
|
sulfate ABC transporter protein; Validated
Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 50.03 E-value: 3.09e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILG--LLTPTEGDMSISGINIKEDIHAYRQHL 77
Cdd:CHL00131 9 EIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEERAHL 84
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
1-216 |
3.19e-07 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 50.50 E-value: 3.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 1 MTVQIKNLTGGygKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAYRQHLS 78
Cdd:PRK10982 249 VILEVRNLTSL--RQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGkkINNHNANEAINHGFA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 79 YIPE---APVIYDALTlkehIEMTAMAYSID-YDTAMAralpLLKTFRLE-------DQLHI-FPSH------FSKGMKQ 140
Cdd:PRK10982 327 LVTEerrSTGIYAYLD----IGFNSLISNIRnYKNKVG----LLDNSRMKsdtqwviDSMRVkTPGHrtqigsLSGGNQQ 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 141 KVMIICAFIVEPDFYIIDEPFLGLDpIGI-----QSMLDLmaSKKEEGrtVLMSTHILATAERYCDRFIILDQGEIVAMG 215
Cdd:PRK10982 399 KVIIGRWLLTQPEILMLDEPTRGID-VGAkfeiyQLIAEL--AKKDKG--IIIISSEMPELLGITDRILVMSNGLVAGIV 473
|
.
gi 2095223075 216 N 216
Cdd:PRK10982 474 D 474
|
|
| PRK11819 |
PRK11819 |
putative ABC transporter ATP-binding protein; Reviewed |
13-98 |
3.40e-07 |
|
putative ABC transporter ATP-binding protein; Reviewed
Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 50.50 E-value: 3.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 13 GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSIS-GINIkedihayrqhlSYIPEAPVIYDALT 91
Cdd:PRK11819 18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPApGIKV-----------GYLPQEPQLDPEKT 86
|
....*..
gi 2095223075 92 LKEHIEM 98
Cdd:PRK11819 87 VRENVEE 93
|
|
| PRK13541 |
PRK13541 |
cytochrome c biogenesis protein CcmA; Provisional |
20-191 |
3.85e-07 |
|
cytochrome c biogenesis protein CcmA; Provisional
Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 49.10 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAYrqhLSYIPEAPVIYDALTLKEHIEMT 99
Cdd:PRK13541 18 DLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY---CTYIGHNLGLKLEMTVFENLKFW 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 100 AMAYsiDYDTAMARAlplLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASK 179
Cdd:PRK13541 95 SEIY--NSAETLYAA---IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLIVMK 169
|
170
....*....|..
gi 2095223075 180 KEEGRTVLMSTH 191
Cdd:PRK13541 170 ANSGGIVLLSSH 181
|
|
| PRK13549 |
PRK13549 |
xylose transporter ATP-binding subunit; Provisional |
17-211 |
1.07e-06 |
|
xylose transporter ATP-binding subunit; Provisional
Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 48.77 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLT-PTEGDMSISG--INIKEDIHAYRQHLSYIPE-------APVI 86
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGkpVKIRNPQQAIAQGIAMVPEdrkrdgiVPVM 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 87 ----------YDALTLKEHIEMTAMAYSIDydTAMAR-----ALPLLKTFRLedqlhifpshfSKGMKQKVMIICAFIVE 151
Cdd:PRK13549 357 gvgknitlaaLDRFTGGSRIDDAAELKTIL--ESIQRlkvktASPELAIARL-----------SGGNQQKAVLAKCLLLN 423
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 152 PDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEI 211
Cdd:PRK13549 424 PKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
|
|
| ABCD_peroxisomal_ALDP |
cd03223 |
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ... |
15-191 |
1.12e-06 |
|
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).
Pssm-ID: 213190 [Multi-domain] Cd Length: 166 Bit Score: 47.15 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 15 KPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMsisginikeDIHAYRQHLsYIPEAPVIYDAlTLKE 94
Cdd:cd03223 14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI---------GMPEGEDLL-FLPQRPYLPLG-TLRE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 95 HIemtamaysidydtamarALPLLKTfrledqlhifpshFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLD 174
Cdd:cd03223 83 QL-----------------IYPWDDV-------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQ 132
|
170
....*....|....*..
gi 2095223075 175 LMaskKEEGRTVLMSTH 191
Cdd:cd03223 133 LL---KELGITVISVGH 146
|
|
| ABC_RNaseL_inhibitor |
cd03222 |
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ... |
24-66 |
2.19e-06 |
|
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.
Pssm-ID: 213189 [Multi-domain] Cd Length: 177 Bit Score: 46.80 E-value: 2.19e-06
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095223075 24 ELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINI 66
Cdd:cd03222 21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP 63
|
|
| COG4938 |
COG4938 |
Predicted ATPase [General function prediction only]; |
2-191 |
3.25e-06 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443965 [Multi-domain] Cd Length: 277 Bit Score: 46.89 E-value: 3.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 2 TVQIKNLtggygkKPIiKNINFELTDGEIvgLIGLNGAGKSTTIKHILGLLT------PTE--GDMSISGINIkedihay 73
Cdd:COG4938 3 SISIKNF------GPF-KEAELELKPLTL--LIGPNGSGKSTLIQALLLLLQsnfiylPAErsGPARLYPSLV------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 74 RQHLSYIPEAPVIYDALTLKEHIEMTAMAYSI---DYDTAMARALPL---LKTFRLEDQLHIFPSHFSK---------GM 138
Cdd:COG4938 67 RELSDLGSRGEYTADFLAELENLEILDDKSKElleQVEEWLEKIFPGkveVDASSDLVRLVFRPSGNGKriplsnvgsGV 146
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 139 KQKVMII--CAFIVEPDFY-IIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTH 191
Cdd:COG4938 147 SELLPILlaLLSAAKPGSLlIIEEPEAHLHPKAQSALAELLAELANSGVQVIIETH 202
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
4-57 |
5.53e-06 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 46.87 E-value: 5.53e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEG 57
Cdd:PRK11147 321 EMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSG 374
|
|
| sufC |
PRK09580 |
cysteine desulfurase ATPase component; Reviewed |
5-216 |
6.81e-06 |
|
cysteine desulfurase ATPase component; Reviewed
Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 45.94 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 5 IKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGL--LTPTEGDMSISGINIKEDIHAYRQ------H 76
Cdd:PRK09580 4 IKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAgegifmA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 LSYIPEAPVIYDALTLKehiemTAMAYSIDYdtamaRALPLLKTFRLED------QLHIFPSH---------FSKGMKQK 141
Cdd:PRK09580 84 FQYPVEIPGVSNQFFLQ-----TALNAVRSY-----RGQEPLDRFDFQDlmeekiALLKMPEDlltrsvnvgFSGGEKKR 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 142 VMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFI-ILDQGEIVAMGN 216
Cdd:PRK09580 154 NDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTHYQRILDYIKPDYVhVLYQGRIVKSGD 229
|
|
| Rli1 |
COG1245 |
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ... |
28-195 |
1.24e-05 |
|
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: 45.93 E-value: 1.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 28 GEIVGLIGLNGAGKSTTIKhIL-GLLTPTEGDMSiSGINIKEDIHAYR----------------------QHLSYIPEA- 83
Cdd:COG1245 99 GKVTGILGPNGIGKSTALK-ILsGELKPNLGDYD-EEPSWDEVLKRFRgtelqdyfkklangeikvahkpQYVDLIPKVf 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 84 -PVIYDALT-------LKEHIEMTAMAYSIDYDTamaralpllktfrledqlhifpSHFSKGMKQKVMIICAFIVEPDFY 155
Cdd:COG1245 177 kGTVRELLEkvdergkLDELAEKLGLENILDRDI----------------------SELSGGELQRVAIAAALLRDADFY 234
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2095223075 156 IIDEPFLGLDpIG--------IQSMLdlmaskkEEGRTVLMSTHILAT 195
Cdd:COG1245 235 FFDEPSSYLD-IYqrlnvarlIRELA-------EEGKYVLVVEHDLAI 274
|
|
| ABCC_SUR1_N |
cd03290 |
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ... |
6-193 |
1.56e-05 |
|
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: 44.63 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 6 KNLTGGY----GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGINIKEDIHAY-----RQH 76
Cdd:cd03290 1 VQVTNGYfswgSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEAtrsrnRYS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 77 LSYIPEAPVIYDAlTLKEHIEMTAMAYSIDYDTAM-ARAL-PLLKTFRLEDQLHIFPS--HFSKGMKQKVMIICAFIVEP 152
Cdd:cd03290 81 VAYAAQKPWLLNA-TVEENITFGSPFNKQRYKAVTdACSLqPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNT 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2095223075 153 DFYIIDEPFLGLDpIGIQSML---DLMASKKEEGRTVLMSTHIL 193
Cdd:cd03290 160 NIVFLDDPFSALD-IHLSDHLmqeGILKFLQDDKRTLVLVTHKL 202
|
|
| PLN03211 |
PLN03211 |
ABC transporter G-25; Provisional |
4-191 |
1.69e-05 |
|
ABC transporter G-25; Provisional
Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 45.26 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLTGGYGKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTegdmSISGINIKEDIHAYRQHL---SYI 80
Cdd:PLN03211 70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGN----NFTGTILANNRKPTKQILkrtGFV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 81 PEAPVIYDALTLKEHIEMTAM-----AYSIDYDTAMARA-LPLLKTFRLEDQL--HIFPSHFSKGMKQKVMIICAFIVEP 152
Cdd:PLN03211 146 TQDDILYPHLTVRETLVFCSLlrlpkSLTKQEKILVAESvISELGLTKCENTIigNSFIRGISGGERKRVSIAHEMLINP 225
|
170 180 190
....*....|....*....|....*....|....*....
gi 2095223075 153 DFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTH 191
Cdd:PLN03211 226 SLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
|
|
| PRK10938 |
PRK10938 |
putative molybdenum transport ATP-binding protein ModF; Provisional |
112-188 |
1.84e-05 |
|
putative molybdenum transport ATP-binding protein ModF; Provisional
Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 45.01 E-value: 1.84e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 112 ARALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLM 188
Cdd:PRK10938 114 ARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGITLVL 190
|
|
| hmuV |
PRK13547 |
heme ABC transporter ATP-binding protein; |
17-215 |
2.53e-05 |
|
heme ABC transporter ATP-binding protein;
Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 44.43 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTpteGDMSISGINIKEDIHAYRQHLSYIPeAPVIYDALTLKEHI 96
Cdd:PRK13547 16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLT---GGGAPRGARVTGDVTLNGEPLAAID-APRLARLRAVLPQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 97 EMTAMAYSID------------------------YDTAMARA-----------------LPLLKTFRLEDQLHifPSHFS 135
Cdd:PRK13547 92 AQPAFAFSAReivllgrypharragalthrdgeiAWQALALAgatalvgrdvttlsggeLARVQFARVLAQLW--PPHDA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 136 kgmkqkvmiicafIVEPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRT-VLMSTHILATAERYCDRFIILDQGEIVAM 214
Cdd:PRK13547 170 -------------AQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAH 236
|
.
gi 2095223075 215 G 215
Cdd:PRK13547 237 G 237
|
|
| ABC_RNaseL_inhibitor_domain1 |
cd03236 |
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ... |
27-194 |
2.63e-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: 44.28 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 27 DGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGiNIKEDIHAYR----------------------QHLSYIPEAp 84
Cdd:cd03236 25 EGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPP-DWDEILDEFRgselqnyftkllegdvkvivkpQYVDLIPKA- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 85 VIYDALTLKEHIEMTAMaysIDYdtamaralpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGL 164
Cdd:cd03236 103 VKGKVGELLKKKDERGK---LDE---------LVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170
|
170 180 190
....*....|....*....|....*....|
gi 2095223075 165 DPIGIQSMLDLMASKKEEGRTVLMSTHILA 194
Cdd:cd03236 171 DIKQRLNAARLIRELAEDDNYVLVVEHDLA 200
|
|
| PRK13409 |
PRK13409 |
ribosome biogenesis/translation initiation ATPase RLI; |
25-160 |
5.34e-05 |
|
ribosome biogenesis/translation initiation ATPase RLI;
Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 44.03 E-value: 5.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 25 LTDGEIVGLIGLNGAGKSTTIKhIL-GLLTPTEGDMSiSGINIKEDIHAYR--------QHLS-----------YIPEAP 84
Cdd:PRK13409 96 PKEGKVTGILGPNGIGKTTAVK-ILsGELIPNLGDYE-EEPSWDEVLKRFRgtelqnyfKKLYngeikvvhkpqYVDLIP 173
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 85 VIYDAlTLKEHIEMTAMAYSIDYdtamaralpLLKTFRLEDQLHIFPSHFSKGMKQKVMIICAFIVEPDFYIIDEP 160
Cdd:PRK13409 174 KVFKG-KVRELLKKVDERGKLDE---------VVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
|
|
| PTZ00243 |
PTZ00243 |
ABC transporter; Provisional |
17-215 |
6.67e-05 |
|
ABC transporter; Provisional
Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.61 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGinikEDIHAY-----RQHLSYIPEAPVIYDAlT 91
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNG----REIGAYglrelRRQFSMIPQDPVLFDG-T 1399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 92 LKEHIEMTAMAYSIDydtaMARALPLL--------KTFRLEDQLHIFPSHFSKGMKQkVMIICAFIVEPD--FYIIDEPF 161
Cdd:PTZ00243 1400 VRQNVDPFLEASSAE----VWAALELVglrervasESEGIDSRVLEGGSNYSVGQRQ-LMCMARALLKKGsgFILMDEAT 1474
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 162 LGLDPI---GIQSMLDLMASkkeeGRTVLMSTHILATAERYcDRFIILDQGEIVAMG 215
Cdd:PTZ00243 1475 ANIDPAldrQIQATVMSAFS----AYTVITIAHRLHTVAQY-DKIIVMDHGAVAEMG 1526
|
|
| AAA_21 |
pfam13304 |
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ... |
131-191 |
9.87e-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: 42.76 E-value: 9.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2095223075 131 PSHFSKGMKQkvmiICAFIV-------EPDFYIIDEPFLGLDPIGIQSMLDLMASKKEEGRTVLMSTH 191
Cdd:pfam13304 234 AFELSDGTKR----LLALLAallsalpKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTH 297
|
|
| AAA |
smart00382 |
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ... |
28-147 |
1.05e-04 |
|
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.
Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 41.20 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 28 GEIVGLIGLNGAGKSTTIKHILGLLTPTEGDM-SISGINIKEDIHAYRQHLSYIPEAPVIYDALTLKEHIEMtAMAYSID 106
Cdd:smart00382 2 GEVILIVGPPGSGKTTLARALARELGPPGGGViYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALAL-ARKLKPD 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2095223075 107 Y---DTAMarALPLLKTFRLEDQLHIFPSHFSKGMKQKVMIICA 147
Cdd:smart00382 81 VlilDEIT--SLLDAEQEALLLLLEELRLLLLLKSEKNLTVILT 122
|
|
| PRK11147 |
PRK11147 |
ABC transporter ATPase component; Reviewed |
7-46 |
3.39e-04 |
|
ABC transporter ATPase component; Reviewed
Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 41.47 E-value: 3.39e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2095223075 7 NLTGGY---GKKPIIKNINFELTDGEIVGLIGLNGAGKSTTIK 46
Cdd:PRK11147 5 SIHGAWlsfSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK 47
|
|
| PLN03073 |
PLN03073 |
ABC transporter F family; Provisional |
11-76 |
1.14e-03 |
|
ABC transporter F family; Provisional
Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 39.84 E-value: 1.14e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2095223075 11 GYGKKPII-KNINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISGiniKEDIHAYRQH 76
Cdd:PLN03073 517 GYPGGPLLfKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSA---KVRMAVFSQH 580
|
|
| 3a01205 |
TIGR00956 |
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other] |
14-100 |
2.17e-03 |
|
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 38.94 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 14 KKPIIKNINFELTDGEIVGLIGLNGAGKSTTIKHIL----GLLTPTEGDMSISGINIKEDIHAYRQHLSYIPEAPVIYDA 89
Cdd:TIGR00956 73 TFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPH 152
|
90
....*....|.
gi 2095223075 90 LTLKEHIEMTA 100
Cdd:TIGR00956 153 LTVGETLDFAA 163
|
|
| PLN03140 |
PLN03140 |
ABC transporter G family member; Provisional |
28-191 |
2.19e-03 |
|
ABC transporter G family member; Provisional
Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 39.06 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 28 GEIVGLIGLNGAGKSTTIKHILGLLTP--TEGDMSISGINIKED----IHAY-RQHLSYIPEAPV----IYDALtLKEHI 96
Cdd:PLN03140 906 GVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQEtfarISGYcEQNDIHSPQVTVreslIYSAF-LRLPK 984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 97 EMTAMAYSIDYDTAMAralpLLKTFRLEDQLHIFP--SHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGLDPIGIQSMLD 174
Cdd:PLN03140 985 EVSKEEKMMFVDEVME----LVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMR 1060
|
170
....*....|....*..
gi 2095223075 175 LMASKKEEGRTVLMSTH 191
Cdd:PLN03140 1061 TVRNTVDTGRTVVCTIH 1077
|
|
| PRK10982 |
PRK10982 |
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional |
20-220 |
2.85e-03 |
|
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 38.56 E-value: 2.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 20 NINFELTDGEIVGLIGLNGAGKSTTIKHILGLLTPTEGDMSISG--INIKEDIHAY-------RQHLSYIPEAPVIyDAL 90
Cdd:PRK10982 16 NVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGkeIDFKSSKEALengismvHQELNLVLQRSVM-DNM 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 91 TLKEHiemTAMAYSIDYDTaMARalpllKTFRLEDQLHI------FPSHFSKGMKQKVMIICAFIVEPDFYIIDEPFLGL 164
Cdd:PRK10982 95 WLGRY---PTKGMFVDQDK-MYR-----DTKAIFDELDIdidpraKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL 165
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2095223075 165 DPIGIQSMLDLMASKKEEGRTVLMSTHILATAERYCDRFIILDQGEIVAMGNLEAL 220
Cdd:PRK10982 166 TEKEVNHLFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGL 221
|
|
| ABC_UvrA |
cd03238 |
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ... |
18-215 |
5.18e-03 |
|
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: 36.53 E-value: 5.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 18 IKNINFELTDGEIVGLIGLNGAGKSTTIKHILGlltptegdmsisginiKEDIHAYRQHLSYIPEAPVIY-DALTLkehi 96
Cdd:cd03238 11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLY----------------ASGKARLISFLPKFSRNKLIFiDQLQF---- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 97 eMTAMAysIDYDTaMARALPLLktfrledqlhifpshfSKGMKQKVMIICAFIVEPD--FYIIDEPFLGLDPIGIQSMLD 174
Cdd:cd03238 71 -LIDVG--LGYLT-LGQKLSTL----------------SGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLE 130
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2095223075 175 LMASKKEEGRTVLMSTHILATAErYCDRFIIL------DQGEIVAMG 215
Cdd:cd03238 131 VIKGLIDLGNTVILIEHNLDVLS-SADWIIDFgpgsgkSGGKVVFSG 176
|
|
| GguA |
NF040905 |
sugar ABC transporter ATP-binding protein; |
17-213 |
7.29e-03 |
|
sugar ABC transporter ATP-binding protein;
Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 37.08 E-value: 7.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 17 IIKNINFELTDGEIVGLIGLNGAGKsttikhilglltpTEGDMSISGinikediHAYRQHLS---YIPEAPViyDALTLK 93
Cdd:NF040905 275 VVDDVSLNVRRGEIVGIAGLMGAGR-------------TELAMSVFG-------RSYGRNISgtvFKDGKEV--DVSTVS 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 94 EHIEmTAMAY--------------SIDYDTAMArALPLLKTFRLEDQ-------------LHI-FPSHF------SKGMK 139
Cdd:NF040905 333 DAID-AGLAYvtedrkgyglnlidDIKRNITLA-NLGKVSRRGVIDEneeikvaeeyrkkMNIkTPSVFqkvgnlSGGNQ 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2095223075 140 QKVMIICAFIVEPDFYIIDEPFLGLDpIG----IQSMLDLMAskkEEGRTVLM-ST---HILATaeryCDRFIILDQGEI 211
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGID-VGakyeIYTIINELA---AEGKGVIViSSelpELLGM----CDRIYVMNEGRI 482
|
..
gi 2095223075 212 VA 213
Cdd:NF040905 483 TG 484
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
4-52 |
9.69e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 37.05 E-value: 9.69e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 2095223075 4 QIKNLT-GGYGKkpiIKNINFELTDGEIVgLIGLNGAGKSTTIKHILGLL 52
Cdd:COG4717 2 KIKELEiYGFGK---FRDRTIEFSPGLNV-IYGPNEAGKSTLLAFIRAML 47
|
|
| |
